|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
438-923 |
0e+00 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 1010.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 438 TVKIPYQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLM 517
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 518 EENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYNLTFTKKEPLGACAIIIPWNYP 597
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 598 LMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGK 677
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 678 QIMKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKI 757
Cdd:cd07140 241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 758 GDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQ 837
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 838 NGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIK 917
Cdd:cd07140 401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
....*.
gi 283436218 918 TVTLEY 923
Cdd:cd07140 481 TVTIEY 486
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
441-920 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 755.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 441 IPYQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLMEEN 520
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 521 QEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarpNYNLTFTKKEPLGACAIIIPWNYPLMM 600
Cdd:cd07091 82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPID----GNFLAYTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 601 LAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIM 680
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 681 KSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDP 760
Cdd:cd07091 238 EAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 761 LDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngD 840
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK--T 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 841 IDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
438-921 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 616.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 438 TVKIPY-QCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENG-EWGRMNARDRGRLMYRLAD 515
Cdd:cd07141 1 NPEIKYtKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 516 LMEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQarpNYnLTFTKKEPLGACAIIIPWN 595
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDG---DF-FTYTRHEPVGVCGQIIPWN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 596 YPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSV 675
Cdd:cd07141 157 FPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 676 GKQIMKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKM 755
Cdd:cd07141 237 GKLIQQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 756 KIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISK 835
Cdd:cd07141 317 VVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 836 FQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLK 915
Cdd:cd07141 397 FK--TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTE 474
|
....*.
gi 283436218 916 IKTVTL 921
Cdd:cd07141 475 VKTVTI 480
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
437-923 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 610.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 437 MTVKiPYQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFenGEWGRMNARDRGRLMYRLADL 516
Cdd:COG1012 1 MTTP-EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 517 MEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPInqARPNYnLTFTKKEPLGACAIIIPWNY 596
Cdd:COG1012 78 LEERREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 597 PLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVG 676
Cdd:COG1012 154 PLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 677 KQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMK 756
Cdd:COG1012 234 RRIAAAAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 757 IGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQR-PGFFMEPTVFTGVEDHMYLAKEESFGPIMVISK 835
Cdd:COG1012 313 VGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 836 FQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVA-APFGGMKQSGFGKDLGEEALNEYL 914
Cdd:COG1012 393 FD--DEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYT 470
|
....*....
gi 283436218 915 KIKTVTLEY 923
Cdd:COG1012 471 ETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
451-919 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 609.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 451 FVDAeDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEAL 530
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 531 DSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPInqarPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLA 610
Cdd:pfam00171 78 ENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPS----DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 611 AGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKK 690
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 691 VSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQ 770
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 771 NHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANN 850
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAND 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 851 TEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDV-AAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
492-921 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 559.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 492 AFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTlALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqa 571
Cdd:cd07078 10 AFK--AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIPSP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 572 rPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSG 651
Cdd:cd07078 85 -DPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 652 GVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAA 731
Cdd:cd07078 164 DEVGAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 732 GRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGG-RQVQRPGFFMEPT 810
Cdd:cd07078 243 SRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGkRLEGGKGYFVPPT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 811 VFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNK-TDV 889
Cdd:cd07078 323 VLTDVDPDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEP 400
|
410 420 430
....*....|....*....|....*....|..
gi 283436218 890 AAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07078 401 SAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
436-919 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 556.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 436 GMTVKIPYQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgEWGRMNARDRGRLMYRLAD 515
Cdd:cd07144 1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 516 LMEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARpnynLTFTKKEPLGACAIIIPWN 595
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNK----LAYTLHEPYGVCGQIIPWN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 596 YPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSV 675
Cdd:cd07144 156 YPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 676 GKQIMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKK- 754
Cdd:cd07144 236 GRLVMKA-AAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQn 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 755 MKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGG---RQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIM 831
Cdd:cd07144 315 YKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 832 VISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALN 911
Cdd:cd07144 395 VISKFK--TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLE 472
|
....*...
gi 283436218 912 EYLKIKTV 919
Cdd:cd07144 473 TYTQTKAV 480
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
462-921 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 553.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTlALK 541
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 THIGMSVQTFRYFAGWCDKIQGSTIPINqaRPNYnLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAVIPVD--KGDY-LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPL 701
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 702 IIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLAS 857
Cdd:cd07114 316 YVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFD--DEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 858 GVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
457-919 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 542.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 457 GETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVY 536
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 537 TLALKTHIGMSVQTFRYFAGWCDKIQGSTIPInqarPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLV 616
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPT----GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 617 LKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVSNLKKVSLELG 696
Cdd:cd07112 157 LKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 697 GKSPLIIFSDC-DLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAH 775
Cdd:cd07112 237 GKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 776 LEKLLQYCETGVQEGATLVYGGRQVQR--PGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqnGDIDGVLQRANNTEY 853
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITF--DSEEEAVALANDSVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 283436218 854 GLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
442-919 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 538.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 442 PYQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLMEENQ 521
Cdd:cd07142 3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 522 EELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYNLtftkKEPLGACAIIIPWNYPLMML 601
Cdd:cd07142 83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTL----HEPIGVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMK 681
Cdd:cd07142 159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 682 SCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPL 761
Cdd:cd07142 239 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 762 DRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDI 841
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK--TV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 283436218 842 DGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
462-919 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 537.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALK 541
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 THIGMSVQTFRYFAGWCDKIQGSTIPInqaRPNYnLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPV---RGPF-LNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVsNLKKVSLELGGKSPL 701
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAG-NLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 702 IIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqnGDIDGVLQRANNTEYGLASGVFT 861
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 283436218 862 RDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:cd07115 392 RDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
438-919 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 536.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 438 TVKIPYQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgEWGR-MNARDRGRLMYRLADL 516
Cdd:cd07143 2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFET-DWGLkVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 517 MEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARpnynLTFTKKEPLGACAIIIPWNY 596
Cdd:cd07143 81 MERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKK----LTYTRHEPIGVCGQIIPWNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 597 PLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVG 676
Cdd:cd07143 157 PLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 677 KQIMKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMK 756
Cdd:cd07143 237 RKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 757 IGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKF 836
Cdd:cd07143 317 VGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 837 QngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKI 916
Cdd:cd07143 397 K--TEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQI 474
|
...
gi 283436218 917 KTV 919
Cdd:cd07143 475 KAV 477
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
446-919 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 533.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinqaRPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKS 605
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYD----VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 606 AACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAv 685
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 SNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07119 235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 766 DHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDI 841
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFD--TE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 283436218 842 DGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
431-919 |
4.72e-180 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 529.78 E-value: 4.72e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 431 SKEVNGMTVKIP----YQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDR 506
Cdd:PLN02766 5 GNCGGASGVKVPeikfTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 507 GRLMYRLADLMEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYNLtftkKEPLG 586
Cdd:PLN02766 85 GRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTL----KEPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 587 ACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRK 666
Cdd:PLN02766 161 VVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 667 LGFTGSTSVGKQIMKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVT 746
Cdd:PLN02766 241 VSFTGSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 747 RVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEES 826
Cdd:PLN02766 321 KLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 827 FGPIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLG 906
Cdd:PLN02766 401 FGPVMSLMKFKT--VEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQG 478
|
490
....*....|...
gi 283436218 907 EEALNEYLKIKTV 919
Cdd:PLN02766 479 MDALDKYLQVKSV 491
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
463-921 |
4.63e-173 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 510.05 E-value: 4.63e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWCDKIQGSTIPinqARPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIP---SPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 623 TPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLI 702
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 703 IFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQY 782
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 783 CETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTR 862
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFD--TEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 283436218 863 DINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
462-922 |
5.83e-172 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 507.23 E-value: 5.83e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlK 541
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 THIGMSVQTFRYFAGWCDKIQGSTIPInqarPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPL----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELTVKAGFPKGVINIIPGsGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPL 701
Cdd:cd07090 154 FTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 702 IIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRQVQ-----RPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQNgdIDGVLQRANNTEYGLA 856
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDT--EEEVIRRANDTTYGLA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 283436218 857 SGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTLE 922
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
462-921 |
6.35e-171 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 504.41 E-value: 6.35e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALK 541
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 THIGMSVQTFRYFAGWCDKIQGSTIPinqARPNYnLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYP---QDGGA-LNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPL 701
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRA-AAPNLKPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 702 IIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLAS 857
Cdd:cd07093 314 YVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFD--DEEEAIELANDTPYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 858 GVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07093 392 YVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
443-922 |
8.91e-167 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 495.17 E-value: 8.91e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQE 522
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQArpnyNLTFTKKEPLGACAIIIPWNYPLMMLA 602
Cdd:PRK13252 85 ELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGG----SFVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVaGQRLSQHPDIRKLGFTGSTSVGKQIMKS 682
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 683 CAVSnLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLD 762
Cdd:PRK13252 240 AAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 763 RSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQR----PGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQn 838
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFD- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 839 gDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKT 918
Cdd:PRK13252 398 -DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
....
gi 283436218 919 VTLE 922
Cdd:PRK13252 477 VQVE 480
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
438-919 |
3.04e-166 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 495.87 E-value: 3.04e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 438 TVKIPY-QCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADL 516
Cdd:PLN02466 52 PVQVSYtQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 517 MEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPinqARPNYNLTfTKKEPLGACAIIIPWNY 596
Cdd:PLN02466 132 LEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVP---ADGPHHVQ-TLHEPIGVAGQIIPWNF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 597 PLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVG 676
Cdd:PLN02466 208 PLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 677 KQIMKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMK 756
Cdd:PLN02466 288 KIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 757 IGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKF 836
Cdd:PLN02466 368 VGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 837 QngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKI 916
Cdd:PLN02466 448 K--DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQV 525
|
...
gi 283436218 917 KTV 919
Cdd:PLN02466 526 KAV 528
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
446-917 |
6.40e-161 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 479.31 E-value: 6.40e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFenGEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPInqarPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKS 605
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 606 AACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScAV 685
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAA-AA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 SNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 766 DHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDI 841
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFS--DE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 283436218 842 DGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIK 917
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
463-921 |
2.54e-151 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 454.00 E-value: 2.54e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFENGeWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWCDKIQGSTIPINqarPNYnLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLG---PGY-FVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 623 TPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLI 702
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 703 IFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRsTDHGPQNHRAHLEKLLQY 782
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 783 CETGVQEGATLVYGGRQVQRP---GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqnGDIDGVLQRANNTEYGLASGV 859
Cdd:cd07109 314 VARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436218 860 FTRDINKAMYVSDKLEAGTVFINTYNKT-DVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
463-920 |
1.53e-150 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 451.78 E-value: 1.53e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALKT 542
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWCDKIQGSTIpiNQARPNYnLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAA--GEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 623 TPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPLI 702
Cdd:cd07092 157 TPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 703 IFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQY 782
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 783 CEtGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTR 862
Cdd:cd07092 315 VE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 283436218 863 DINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVM 449
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
443-923 |
1.94e-150 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 452.95 E-value: 1.94e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQE 522
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYNLtftkKEPLGACAIIIPWNYPLMMLA 602
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHF----HEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKS 682
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 683 cAVSNLKKVSLELGGKSPLIIFSD-----CDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKI 757
Cdd:cd07559 234 -AAENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 758 GDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVI 833
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 834 SKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEY 913
Cdd:cd07559 393 ITFK--DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
490
....*....|
gi 283436218 914 LKIKTVTLEY 923
Cdd:cd07559 471 QQTKNILVSY 480
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
492-921 |
2.57e-149 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 449.10 E-value: 2.57e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 492 AFENGEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTipinqa 571
Cdd:cd07118 31 AFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEIEGAADLWRYAASLARTLHGDS------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 572 rpnYN------LTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVIN 645
Cdd:cd07118 104 ---YNnlgddmLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 646 IIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKG 725
Cdd:cd07118 181 IVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 726 ENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQV-QRPG 804
Cdd:cd07118 260 ECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLaSAAG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 805 FFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTY 884
Cdd:cd07118 340 LFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFD--TVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTF 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 283436218 885 NKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07118 418 LDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
446-921 |
1.14e-148 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 447.72 E-value: 1.14e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAG------WCDKIQGSTIpinqarpnynltftKKEPLGACAIIIPWNYPLM 599
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV--------------VREPIGVCGLITPWNWPLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 600 MLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQI 679
Cdd:cd07138 146 QIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 680 MKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGD 759
Cdd:cd07138 226 AEA-AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 760 PLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGrqVQRP-----GFFMEPTVFTGVEDHMYLAKEESFGPIMVIS 834
Cdd:cd07138 305 PRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 835 KFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINtYNKTDVAAPFGGMKQSGFGKDLGEEALNEYL 914
Cdd:cd07138 383 PYD--DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFL 459
|
....*..
gi 283436218 915 KIKTVTL 921
Cdd:cd07138 460 EVKSIQG 466
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
23-225 |
1.53e-147 |
|
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.
Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 434.57 E-value: 1.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 23 LKLALIGQSLFGQEVYSQLLKEGHRVVGVFTVPDKDGKADPLALAAEKDGTPVFKFPRWRLKGKTIKEVAEAYQSVGAEL 102
Cdd:cd08647 1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 103 NVLPFCTQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTV 182
Cdd:cd08647 81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 283436218 183 DSLYNRFLFPEGIKAMVEAVQLIADGKAPRTPQPEEGATYEGI 225
Cdd:cd08647 161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
492-921 |
1.56e-147 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 440.90 E-value: 1.56e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 492 AFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGWCDKIQGSTIPINqa 571
Cdd:cd06534 6 AFK--AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 572 rPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSG 651
Cdd:cd06534 81 -DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 652 GVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAA 731
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 732 GRLFVEEAIHDEFVTRVVeeikkmkigdpldrstdhgpqnhrahlekllqycetgvqegatlvyggrqvqrpgffmepTV 811
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 812 FTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNK-TDVA 890
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPE 336
|
410 420 430
....*....|....*....|....*....|.
gi 283436218 891 APFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
442-919 |
1.06e-145 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 440.50 E-value: 1.06e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 442 PYQCFINGQFVDAEdGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQ 521
Cdd:PRK13473 2 QTKLLINGELVAGE-GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP--EWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 522 EELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGStipinqARPNYNLTFT---KKEPLGACAIIIPWNYPL 598
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGK------AAGEYLEGHTsmiRRDPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 599 MMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAgFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQ 678
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 679 IMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIG 758
Cdd:PRK13473 232 VLSA-AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 759 DPLDRSTDHGPQNHRAHLEKLLQYCETGVQEG-ATLVYGGRQVQRPGFFMEPTVFTGV--EDHMYlaKEESFGPIMVISK 835
Cdd:PRK13473 311 DPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGArqDDEIV--QREVFGPVVSVTP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 836 FQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLK 915
Cdd:PRK13473 389 FD--DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTV 466
|
....
gi 283436218 916 IKTV 919
Cdd:PRK13473 467 VRHV 470
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
446-921 |
1.88e-145 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 439.70 E-value: 1.88e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWcdkiqGSTIPINQARP--NYNLTFTKKEPLGACAIIIPWNYPLMMLAW 603
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAAL-----ARDFPFEERRPgsGGGHVLVRREPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 604 KSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGsGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSC 683
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 684 AvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:cd07139 236 G-ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 764 STDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGrqvQRP-----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQn 838
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGG---GRPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYD- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 839 gDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYnKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKT 918
Cdd:cd07139 391 -DEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKS 468
|
...
gi 283436218 919 VTL 921
Cdd:cd07139 469 IYL 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
446-921 |
2.84e-145 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 439.01 E-value: 2.84e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNYNLtFTKKEPLGACAIIIPWNYPLMMLAWKS 605
Cdd:cd07088 79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIP--SDRPNENI-FIFKVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 606 AACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAV 685
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 sNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07088 235 -NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 766 DHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQ-RPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGV 844
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS--SLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 283436218 845 LQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
446-919 |
2.51e-143 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 433.98 E-value: 2.51e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGEtyATVNPTD-GTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEEL 524
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFP--AWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 525 ATIEALDSGAvyTLAL-KTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNYNLtFTKKEPLGACAIIIPWNYPLMMLAW 603
Cdd:cd07097 80 ARLLTREEGK--TLPEaRGEVTRAGQIFRYYAGEALRLSGETLP--STRPGVEV-ETTREPLGVVGLITPWNFPIAIPAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 604 KSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSc 683
Cdd:cd07097 155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 684 AVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:cd07097 234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 764 STDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRP--GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDI 841
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR--DY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 842 DGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN-TYNKTDVAAPFGGMKQSGFG-KDLGEEALNEYLKIKTV 919
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
446-915 |
4.62e-139 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 423.35 E-value: 4.62e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQgstipinQARPNYnltftkkEPLGACAIIIPWNYPLMMLAWKS 605
Cdd:cd07111 103 VLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-------TELAGW-------KPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 606 AACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVaGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAV 685
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 SNlKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07111 248 TG-KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 766 DHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQNGdiDGVL 845
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA--KEAV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 846 QRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLK 915
Cdd:cd07111 405 ALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
446-923 |
1.42e-138 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 421.85 E-value: 1.42e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEnGEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPN---YNlTFTKKEPLGACAIIIPWNYPLMMLA 602
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQgerYT-AFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVaGQRLSQHPDIRKLGFTGSTSVGKQIMKS 682
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 683 cAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLD 762
Cdd:cd07113 240 -AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 763 RSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPT--VFTGVEDHMYlaKEESFGPIMVISKFQNGd 840
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDE- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 841 iDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:cd07113 396 -EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
...
gi 283436218 921 LEY 923
Cdd:cd07113 475 IRY 477
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
443-919 |
2.37e-138 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 421.48 E-value: 2.37e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQE 522
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQArpnyNLTFTKKEPLGACAIIIPWNYPLMMLA 602
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDED----TLSIVLREPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKS 682
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 683 cAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLD 762
Cdd:cd07117 234 -AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 763 RSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQn 838
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 839 gDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKT 918
Cdd:cd07117 392 -TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKN 470
|
.
gi 283436218 919 V 919
Cdd:cd07117 471 I 471
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
462-921 |
8.38e-138 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 419.07 E-value: 8.38e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFenGEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAvytlALK 541
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGN----ALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 TH----IGMSVQTFRYFAGWCDKIQGSTIPinqARPNYnLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVL 617
Cdd:cd07108 75 TQarpeAAVLADLFRYFGGLAGELKGETLP---FGPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 618 KPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScAVSNLKKVSLELGG 697
Cdd:cd07108 151 KAAEDAPLAVLLLAEI-LAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRA-AADRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 698 KSPLIIFSDCDLEKAVR---MGMGavFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRA 774
Cdd:cd07108 229 KSPMIVFPDADLDDAVDgaiAGMR--FTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 775 HLEKLLQYCETGVQE-GATLVYGGRQ----VQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRAN 849
Cdd:cd07108 307 QFAKVCGYIDLGLSTsGATVLRGGPLpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWK--DEDEVIAMAN 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436218 850 NTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLG-EEALNEYLKIKTVTL 921
Cdd:cd07108 385 DSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
462-920 |
4.81e-137 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 417.14 E-value: 4.81e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALk 541
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 THIGMSVQTFRYFAGWCDKI---QGSTIPINQARPNYNltfTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLK 618
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLdakAERAVPLPSEDFKAR---VRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 619 PAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGK 698
Cdd:cd07110 155 PSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 699 SPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEK 778
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 779 LLQYCETGVQEGATLVYGGRQVQ--RPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLA 856
Cdd:cd07110 314 VLSFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFA--TEDEAIALANDSEYGLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 857 SGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:cd07110 392 AAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
463-919 |
2.67e-136 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 415.49 E-value: 2.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWgRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALKT 542
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWCDKIQGS-TIPINQARPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPL 701
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 702 IIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRqvqRP-----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLA 856
Cdd:cd07089 320 YIARGRDEGARLVTGGG---RPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYD--DDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436218 857 SGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
462-923 |
1.33e-135 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 413.31 E-value: 1.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTlALK 541
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 THIGMSVQTFRYFAGWCDKIQGSTIPInqarPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07107 78 GDVMVAAALLDYFAGLVTELKGETIPV----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPL 701
Cdd:cd07107 154 QAPLSALRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRA-AAEGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 702 IIFSDCDLEKAVR-MGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLL 780
Cdd:cd07107 232 IVFPDADPEAAADaAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 781 QYCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLA 856
Cdd:cd07107 312 HYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWR--DEAEMVAQANGVEYGLT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 283436218 857 SGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTLEY 923
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
439-919 |
2.76e-135 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 414.29 E-value: 2.76e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 439 VKIPYQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWGRMNARDRGRLMYRLADLME 518
Cdd:PRK09847 16 LAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 519 ENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarpNYNLTFTKKEPLGACAIIIPWNYPL 598
Cdd:PRK09847 96 AHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS----SHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 599 MMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQ 678
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 679 IMKSCAVSNLKKVSLELGGKSPLIIFSDC-DLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKI 757
Cdd:PRK09847 252 LLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 758 GDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGaTLVYGGRQVQRPGfFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQ 837
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 838 NGdiDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIK 917
Cdd:PRK09847 410 SE--EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
..
gi 283436218 918 TV 919
Cdd:PRK09847 488 TI 489
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
446-923 |
1.30e-133 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 409.04 E-value: 1.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTIC-RVSYASLADVDRAVAAAKDAFenGEWGRMNARDRGRLMYRLADLMEENQEEL 524
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVgTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 525 ATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNYNLtFTKKEPLGACAIIIPWNYPLMMLAWK 604
Cdd:cd07131 80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVP--SELPNKDA-MTRRQPIGVVALITPWNFPVAIPSWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 605 SAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCA 684
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 685 VSNlKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRS 764
Cdd:cd07131 236 RPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 765 TDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQR----PGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqnGD 840
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV--SS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 841 IDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINtyNKT---DVAAPFGGMKQSGFG-KDLGEEALNEYLKI 916
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEW 470
|
....*..
gi 283436218 917 KTVTLEY 923
Cdd:cd07131 471 KAVYVDY 477
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
464-921 |
2.80e-132 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 404.67 E-value: 2.80e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 464 NPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALKtH 543
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAK--EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 544 IGMSVQTFRYFAGWCDKIQGSTIPINQARPNYN-LTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIPFDASPGGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 623 TPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScavSNLKKVSLELGGKSPLI 702
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARK---AGLKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 703 IFSDCDLEKAV-RMGMGAvFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07149 239 VDADADLEKAVeRCVSGA-FANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRqvqRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFT 861
Cdd:cd07149 318 WVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD--TLDEAIAMANDSPYGLQAGVFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436218 862 RDINKAMYVSDKLEAGTVFIN---TYnKTDvAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07149 393 NDLQKALKAARELEVGGVMINdssTF-RVD-HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
444-921 |
2.63e-131 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 403.69 E-value: 2.63e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 444 QCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEE 523
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 524 LATIEALDSGAVYTLAL-KTHIGMSVqtFRYFAGWCDKIQGSTIPINQARPNynlTFTKKEPLGACAIIIPWNYPLMMLA 602
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAIgEVAYGASF--LEYFAEEAKRVYGDIIPSPFPDRR---LLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKS 682
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 683 CAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLD 762
Cdd:PLN02278 259 AA-ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 763 RSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDID 842
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK--TEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283436218 843 GVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
463-921 |
6.29e-130 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 398.44 E-value: 6.29e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWcdKIQGSTIPINQARpnynLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07106 79 EVGGAVAWLRYTASL--DLPDEVIEDDDTR----RVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 623 TPLTALKFAELTVKAgFPKGVINIIPGSGGVaGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLI 702
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 703 IFSDCDLEKAVR-MGMGAvFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07106 230 VLPDVDIDAVAPkLFWGA-FINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFT 861
Cdd:cd07106 309 LVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYS--DEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 862 RDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
437-920 |
3.48e-128 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 396.03 E-value: 3.48e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 437 MTVKIP-YQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAF---ENGEWGRMNARDRGRLMYR 512
Cdd:PLN02467 1 MAIPVPrRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 513 LADLMEENQEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGWCDKIQG-STIPINQARPNYNlTFTKKEPLGACAII 591
Cdd:PLN02467 81 IAAKITERKSELAKLETLDCGKPLDEAA-WDMDDVAGCFEYYADLAEALDAkQKAPVSLPMETFK-GYVLKEPLGVVGLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 592 IPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTG 671
Cdd:PLN02467 159 TPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 672 STSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEE 751
Cdd:PLN02467 239 STATGRKIMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 752 IKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGR--QVQRPGFFMEPTVFTGVEDHMYLAKEESFGP 829
Cdd:PLN02467 318 AKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 830 IMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEA 909
Cdd:PLN02467 398 VLCVKTFS--TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWG 475
|
490
....*....|.
gi 283436218 910 LNEYLKIKTVT 920
Cdd:PLN02467 476 LENYLSVKQVT 486
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
490-921 |
1.55e-125 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 386.50 E-value: 1.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 490 KDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYtlaLKTH--IGMSVQTFRYFAGWCDKIQGSTIP 567
Cdd:cd07104 10 AAAQK--AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR---PKAAfeVGAAIAILREAAGLPRRPEGEILP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 568 INQA-RPNYnltfTKKEPLGACAIIIPWNYPLMmLAWKSAA-CLAAGNTLVLKPAQVTPLT-ALKFAELTVKAGFPKGVI 644
Cdd:cd07104 85 SDVPgKESM----VRRVPLGVVGVISPFNFPLI-LAMRSVApALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 645 NIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVsNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNK 724
Cdd:cd07104 160 NVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 725 GENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQ-NHRAhLEKLLQYCETGVQEGATLVYGGRqvqRP 803
Cdd:cd07104 239 GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLiNERQ-VDRVHAIVEDAVAAGARLLTGGT---YE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 804 GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN- 882
Cdd:cd07104 315 GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFD--DDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINd 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 283436218 883 -TYNKtDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07104 393 qTVND-EPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
463-921 |
7.13e-125 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 385.55 E-value: 7.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYN-LTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPL 701
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 702 IIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQ 781
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 782 YCETGVQEGATLVYGGRQVQrpGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFT 861
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVK--DDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 283436218 862 RDINKAMYVSDKLEAGTVFIN--TYNKTDvAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07145 396 NDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
464-921 |
1.07e-124 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 384.76 E-value: 1.07e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 464 NPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALkTH 543
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFP--AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW-FE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 544 IGMSVQTFRYFAGWCDKIQGSTIPinqarPNYNLTF--TKKEPLGACAIIIPWNYPLMmLAWKSAA-CLAAGNTLVLKPA 620
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLP-----SDSPGTVsmSVRRPLGVVAGITPFNYPLI-LATKKVAfALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 621 QVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVsNLKKVSLELGGKSP 700
Cdd:cd07150 156 EETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 701 LIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLL 780
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 781 QYCETGVQEGATLVYGGRqvqRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVF 860
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAK--DAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 283436218 861 TRDINKAMYVSDKLEAGTVFINTYNKTDVA-APFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
445-923 |
2.80e-120 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 374.21 E-value: 2.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 445 CFINGQFVDAeDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFenGEWGRMNARDRGRLMYRLADLMEENQEEL 524
Cdd:cd07086 1 GVIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 525 ATIEALDSGAVYTLALKthigmSVQTF----RYFAGWCDKIQGSTIPinQARPNYNLtFTKKEPLGACAIIIPWNYPLMM 600
Cdd:cd07086 78 GRLVSLEMGKILPEGLG-----EVQEMidicDYAVGLSRMLYGLTIP--SERPGHRL-MEQWNPLGVVGVITAFNFPVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 601 LAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKA----GFPKGVINIIPGSGGVaGQRLSQHPDIRKLGFTGSTSVG 676
Cdd:cd07086 150 PGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 677 KQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMK 756
Cdd:cd07086 229 RRVGETVA-RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 757 IGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQR--PGFFMEPTVFTGVEDHMYLAKEESFGPIMVIS 834
Cdd:cd07086 308 IGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 835 KFQngDIDGVLQRANNTEYGLASGVFTRDINKAM-YVSDK-LEAGTVFINT-YNKTDVAAPFGGMKQSGFGKDLGEEALN 911
Cdd:cd07086 388 KFD--SLEEAIAINNDVPQGLSSSIFTEDLREAFrWLGPKgSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWK 465
|
490
....*....|..
gi 283436218 912 EYLKIKTVTLEY 923
Cdd:cd07086 466 QYMRRSTCTINY 477
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
491-919 |
4.21e-118 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 366.79 E-value: 4.21e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 491 DAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAgwcDKI----QGSTI 566
Cdd:cd07100 10 AAFL--AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYA---ENAeaflADEPI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 567 PINQARpnynlTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGV-IN 645
Cdd:cd07100 84 ETDAGK-----AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 646 IIPGSGGVAgqRLSQHPDIRKLGFTGSTSVGKQImKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKG 725
Cdd:cd07100 159 LLIDSDQVE--AIIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 726 ENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGF 805
Cdd:cd07100 236 QSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 806 FMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYN 885
Cdd:cd07100 316 FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVK--DEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMV 393
|
410 420 430
....*....|....*....|....*....|....
gi 283436218 886 KTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:cd07100 394 KSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
462-921 |
1.70e-116 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 363.59 E-value: 1.70e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 462 TVNPTDGTTICRVSYASLADVDRAVAAAKDAFENGEWgRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlK 541
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 THIGMSVQTFRYFAGWCDKIQGSTIpinQARPNyNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMI---EPEPG-SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 622 VTPLTALKFAELTVKA-GFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSP 700
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 701 LIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLL 780
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 781 QYCETGVQEGAT-LVYGGRQVQR--PGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLAS 857
Cdd:cd07120 314 RMVERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFD--DEAEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 858 GVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
443-923 |
1.88e-116 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 364.47 E-value: 1.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQE 522
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE--AWGKTSVAERANILNKIADRMEANLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYNLtftkKEPLGACAIIIPWNYPLMMLA 602
Cdd:cd07116 79 MLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHF----HEPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKS 682
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 683 cAVSNLKKVSLELGGKSPLIIFSDCD------LEKAVRmGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMK 756
Cdd:cd07116 234 -ASENIIPVTLELGGKSPNIFFADVMdaddafFDKALE-GFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 757 IGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPG-----FFMEPTVFTGveDHMYLAKEESFGPIM 831
Cdd:cd07116 312 QGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGllgggYYVPTTFKGG--NKMRIFQEEIFGPVL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 832 VISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALN 911
Cdd:cd07116 390 AVTTFK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLD 467
|
490
....*....|..
gi 283436218 912 EYLKIKTVTLEY 923
Cdd:cd07116 468 HYQQTKNLLVSY 479
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
444-921 |
1.59e-113 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 356.91 E-value: 1.59e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 444 QCFINGQFVDAEDGETYATVNPTDGTTICRVSyasladvDRAVAAAKDAFENGE-----WGRMNARDRGRLMYRLADLME 518
Cdd:PRK11241 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVP-------KMGADETRAAIDAANralpaWRALTAKERANILRRWFNLMM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 519 ENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPINQarPNYNLTFTKkEPLGACAIIIPWNYPL 598
Cdd:PRK11241 85 EHQDDLARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQ--ADKRLIVIK-QPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 599 MMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQ 678
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 679 IMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIG 758
Cdd:PRK11241 241 LMEQCA-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 759 DPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqn 838
Cdd:PRK11241 320 DGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF-- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 839 GDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKT 918
Cdd:PRK11241 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKY 477
|
...
gi 283436218 919 VTL 921
Cdd:PRK11241 478 MCI 480
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
449-922 |
4.86e-107 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 339.28 E-value: 4.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 449 GQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAfeNGEWGRMNARDRGRLMYRLADLMEENQEELATIE 528
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 529 ALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPIN-QARPNYnltfTKKEPLGACAIIIPWNYPLMmLAWKSAA 607
Cdd:cd07151 79 IRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvPGKENR----VYREPLGVVGVISPWNFPLH-LSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 608 -CLAAGNTLVLKPAQVTPLTA-LKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAv 685
Cdd:cd07151 153 pALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 SNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 766 DHGPQNHRAHLEKLLQYCETGVQEGATLVYGGrqvQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVL 845
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKAD--DEEEAL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 283436218 846 QRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVA-APFGGMKQSGFGKDLGEEALNEYLKIKTVTLE 922
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
461-921 |
1.85e-106 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 337.10 E-value: 1.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 461 ATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAL 540
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 541 KtHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYN-LTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP 619
Cdd:cd07094 80 V-EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNrLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 620 AQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMkscAVSNLKKVSLELGGKS 699
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALR---ANAGGKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 700 PLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKL 779
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 780 LQYCETGVQEGATLVYGGRqvqRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGV 859
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 860 FTRDINKAMYVSDKLEAGTVFIN--TYNKTDvAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVNdsSAFRTD-WMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
443-920 |
6.71e-106 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 337.66 E-value: 6.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAEDgeTYATVNPTD-GTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQ 521
Cdd:cd07124 33 YPLVIGGKEVRTEE--KIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFP--TWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 522 EELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGWCDKIQGStiPINQARPNYNLTFTkkEPLGACAIIIPWNYPLMML 601
Cdd:cd07124 109 FELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNRYVY--RPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMK 681
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 682 SCAV-----SNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMK 756
Cdd:cd07124 264 RAAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 757 IGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGaTLVYGGR--QVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVIS 834
Cdd:cd07124 344 VGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 835 KFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINtyNKTDVA----APFGGMKQSGFG-KDLGEEA 909
Cdd:cd07124 423 KAK--DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN--RKITGAlvgrQPFGGFKMSGTGsKAGGPDY 498
|
490
....*....|.
gi 283436218 910 LNEYLKIKTVT 920
Cdd:cd07124 499 LLQFMQPKTVT 509
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
492-921 |
1.83e-103 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 328.38 E-value: 1.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 492 AFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLA---LKTHIGMsvqtFRYFAGWCDKIQGSTIPi 568
Cdd:cd07105 12 AFP--AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAgfnVDLAAGM----LREAASLITQIIGGSIP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 569 nQARPNyNLTFTKKEPLGACAIIIPWNYPLMmLAWKSAAC-LAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINII 647
Cdd:cd07105 85 -SDKPG-TLAMVVKEPVGVVLGIAPWNAPVI-LGTRAIAYpLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 648 PGSGGVAGQRLSQ---HPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVrmgMGAV---F 721
Cdd:cd07105 162 THSPEDAPEVVEAliaHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAA---NAALfgaF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 722 FNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDpldrsTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQ 801
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 802 RP-GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqnGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVF 880
Cdd:cd07105 313 SPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 283436218 881 INTYNKTDVA-APFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07105 391 INGMTVHDEPtLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
463-917 |
2.54e-102 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 326.12 E-value: 2.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWCDKIQGSTIP--INQARPNYnLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPA 620
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldISARGEGR-QGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 621 QVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAgQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVsnlKKVSLELGGKSP 700
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 701 LIIFSDCDLEKAV-RMGMGAvFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKL 779
Cdd:cd07147 236 VIVDSDADLDFAAqRIIFGA-FYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 780 LQYCETGVQEGATLVYGGRqvqRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGV 859
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 860 FTRDINKAMYVSDKLEAGTVFINtynktDV------AAPFGGMKQSGFGKDLGEEALNEYLKIK 917
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVIN-----DVptfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
446-920 |
1.02e-101 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 325.63 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNYNlTFTKKEPLGACAIIIPWNYPLMMLAWKS 605
Cdd:cd07085 82 RLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLE--NVARGID-TYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 606 AACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGsGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScAV 685
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYER-AA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 SNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 766 DHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqnGDI 841
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRV--DTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 842 DGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINtynkTDVAAP-----FGGMKQSGFGkDL---GEEALNEY 913
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLhfyGKDGVRFY 468
|
....*..
gi 283436218 914 LKIKTVT 920
Cdd:cd07085 469 TQTKTVT 475
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
510-923 |
2.60e-99 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 316.68 E-value: 2.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 510 MYRLADLMEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPINqaRPNYNLtFTKKEPLGACA 589
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSD--RPGENI-LLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 590 IIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGF 669
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 670 TGSTSVGKQIMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVV 749
Cdd:PRK10090 157 TGSVSAGEKIMAA-AAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 750 EEIKKMKIGDPLDRST-DHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFG 828
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 829 PIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEE 908
Cdd:PRK10090 316 PVLPVVAFDT--LEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393
|
410
....*....|....*
gi 283436218 909 ALNEYLKIKTVTLEY 923
Cdd:PRK10090 394 GLHEYLQTQVVYLQS 408
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
497-920 |
1.03e-98 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 316.94 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 497 EWGRMNARDRGRLMYRLADLMEENQEELATIEALDSG----AVYTLALKTHIGMsvqtfRYFAGWCDKI-----QGSTIP 567
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGkarrHAFEEVLDVAIVA-----RYYARRAERLlkprrRRGAIP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 568 -INQARPNYNltftkkePLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINI 646
Cdd:cd07101 108 vLTRTTVNRR-------PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 647 IPGSGGVAGQRLSQHPDIrkLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGE 726
Cdd:cd07101 181 VTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 727 NCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRqvQRPG-- 804
Cdd:cd07101 258 LCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGR--ARPDlg 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 805 -FFMEPTVFTGVEDHMYLAKEESFGPIMVISKFqnGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN- 882
Cdd:cd07101 336 pYFYEPTVLTGVTEDMELFAEETFGPVVSIYRV--ADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNe 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 283436218 883 ----TYNKTDvaAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:cd07101 414 gyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
463-920 |
2.85e-97 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 313.00 E-value: 2.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALkT 542
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR--AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFAGWCDKIQGStipinQARPNYNLTFTKK-----EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVL 617
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLAP-----RKVPTGLLMPNKKatveyRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 618 KPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDirKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGG 697
Cdd:cd07099 153 KPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAGVD--KVAFTGSVATGRKVMAAAA-ERLIPVVLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 698 KSPLIIFSDCDLEKAVRmgmGAV---FFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRA 774
Cdd:cd07099 230 KDPMIVLADADLERAAA---AAVwgaMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 775 HLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYG 854
Cdd:cd07099 307 QLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYG 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 283436218 855 LASGVFTRDINKAMYVSDKLEAGTVFIN--TYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:cd07099 385 LSASVFSRDLARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
497-906 |
5.80e-96 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 309.22 E-value: 5.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 497 EWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVytlALKTH--IGMSVQTFRYFAGWCDKIQGSTIPINQARPN 574
Cdd:cd07152 28 AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSI---RPKAGfeVGAAIGELHEAAGLPTQPQGEILPSAPGRLS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 575 YnltfTKKEPLGACAIIIPWNYPLMmLAWKS-AACLAAGNTLVLKPAQVTPLTA-LKFAELTVKAGFPKGVINIIPGsGG 652
Cdd:cd07152 105 L----ARRVPLGVVGVISPFNFPLI-LAMRSvAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 653 VAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAG 732
Cdd:cd07152 179 DAGEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 733 RLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRqvqRPGFFMEPTVF 812
Cdd:cd07152 258 RHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YDGLFYRPTVL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 813 TGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN--TYNKtDVA 890
Cdd:cd07152 335 SGVKPGMPAFDEEIFGPVAPVTVFD--SDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdqTVND-EPH 411
|
410
....*....|....*.
gi 283436218 891 APFGGMKQSGFGKDLG 906
Cdd:cd07152 412 NPFGGMGASGNGSRFG 427
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
497-920 |
6.59e-95 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 309.12 E-value: 6.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 497 EWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALK--THIGMsvqTFRYFAGWCDKI-----QGSTIPI- 568
Cdd:PRK09407 69 AWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEevLDVAL---TARYYARRAPKLlaprrRAGALPVl 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 569 NQARPNYNltftkkePLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIP 648
Cdd:PRK09407 146 TKTTELRQ-------PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 649 GSGGVAGQRLSQHPDIrkLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENC 728
Cdd:PRK09407 219 GPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAG-RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLC 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 729 IAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRqvQRP--G-F 805
Cdd:PRK09407 296 ISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGK--ARPdlGpL 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 806 FMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN--- 882
Cdd:PRK09407 374 FYEPTVLTGVTPDMELAREETFGPVVSVYPVA--DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegy 451
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 283436218 883 --TYNKTDvaAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:PRK09407 452 aaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
499-921 |
7.69e-95 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 306.59 E-value: 7.69e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 499 GRMNARDRGRLMYRLADLMEENQEELATIEALDSGavytLALKT---HIGMSVQTFRYFAGWCDKIQGSTIPIN-----Q 570
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESG----LCLKDtryEVGRAADVLRFAAAEALRDDGESFSCDltangK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 571 ARpnynLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGS 650
Cdd:cd07146 111 AR----KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 651 GGVAGQRLSQHPDIRKLGFTGSTSVGKQImksCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIA 730
Cdd:cd07146 187 PGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 731 AGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGrqvQRPGFFMEPT 810
Cdd:cd07146 264 VKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGN---QRQGALYAPT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 811 VFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVA 890
Cdd:cd07146 341 VLDHVPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSE 418
|
410 420 430
....*....|....*....|....*....|...
gi 283436218 891 -APFGGMKQSGFGKDLG-EEALNEYLKIKTVTL 921
Cdd:cd07146 419 lSPFGGVKDSGLGGKEGvREAMKEMTNVKTYSL 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
443-902 |
2.88e-93 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 302.95 E-value: 2.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAeDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFeNGEWGRMNARDRGRLMYRLADLMEENQE 522
Cdd:cd07082 2 FKYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 523 ELATIEALDSGAVYTLALKtHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNYN-LTFTKKEPLGACAIIIPWNYPLMML 601
Cdd:cd07082 80 EVANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMK 681
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 682 ScavSNLKKVSLELGGKSPLIIFSDCDLEKAV-RMGMGAVFFNkGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDP 760
Cdd:cd07082 239 Q---HPMKRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 761 LDRSTDHGP---QNHRAHLEKLLqycETGVQEGATLVYGGRqvQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQ 837
Cdd:cd07082 315 WDNGVDITPlidPKSADFVEGLI---DDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 283436218 838 ngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNK--TDVaAPFGGMKQSGFG 902
Cdd:cd07082 390 --DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgPDH-FPFLGRKDSGIG 453
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
497-920 |
7.27e-90 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 293.44 E-value: 7.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 497 EWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGavytlalKTHI----GMSVQTfryfagwCDKIQ-----GSTIP 567
Cdd:cd07098 33 EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG-------KTMVdaslGEILVT-------CEKIRwtlkhGEKAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 568 INQARPNYNLTFTKK-----EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKA----G 638
Cdd:cd07098 99 RPESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 639 FPKGVINIIPGSGGvAGQRLSQHPDIRKLGFTGSTSVGKQIMKsCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMG 718
Cdd:cd07098 179 HDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMA-AAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 719 AVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGP---QNHRAHLEKLLQyceTGVQEGATLVY 795
Cdd:cd07098 257 GTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAmisPARFDRLEELVA---DAVEKGARLLA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 796 GGRQVQRP----GFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVS 871
Cdd:cd07098 334 GGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKAS--DDEEAVEIANSTEYGLGASVFGKDIKRARRIA 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 283436218 872 DKLEAGTVFINTYNKT--DVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVT 920
Cdd:cd07098 412 SQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
463-921 |
2.09e-88 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 289.15 E-value: 2.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 543 HIGMSVQTFRYFagwCDKIQGSTIPINQARPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07102 78 EIRGMLERARYM---ISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 623 TPLTALKFAELTVKAGFPKGVINIIPGSGGVaGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVsNLKKVSLELGGKSPLI 702
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 703 IFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQY 782
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 783 CETGVQEGATLVYGG---RQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQNgDiDGVLQRANNTEYGLASGV 859
Cdd:cd07102 313 IADAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKS-D-AEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 283436218 860 FTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTVTL 921
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
405-920 |
3.04e-87 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 288.37 E-value: 3.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 405 FGDF-IQKVVRRLRgedEEAEMVVDYVSKEvngmtvkipYQCFINGQFVDAEDgeTYATVNPTDGT-TICRVSYASLADV 482
Cdd:PRK03137 10 FTDFsVEENVEAFE---EALKKVEKELGQD---------YPLIIGGERITTED--KIVSINPANKSeVVGRVSKATKELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 483 DRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKI- 561
Cdd:PRK03137 76 EKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 562 QGStiPINQaRPN-YNLTFTkkEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFP 640
Cdd:PRK03137 153 DGK--PVES-RPGeHNRYFY--IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 641 KGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVSN-----LKKVSLELGGKSPLIIFSDCDLEKAVRM 715
Cdd:PRK03137 228 AGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 716 GMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRsTDHGPQNHRAHLEKLLQYCETGVQEGaTLVY 795
Cdd:PRK03137 308 IVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 796 GGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLE 875
Cdd:PRK03137 386 GGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK--DFDHALEIANNTEYGLTGAVISNNREHLEKARREFH 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 283436218 876 AGtvfiNTY-NKTDVAA-----PFGGMKQSGF-GKDLGEEALNEYLKIKTVT 920
Cdd:PRK03137 464 VG----NLYfNRGCTGAivgyhPFGGFNMSGTdSKAGGPDYLLLFLQAKTVS 511
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
443-920 |
5.58e-87 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 287.53 E-value: 5.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAEDgeTYATVNPTDGT-TICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQ 521
Cdd:TIGR01237 33 YPLVINGERVETEN--KIVSINPCDKSeVVGTVSKASQEHAEHALQAAAKAFE--AWKKTDPEERAAILFKAAAIVRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 522 EELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTiPINQARPNYNLTFTkkEPLGACAIIIPWNYPLMML 601
Cdd:TIGR01237 109 HEFSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGK-PVNSREGETNQYVY--TPTGVTVVISPWNFPFAIM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMK 681
Cdd:TIGR01237 185 VGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 682 SCAV-----SNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMK 756
Cdd:TIGR01237 265 RAAKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 757 IGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGaTLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKF 836
Cdd:TIGR01237 345 VGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 837 QngDIDGVLQRANNTEYGLASGVFTRD---INKAmyvSDKLEAGTVFIntyNKTDVAA-----PFGGMKQSGFG-KDLGE 907
Cdd:TIGR01237 424 S--DFDEALEIANNTEYGLTGGVISNNrdhINRA---KAEFEVGNLYF---NRNITGAivgyqPFGGFKMSGTDsKAGGP 495
|
490
....*....|...
gi 283436218 908 EALNEYLKIKTVT 920
Cdd:TIGR01237 496 DYLALFMQAKTVT 508
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
461-919 |
4.20e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 277.77 E-value: 4.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 461 ATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLAl 540
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 541 KTHIGMSVQTFRYFAGWCDKIQGSTiPINQARPNYNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPA 620
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADE-PADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 621 QVTPLTALKFAELTVKAGFPKGVI-NIIPGSGGVagQRLSQHPDIRKLGFTGSTSVGKQImKSCAVSNLKKVSLELGGKS 699
Cdd:PRK09406 160 SNVPQTALYLADLFRRAGFPDGCFqTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 700 PLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGP---QNHRAHL 776
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPlatEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 777 EKLLqycETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPimVISKFQNGDIDGVLQRANNTEYGLA 856
Cdd:PRK09406 317 EKQV---DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGP--VASLYRVADIDEAIEIANATTFGLG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436218 857 SGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
23-327 |
1.47e-76 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 252.33 E-value: 1.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 23 LKLALIGQSLFGQEVYSQLLKEGHRVVGVFTVPDKD---GK---ADPLALAAEKDGTPVFKfPRwRLKGKtikEVAEAYQ 96
Cdd:COG0223 1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQ-PE-SLKDP---EFLEELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 97 SVGAELNVLPFCTQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDV 176
Cdd:COG0223 76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 177 KPNDTVDSLYNRfLFPEGIKAMVEAVQLIADGKAPRTPQPEEGATYEGIQKKENAEVSWDQPAEGLHNWIRGHDKVPGAW 256
Cdd:COG0223 156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 257 AEINGQMVTFYGSslltssvpsgEPLDIRGAKKPGLV---TKNGLVLFGNDGkALMVRNLQFEDGKMIPASQYF 327
Cdd:COG0223 235 TTLDGKRLKIWKA----------RVLEEAGGGAPGTIlavDKDGLLVACGDG-ALRLLELQPAGKKRMSAADFL 297
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
445-902 |
2.07e-76 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 259.05 E-value: 2.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 445 CFINGQfvDAEDGETYATVNPTDG-TTICRVSYASLADVDRAVAAAKDAFenGEWGRMNARDRGRLMYRLADLMEENQEE 523
Cdd:cd07125 35 PIINGE--ETETGEGAPVIDPADHeRTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 524 LATIEALDSGAvyTLAlKTHIGMS--VQTFRYFA------GWCDKIQGSTIPINQARpnynltftkKEPLGACAIIIPWN 595
Cdd:cd07125 111 LIALAAAEAGK--TLA-DADAEVReaIDFCRYYAaqarelFSDPELPGPTGELNGLE---------LHGRGVFVCISPWN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 596 YPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSV 675
Cdd:cd07125 179 FPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 676 GKQIMKSCAVSNLKKVSL--ELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIK 753
Cdd:cd07125 259 AKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 754 KMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEgATLVYggrQVQRP---GFFMEPTVF--TGVEDHmylaKEESFG 828
Cdd:cd07125 339 SLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIA---PAPLDdgnGYFVAPGIIeiVGIFDL----TTEVFG 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283436218 829 PIMVISKFQNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIntyNKTDVAA-----PFGGMKQSGFG 902
Cdd:cd07125 411 PILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYI---NRNITGAivgrqPFGGWGLSGTG 486
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
457-923 |
4.06e-76 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 256.75 E-value: 4.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 457 GETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVY 536
Cdd:cd07130 11 GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 537 TLALKthigmSVQTF----RYFAGWCDKIQGSTIPinQARPNYNLtFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAG 612
Cdd:cd07130 89 PEGLG-----EVQEMidicDFAVGLSRQLYGLTIP--SERPGHRM-MEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 613 NTLVLKPAQVTPLTALK----FAELTVKAGFPKGVINIIPGsGGVAGQRLSQHPDIRKLGFTGSTSVGKQImkSCAVS-N 687
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV--GQAVAaR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 688 LKKVSLELGGKSPLIIFSDCDLEKAVRmgmgAVFF----NKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:cd07130 238 FGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 764 STDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGvEDHMYLAKEESFGPIMVISKFQngDIDG 843
Cdd:cd07130 314 GTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFD--TLEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 844 VLQRANNTEYGLASGVFTRDINKAM-----YVSDkleAGTVFINT-YNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIK 917
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFrwlgpKGSD---CGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRS 467
|
....*.
gi 283436218 918 TVTLEY 923
Cdd:cd07130 468 TCTINY 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
407-920 |
4.52e-72 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 246.72 E-value: 4.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 407 DFIQKVVRRLRGEDEEAemvvdyvskevngmtvkipYQCFINGQFVDAedGETYATVNPTD-GTTICRVSYASLADVDRA 485
Cdd:cd07083 2 RAMREALRRVKEEFGRA-------------------YPLVIGGEWVDT--KERMVSVSPFApSEVVGTTAKADKAEAEAA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 486 VAAAKDAFenGEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALKThIGMSVQTFRYFAGWCDKIQGST 565
Cdd:cd07083 61 LEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDD-VAEAIDFIRYYARAALRLRYPA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 566 IPINQARPNYNLTFTKkePLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVIN 645
Cdd:cd07083 138 VEVVPYPGEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 646 IIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCA-----VSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAV 720
Cdd:cd07083 216 FLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArlapgQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 721 FFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGaTLVYGGRQV 800
Cdd:cd07083 296 FGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 801 QRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVF 880
Cdd:cd07083 375 EGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLY 454
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 283436218 881 INTYNKTDVAA--PFGGMKQSGFG-KDLGEEALNEYLKIKTVT 920
Cdd:cd07083 455 INRKITGALVGvqPFGGFKLSGTNaKTGGPHYLRRFLEMKAVA 497
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
459-919 |
9.45e-69 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 236.30 E-value: 9.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 459 TYA-TVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYT 537
Cdd:PRK13968 7 THAiSVNPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 538 LAlKTHIGMSvqtfryfAGWCD----------KIQGSTIPINQARPNYnltftkkEPLGACAIIIPWNYPLMMLAWKSAA 607
Cdd:PRK13968 85 QA-RAEVAKS-------ANLCDwyaehgpamlKAEPTLVENQQAVIEY-------RPLGTILAIMPWNFPLWQVMRGAVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 608 CLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQhPDIRKLGFTGSTSVGKQImKSCAVSN 687
Cdd:PRK13968 150 ILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAI-GAQAGAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 688 LKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDH 767
Cdd:PRK13968 228 LKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 768 GPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQngDIDGVLQR 847
Cdd:PRK13968 308 GPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAK--DAEHALEL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 283436218 848 ANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTYNKTDVAAPFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:PRK13968 386 ANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
512-903 |
5.59e-63 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 219.32 E-value: 5.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 512 RLADLMEENQEELatIEAL--DSGAVYTLALKTHIGMSVQTFRY----FAGWCDKIQGSTIPINQ-ARpnynlTFTKKEP 584
Cdd:cd07087 28 ALKRMLTENEEEI--AAALyaDLGKPPAEAYLTEIAVVLGEIDHalkhLKKWMKPRRVSVPLLLQpAK-----AYVIPEP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 585 LGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAgFPKGVINIIPGSGGVAGQRLSQHPDi 664
Cdd:cd07087 101 LGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALLAEPFD- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 665 rKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEF 744
Cdd:cd07087 179 -HIFFTGSPAVGKIVMEA-AAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 745 VTRVVEEIKKMkIGDPLDRSTDHGPQNHRAHLEKLLQYCETGvqegaTLVYGGrQVQRPGFFMEPTVFTGVEDHMYLAKE 824
Cdd:cd07087 257 IEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-QVDKEERYIAPTILDDVSPDSPLMQE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 825 ESFGPIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINtynktDV-------AAPFGGMK 897
Cdd:cd07087 330 EIFGPILPILTYDD--LDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN-----DVllhaaipNLPFGGVG 402
|
....*.
gi 283436218 898 QSGFGK 903
Cdd:cd07087 403 NSGMGA 408
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
497-900 |
4.96e-61 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 214.06 E-value: 4.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 497 EWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGA--------VYTLALKthIGMSVQTFRYFAGwcDKiqgsTIPI 568
Cdd:cd07095 15 GWAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqteVAAMAGK--IDISIKAYHERTG--ER----ATPM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 569 NQARpnynlTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIP 648
Cdd:cd07095 87 AQGR-----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 649 GsGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENC 728
Cdd:cd07095 162 G-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 729 IAAGRLFVEE-AIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFM 807
Cdd:cd07095 241 TCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 808 EPTVF--TGVEDHmylAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN-TY 884
Cdd:cd07095 321 SPGIIdvTDAADV---PDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrPT 395
|
410
....*....|....*.
gi 283436218 885 NKTDVAAPFGGMKQSG 900
Cdd:cd07095 396 TGASSTAPFGGVGLSG 411
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
583-907 |
5.86e-60 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 210.93 E-value: 5.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 583 EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHP 662
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI-IREAFDEDEVAVFEGDAEVAQALLELPF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 663 DirKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHD 742
Cdd:cd07134 178 D--HIFFTGSPAVGKIVMAA-AAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 743 EFVTRVVEEIKKMKIGDPLDR-STDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGrQVQRPGFFMEPTVFTGVEDHMYL 821
Cdd:cd07134 255 AFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVTPDMKI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 822 AKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINtynktDVAA-------PFG 894
Cdd:cd07134 334 MQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-----DVVLhflnpnlPFG 406
|
330
....*....|...
gi 283436218 895 GMKQSGFGKDLGE 907
Cdd:cd07134 407 GVNNSGIGSYHGV 419
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
447-906 |
1.05e-56 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 203.99 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 447 INGQFVDaeDGETYATVNPTDGTTIC-RVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:TIGR01238 42 IGHSYKA--DGEAQPVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFP--TWNATPAKERAAKLDRLADLLELHMPELM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGAVYTLALkTHIGMSVQTFRYFAgwcdkiqgstipiNQARpnYNLTFTKKEPLGACAIIIPWNYPLMMLAWKS 605
Cdd:TIGR01238 118 ALCVREAGKTIHNAI-AEVREAVDFCRYYA-------------KQVR--DVLGEFSVESRGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 606 AACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAV 685
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 SNLKKVSL--ELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:TIGR01238 262 REDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 764 STDHGP-------QNHRAHLEKLLQYCETGVQegatLVYGGRQVQRPGFFMEPTVFTgvEDHMYLAKEESFGPIMVISKF 836
Cdd:TIGR01238 342 TTDVGPvidaeakQNLLAHIEHMSQTQKKIAQ----LTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRY 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436218 837 QNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIntyNKTDVAA-----PFGGMKQSGFGKDLG 906
Cdd:TIGR01238 416 KARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYV---NRNQVGAvvgvqPFGGQGLSGTGPKAG 487
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
23-202 |
8.31e-56 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 190.58 E-value: 8.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 23 LKLALI--GQSLFGQEVYSQLLKEGHRVVGVFTVPDKDGKADPLALAAEKDGTPVFKFPRWRLKGKTIKEVAEAYQSVGA 100
Cdd:pfam00551 1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 101 ELNVLPFCTQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPND 180
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|..
gi 283436218 181 TVDSLYNRFLFPEGiKAMVEAV 202
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
579-902 |
2.61e-54 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 195.42 E-value: 2.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 579 FTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRL 658
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 659 SQHPDirKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEE 738
Cdd:cd07136 174 DQKFD--YIFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 739 AIHDEFVTRVVEEIKKMKIGDPLDrSTDHGPQNHRAHLEKLLQYCETGvqegaTLVYGGrQVQRPGFFMEPTVFTGVEDH 818
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLDNG-----KIVFGG-NTDRETLYIEPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 819 MYLAKEESFGPIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAG------TV--FINTYnktdva 890
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDT--LDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggcindTImhLANPY------ 395
|
330
....*....|..
gi 283436218 891 APFGGMKQSGFG 902
Cdd:cd07136 396 LPFGGVGNSGMG 407
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
578-902 |
3.78e-54 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 194.75 E-value: 3.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 578 TFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIpgSGGVA--G 655
Cdd:cd07135 102 PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVV--QGGVPetT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 656 QRLSQHPDirKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLF 735
Cdd:cd07135 179 ALLEQKFD--KIFYTGSGRVGRIIAEA-AAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 736 VEEAIHDEFVTRVVEEIKKMKIGDPlDRSTDHGPQNHRAHLEKLLQYCETgvqEGATLVYGGRQvQRPGFFMEPTVFTGV 815
Cdd:cd07135 256 VDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEM-DEATRFIPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 816 EDHMYLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN-TYNKTDV-AAPF 893
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVdNAPF 408
|
....*....
gi 283436218 894 GGMKQSGFG 902
Cdd:cd07135 409 GGVGDSGYG 417
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
578-903 |
1.10e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.86 E-value: 1.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 578 TFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAgFPKGVINIIPGSGGVAGQR 657
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 658 LSQHPDIrkLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVE 737
Cdd:PTZ00381 182 LKEPFDH--IFFTGSPRVGKLVMQA-AAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 738 EAIHDEFVTRVVEEIKKMkIGDPLDRSTDHGPQNHRAHLEKLLQYCETgvqEGATLVYGGrQVQRPGFFMEPTVFTGVED 817
Cdd:PTZ00381 259 RSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGG-EVDIENKYVAPTIIVNPDL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 818 HMYLAKEESFGPIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIN--TYNKTDVAAPFGG 895
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYEN--IDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGG 411
|
....*...
gi 283436218 896 MKQSGFGK 903
Cdd:PTZ00381 412 VGNSGMGA 419
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
463-902 |
5.30e-52 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 189.17 E-value: 5.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 463 VNPTDGTTICRVSYASLADVDRAVAAAKDAFEN-GEWgrMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALk 541
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 542 thigmsVQTFRYFAG--WCDK----IQGSTIPIN--QARPNyNLTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGN 613
Cdd:cd07148 81 ------VEVTRAIDGveLAADelgqLGGREIPMGltPASAG-RIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 614 TLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAgQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVSNlkKVSL 693
Cdd:cd07148 154 PVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVA-EKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 694 ELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHR 773
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 774 AHLEKLLQYCETGVQEGATLVYGGRQVQRPGFfmEPTVFTGVEDHMYLAKEESFGPIMVIskFQNGDIDGVLQRANNTEY 853
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCV--YSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 283436218 854 GLASGVFTRDINKAMYVSDKLEAGTVFIN--TYNKTDvAAPFGGMKQSGFG 902
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVNdhTAFRVD-WMPFAGRRQSGYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
446-902 |
2.25e-51 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 195.80 E-value: 2.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGqfvdaeDGETYATVNPTDGT-TICRVSYASLADVDRAVAAAKDAFenGEWGRMNARDRGRLMYRLADLMEENQEE- 523
Cdd:PRK11904 556 IING------EGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAEl 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 524 --LATIEAldsGavytlalKT-HIGMS-----VQTFRYFAgwcdkiqgstipiNQARpnynLTFTKKEPL---------- 585
Cdd:PRK11904 628 iaLCVREA---G-------KTlQDAIAevreaVDFCRYYA-------------AQAR----RLFGAPEKLpgptgesnel 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 586 -----GACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQ 660
Cdd:PRK11904 681 rlhgrGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTA 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 661 HPDIRKLGFTGSTSVGKQIMKSCAVSNLKKVSL--ELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEE 738
Cdd:PRK11904 761 DPRIAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQE 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 739 AIHDefvtRVVEEIK----KMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEgATLVYggrQVQRP-----GFFMEP 809
Cdd:PRK11904 841 DIAD----RVIEMLKgamaELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLA---QLPLPagtenGHFVAP 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 810 TVFtgvE-DHMYLAKEESFGPIMVISKFQNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIntyNKTD 888
Cdd:PRK11904 913 TAF---EiDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYV---NRNQ 986
|
490
....*....|....*....
gi 283436218 889 VAA-----PFGGMKQSGFG 902
Cdd:PRK11904 987 IGAvvgvqPFGGQGLSGTG 1005
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
445-923 |
2.32e-51 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 188.89 E-value: 2.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 445 CFINGQFvdAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEEL 524
Cdd:PLN02315 23 CYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 525 ATIEALDSGAVytlaLKTHIGmSVQTF----RYFAGWCDKIQGSTIPinQARPNYnLTFTKKEPLGACAIIIPWNYPLMM 600
Cdd:PLN02315 99 GRLVSLEMGKI----LAEGIG-EVQEIidmcDFAVGLSRQLNGSIIP--SERPNH-MMMEVWNPLGIVGVITAFNFPCAV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 601 LAWKSAACLAAGNTLVLKPAQVTPLTALK----FAELTVKAGFPKGVINIIPGsGGVAGQRLSQHPDIRKLGFTGSTSVG 676
Cdd:PLN02315 171 LGWNACIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 677 kqIMKSCAV-SNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKM 755
Cdd:PLN02315 250 --LMVQQTVnARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 756 KIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVFTgVEDHMYLAKEESFGPIMVISK 835
Cdd:PLN02315 328 KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 836 FQNgdIDGVLQRANNTEYGLASGVFTRD---INKAM--YVSDkleAGTVFINT-YNKTDVAAPFGGMKQSGFGKDLGEEA 909
Cdd:PLN02315 407 FKT--LEEAIEINNSVPQGLSSSIFTRNpetIFKWIgpLGSD---CGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDS 481
|
490
....*....|....
gi 283436218 910 LNEYLKIKTVTLEY 923
Cdd:PLN02315 482 WKQYMRRSTCTINY 495
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
583-919 |
3.21e-51 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 186.15 E-value: 3.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 583 EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAgQRLSQHP 662
Cdd:cd07133 100 QPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDEVAVVTGGADVA-AAFSSLP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 663 -DirKLGFTGSTSVGKQIMKSCAvSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIH 741
Cdd:cd07133 178 fD--HLLFTGSTAVGRHVMRAAA-ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 742 DEFVTRVVEEIKKMkIGDPLDRSTDHGPQNHRaHLEKLLQYCETGVQEGATLVYGGRQVQRP--GFFMEPTVFTGVEDHM 819
Cdd:cd07133 255 EEFVAAAKAAVAKM-YPTLADNPDYTSIINER-HYARLQGLLEDARAKGARVIELNPAGEDFaaTRKLPPTLVLNVTDDM 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 820 YLAKEESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINtynktDVA-------AP 892
Cdd:cd07133 333 RVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN-----DTLlhvaqddLP 405
|
330 340
....*....|....*....|....*..
gi 283436218 893 FGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:cd07133 406 FGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
437-923 |
4.69e-51 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 189.96 E-value: 4.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 437 MTVKIPYqcFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADL 516
Cdd:PLN02419 110 MPPRVPN--LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQEL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 517 MEENQEELATIEALDSGAVytlaLKTHIGMSVQTFRYFAGWCDKiqgSTIPINQARPNYNL---TFTKKEPLGACAIIIP 593
Cdd:PLN02419 186 IRKNMDKLAMNITTEQGKT----LKDSHGDIFRGLEVVEHACGM---ATLQMGEYLPNVSNgvdTYSIREPLGVCAGICP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 594 WNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQrLSQHPDIRKLGFTGST 673
Cdd:PLN02419 259 FNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 674 SVGKQIMKSCAVSNlKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGR-LFVEEAihDEFVTRVVEEI 752
Cdd:PLN02419 338 TAGMHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 753 KKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGF----FMEPTVFTGVEDHMYLAKEESFG 828
Cdd:PLN02419 415 KALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFG 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 829 PIMVIskFQNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTynKTDVAAPFGGM--KQSGFGKDL- 905
Cdd:PLN02419 495 PVLVC--MQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgNKASFAGDLn 570
|
490 500
....*....|....*....|
gi 283436218 906 --GEEALNEYLKIKTVTLEY 923
Cdd:PLN02419 571 fyGKAGVDFFTQIKLVTQKQ 590
|
|
| FDH_Hydrolase_C |
cd08703 |
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ... |
228-327 |
5.75e-51 |
|
The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.
Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 174.07 E-value: 5.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 228 KENAEVSWDQPAEGLHNWIRGHDKVPGAWAEINGQMVTFYGSSLLTSSVPSGEPLDIRGAKKPGLVTKNGLVLFGNDGKA 307
Cdd:cd08703 1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGGEVEVEGLERPGIVHKNGLLITGSDGKM 80
|
90 100
....*....|....*....|
gi 283436218 308 LMVRNLQFEDGKMIPASQYF 327
Cdd:cd08703 81 VNVKRLQFEDGKMIPASKYG 100
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
447-902 |
1.00e-48 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 188.22 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 447 INGQfvdAEDGETYATVNPTDGTTIC-RVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:COG4230 562 IAGE---AASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFP--AWSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TI-----------------EALDsgavytlalkthigmsvqtF-RYFAgwcdkiqgstipiNQARPNYNlTFTKKEPLGA 587
Cdd:COG4230 637 ALlvreagktlpdaiaevrEAVD-------------------FcRYYA-------------AQARRLFA-APTVLRGRGV 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 588 CAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKL 667
Cdd:COG4230 684 FVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGV 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 668 GFTGSTSVGKQIMKSCAVSNLKKVSL--ELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFV 745
Cdd:COG4230 764 AFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVL 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 746 TRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQEGaTLVYggrQVQRP-----GFFMEPTVFtgvE-DHM 819
Cdd:COG4230 844 EMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVH---QLPLPeecanGTFVAPTLI---EiDSI 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 820 YLAKEESFGPIMVISKFQNGDIDGVLQRANNTEYGLASGVFTRdINK-AMYVSDKLEAGTVFIntyNKTDVAA-----PF 893
Cdd:COG4230 917 SDLEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGVHSR-IDEtIDRVAARARVGNVYV---NRNIIGAvvgvqPF 992
|
....*....
gi 283436218 894 GGMKQSGFG 902
Cdd:COG4230 993 GGEGLSGTG 1001
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
443-918 |
1.07e-48 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 180.72 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 443 YQCFINGQFVDAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAfeNGEWGRMNARDRGRLMYRLADLMEENQE 522
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 523 ELAtiEALdsgaVYTLA-----LKTHIGMSVQTFRYFA-------GWCDKIQGSTIPINqARPNYNLTftKKEPLGACAI 590
Cdd:PLN00412 94 PIA--ECL----VKEIAkpakdAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGN-ERNKYCLT--SKIPLGVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 591 IIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFT 670
Cdd:PLN00412 165 IPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 671 GSTSvGKQIMKSCAVSNLKkvsLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVE 750
Cdd:PLN00412 245 GGDT-GIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 751 EIKKMKIGDPLDRStDHGP---QNHRAHLEKLLqycETGVQEGATLVyggRQVQRPGFFMEPTVFTGVEDHMYLAKEESF 827
Cdd:PLN00412 321 KVAKLTVGPPEDDC-DITPvvsESSANFIEGLV---MDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 828 GPIMVISKFqnGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFINTY-NKTDVAAPFGGMKQSGFGKDLG 906
Cdd:PLN00412 394 GPVLPVIRI--NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGI 471
|
490
....*....|..
gi 283436218 907 EEALNEYLKIKT 918
Cdd:PLN00412 472 TNSINMMTKVKS 483
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
453-902 |
2.22e-48 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 186.99 E-value: 2.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 453 DAEDGETYATVNPTD-GTTICRVSYASLADVDRAVAAAKDAFENgeWGRMNARDRGRLMYRLADLMEENQEEL---ATIE 528
Cdd:PRK11905 562 GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELfalAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 529 AldsGAVYTLAlkthIGM---SVQTFRYFAgwcdkiqgstipiNQARPNYNLTFTKkePLGACAIIIPWNYPLMMLAWKS 605
Cdd:PRK11905 640 A---GKTLANA----IAEvreAVDFLRYYA-------------AQARRLLNGPGHK--PLGPVVCISPWNFPLAIFTGQI 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 606 AACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAV 685
Cdd:PRK11905 698 AAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAK 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 686 SNLKKVSL--ELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:PRK11905 778 RSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 764 STDHGPQNHRAHLEKLLQYCETGVQEGaTLVYggrQVQRP-----GFFMEPTVFTgVEDHMYLaKEESFGPIMVISKFQN 838
Cdd:PRK11905 858 STDVGPVIDAEAQANIEAHIEAMRAAG-RLVH---QLPLPaetekGTFVAPTLIE-IDSISDL-EREVFGPVLHVVRFKA 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 839 GDIDGVLQRANNTEYGLASGVFTRdINKAM-YVSDKLEAGTVFIntyNKTDVAA-----PFGGMKQSGFG 902
Cdd:PRK11905 932 DELDRVIDDINATGYGLTFGLHSR-IDETIaHVTSRIRAGNIYV---NRNIIGAvvgvqPFGGEGLSGTG 997
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
25-204 |
3.57e-48 |
|
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.
Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 169.01 E-value: 3.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 25 LALIGQSLFGQEVYSQLL-KEGHRVVGVFTVPDKDGKADPLALAAEKDgtpvfkfPRWRLKGKTIKEVAEAYQSVGAELN 103
Cdd:cd08369 1 IVILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSPRGTAQLSLELVGG-------KVYLDSNINTPELLELLKEFAPDLI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 104 VLPFCTQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVD 183
Cdd:cd08369 74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAG 153
|
170 180
....*....|....*....|.
gi 283436218 184 SLYNRfLFPEGIKAMVEAVQL 204
Cdd:cd08369 154 TLYQR-LIELGPKLLKEALQK 173
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
446-900 |
6.81e-47 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 175.15 E-value: 6.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 446 FINGQFVdAEDGETYATVNPTDGTTICRVSYASLADVDRAVAAAKDAFEngEWGRMNARDRGRLMYRLADLMEENQEELA 525
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 526 TIEALDSGA--------VYTLALKthIGMSVQTFRYFAGwcdkIQGSTIPINQArpnynltFTKKEPLGACAIIIPWNYP 597
Cdd:PRK09457 81 EVIARETGKplweaateVTAMINK--IAISIQAYHERTG----EKRSEMADGAA-------VLRHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 598 LMMLAWKSAACLAAGNTLVLKPAQVTPltalKFAELTVK----AGFPKGVINIIPGsGGVAGQRLSQHPDIRKLGFTGST 673
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTP----WVAELTVKlwqqAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 674 SVGKQIMKSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVEEAIH-DEFVTRVVEEI 752
Cdd:PRK09457 223 NTGYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 753 KKMKIGDPldrstDHGPQ-------NHRAhLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVF--TGVEDhmyLAK 823
Cdd:PRK09457 303 KRLTVGRW-----DAEPQpfmgaviSEQA-AQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIdvTGVAE---LPD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 824 EESFGPIMVISKFQngDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVfinTYNK----TDVAAPFGGMKQS 899
Cdd:PRK09457 374 EEYFGPLLQVVRYD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPFGGVGAS 448
|
.
gi 283436218 900 G 900
Cdd:PRK09457 449 G 449
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
23-330 |
7.43e-47 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 170.27 E-value: 7.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 23 LKLALIGQSLFGQEVYSQLLKEGHRVVGVFTVPDKDG------KADPLALAAEKDGTPVFKFprwrlkgkTIKEVAEAYQ 96
Cdd:TIGR00460 1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP--------EKQRQLEELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 97 SVGaELN-----VLPFcTQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQ 171
Cdd:TIGR00460 73 LVR-ELKpdvivVVSF-GKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 172 RSCDVKPNDTVDSLYNRfLFPEGIKAMVEAVQLIADGKAPRTPQPEEGATYEGIQKKENAEVSWDQPAEGLHNWIRGHDK 251
Cdd:TIGR00460 151 ETFPIEEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNP 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283436218 252 VPGAWAEINGQMVTFYGSSLLTSSVPSGEPLDIRGAKKPGLvtkngLVLFGNDGkALMVRNLQFEDGKMIPASQYFSAG 330
Cdd:TIGR00460 230 WPTAWLTFEGKNIKIHKAKVIDLSTYKAKPGEIVYHNKKGI-----LVACGKDG-ILLLLSLQPPGKKVMRAEDFYNGS 302
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
432-900 |
5.27e-46 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 173.54 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 432 KEVNGMTVKIPyqCFINGQFVdaEDGETYATVNPTD-GTTICRVSYASladvdraVAAAKDAFEN-----GEWGRMNARD 505
Cdd:cd07123 24 AELKSLTVEIP--LVIGGKEV--RTGNTGKQVMPHDhAHVLATYHYAD-------AALVEKAIEAalearKEWARMPFED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 506 RGRLMYRLADLMEENQEelatiealdsgavYTLALKTHIGMS--------------VQTFRYFAGWCDKIQGSTiPINQA 571
Cdd:cd07123 93 RAAIFLKAADLLSGKYR-------------YELNAATMLGQGknvwqaeidaacelIDFLRFNVKYAEELYAQQ-PLSSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 572 RPNYNltFTKKEPL-GACAIIIPWNY----------PLMMlawksaaclaaGNTLVLKPAQVTPLTALKFAELTVKAGFP 640
Cdd:cd07123 159 AGVWN--RLEYRPLeGFVYAVSPFNFtaiggnlagaPALM-----------GNVVLWKPSDTAVLSNYLVYKILEEAGLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 641 KGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVS-----NLKKVSLELGGKSPLIIFSDCDLEKAVRM 715
Cdd:cd07123 226 PGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 716 GMGAVFFNKGENCIAAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETGVQE-GATLV 794
Cdd:cd07123 306 TVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEII 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 795 YGGRQVQRPGFFMEPTVFTGVEDHMYLAKEESFGPIMVISKFQNGDIDGVLQRANNT-EYGLASGVFTRD---INKAmyv 870
Cdd:cd07123 386 AGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTsPYALTGAIFAQDrkaIREA--- 462
|
490 500 510
....*....|....*....|....*....|....
gi 283436218 871 SDKLE--AGTVFINTYNKTDVAA--PFGGMKQSG 900
Cdd:cd07123 463 TDALRnaAGNFYINDKPTGAVVGqqPFGGARASG 496
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
41-222 |
6.15e-46 |
|
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 163.77 E-value: 6.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 41 LLKEGHRVVGVFTVPDKD---GK---ADPLALAAEKDGTPVFKFPRWRLKgktikEVAEAYQSVGAELNVLPFCTQFIPM 114
Cdd:cd08646 19 LLKSGHEVVAVVTQPDKPrgrGKkltPSPVKELALELGLPVLQPEKLKDE-----EFLEELKALKPDLIVVVAYGQILPK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 115 DVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRfLFPEG 194
Cdd:cd08646 94 EILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK-LAELG 172
|
170 180
....*....|....*....|....*...
gi 283436218 195 IKAMVEAVQLIADGKAPRTPQPEEGATY 222
Cdd:cd08646 173 ADLLLEVLDDIEAGKLNPVPQDESEATY 200
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
23-223 |
1.37e-43 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 156.47 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 23 LKLALIGQSLFGQEVYSQLLKEGHRVVGVfTVPDKDGKADPLALAAEKDGTPVFKFPRwrLKGKTIKEvaeayqsvGAEL 102
Cdd:cd08822 1 MKIAIAGQKWFGTAVLEALRARGIALLGV-AAPEEGDRLAAAARTAGSRGLPRAGVAV--LPADAIPP--------GTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 103 NVLPFCTQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTV 182
Cdd:cd08822 70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 283436218 183 DSLYNRFLFPEGIKAMVEAVQ-LIADGKAPRTPQPEEGATYE 223
Cdd:cd08822 150 AELWRRALAPMGVKLLTQVIDaLLRGGNLPAQPQDERLATWE 191
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
579-912 |
1.80e-38 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 149.29 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 579 FTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVK----AGFPkgVINiipgsGGV- 653
Cdd:cd07132 95 YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKyldkECYP--VVL-----GGVe 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 654 -AGQRLSQHPDirKLGFTGSTSVGKQIMKScAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAG 732
Cdd:cd07132 168 eTTELLKQRFD--YIFYTGSTSVGKIVMQA-AAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 733 RLFVEEAIHDEFVTRVVEEIKKMKIGDPLDrSTDHGP---QNHRAHLEKLLqycetgvqEGATLVYGGRQVQRPGfFMEP 809
Cdd:cd07132 245 YVLCTPEVQEKFVEALKKTLKEFYGEDPKE-SPDYGRiinDRHFQRLKKLL--------SGGKVAIGGQTDEKER-YIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 810 TVFTGVEDHMYLAKEESFGPIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRD---INKAMyvsDKLEAGTVFINtynk 886
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNN--LDEAIEFINSREKPLALYVFSNNkkvINKIL---SNTSSGGVCVN---- 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 283436218 887 tDV-------AAPFGGMKQSGFG-------------------KDLGEEALNE 912
Cdd:cd07132 386 -DTimhytldSLPFGGVGNSGMGayhgkysfdtfshkrsclvKSLNMEKLNS 436
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
583-902 |
6.01e-38 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 147.56 E-value: 6.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 583 EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHP 662
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 663 DirKLGFTGSTSVGKQIMkSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAVRMGMGAVF-FNKGENCIAAGRLFVEEAIH 741
Cdd:cd07137 179 D--KIFFTGSPRVGRIIM-AAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 742 DEFVTRVVEEIKKMKIGDPldRSTDHGPQ----NHRAHLEKLLQycETGVQegATLVYGGrQVQRPGFFMEPTVFTGVED 817
Cdd:cd07137 256 PTLIDALKNTLEKFFGENP--KESKDLSRivnsHHFQRLSRLLD--DPSVA--DKIVHGG-ERDEKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 818 HMYLAKEESFGPIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVfinTYNKTDV-----AAP 892
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKK--IEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV---TFNDTVVqyaidTLP 403
|
330
....*....|
gi 283436218 893 FGGMKQSGFG 902
Cdd:cd07137 404 FGGVGESGFG 413
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
505-902 |
4.73e-37 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 151.28 E-value: 4.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 505 DRGRLMYRLADLMEENQEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGwcdkiqgstipinQARPNY-NLTftkKE 583
Cdd:PRK11809 705 ERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI-AEVREAVDFLRYYAG-------------QVRDDFdNDT---HR 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 584 PLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPD 663
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADAR 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 664 IRKLGFTGSTSVGKQIMKSCAvSNL----KKVSL--ELGGKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVE 737
Cdd:PRK11809 848 VRGVMFTGSTEVARLLQRNLA-GRLdpqgRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 738 EAIHDEFVTRVVEEIKKMKIGDPlDR-STDHGP---QNHRAHLEKLLQYCETGVQEGATLVYGGRQVQRPGFFMEPTVft 813
Cdd:PRK11809 927 DDVADRTLKMLRGAMAECRMGNP-DRlSTDIGPvidAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTL-- 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 814 gVE-DHMYLAKEESFGPIMVISKFQNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVFIntyNKTDVAA- 891
Cdd:PRK11809 1004 -IElDSFDELKREVFGPVLHVVRYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYV---NRNMVGAv 1079
|
410
....*....|....*
gi 283436218 892 ----PFGGMKQSGFG 902
Cdd:PRK11809 1080 vgvqPFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
583-903 |
4.57e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 122.14 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 583 EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTAlKFAELTVKAGFPKGVINIIPGsGGVAGQRLSQHP 662
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 663 -DirKLGFTGSTSVGKQIMkSCAVSNLKKVSLELGGKSPLI---IFSDCDLEKAVRMGMGAVFFN-KGENCIAAGRLFVE 737
Cdd:PLN02203 185 wD--KIFFTGSPRVGRIIM-TAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 738 EaihdEFVTRVVEEIKKM--KIGDPLDRSTDHGP----QNHRAHLEKLLQycETGVQegATLVYGGrQVQRPGFFMEPTV 811
Cdd:PLN02203 262 E----RFAPILIELLKSTikKFFGENPRESKSMArilnKKHFQRLSNLLK--DPRVA--ASIVHGG-SIDEKKLFIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 812 FTGVEDHMYLAKEESFGPIMVISKFQNgdIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLEAGTVfinTYNKTDV-- 889
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKK--IEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAIIqy 407
|
330
....*....|....*..
gi 283436218 890 ---AAPFGGMKQSGFGK 903
Cdd:PLN02203 408 acdSLPFGGVGESGFGR 424
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
24-205 |
8.83e-29 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 113.52 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 24 KLALIGQSLFGQEVYSQLLKEGHRVVGVFTVPDKDGKADP----LALAAEKDGTPVFKFprwrlkgKTI--KEVAEAYQS 97
Cdd:cd08651 1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSdyldLDSFARKNGIPYYKF-------TDIndEEIIEWIKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 98 VGAELNvlpFC---TQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSC 174
Cdd:cd08651 74 ANPDII---FVfgwSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPF 150
|
170 180 190
....*....|....*....|....*....|.
gi 283436218 175 DVKPNDTVDSLYNRFlfpegIKAMVEAVQLI 205
Cdd:cd08651 151 PIDKDDTANSLYDKI-----MEAAKQQIDKF 176
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
496-915 |
1.37e-28 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 120.04 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 496 GEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALKthIGMSVQTFRYFAgwcDKIQGSTIPINQA-RPN 574
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAEN--ICGDQVQLRARA---FVIYSYRIPHEPGnHLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 575 YNLTFTKKE---PLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAG-FPKGVINIIPGS 650
Cdd:cd07084 88 QGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 651 GGvAGQRLSQHPDIRKLGFTGSTSVGKQImkscaVSNLK--KVSLELGGKSPLIIFSDCDLEKAV------RMGMGAvff 722
Cdd:cd07084 168 GK-TMQALLLHPNPKMVLFTGSSRVAEKL-----ALDAKqaRIYLELAGFNWKVLGPDAQAVDYVawqcvqDMTACS--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 723 nkGENCIAAGRLFVEEAIHDE-FVTRVVEEIKKMKIGDP-LDRSTDHGPQNHRAHLEKLLqycetgvqeGATLVYGGRQV 800
Cdd:cd07084 239 --GQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLlLGPVQTFTTLAMIAHMENLL---------GSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 801 QR------PGFFMEPTVFTGVE--DHMYLA-KEESFGPIMVISKFQNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVS 871
Cdd:cd07084 308 KNhsipsiYGACVASALFVPIDeiLKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELI 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 283436218 872 DKLE-AGTVFINTYNKTDVAAP---FGGMKQSGFGKDLG-EEALNEYLK 915
Cdd:cd07084 388 GNLWvAGRTYAILRGRTGVAPNqnhGGGPAADPRGAGIGgPEAIKLVWR 436
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
583-919 |
2.18e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 113.99 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 583 EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELtVKAGFPKGVINIIPGSGGVAGQRLSQHP 662
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 663 DirKLGFTGSTSVGKQIMkSCAVSNLKKVSLELGGKSPLIIFSDCDLEKAV-RMGMGAVFFNKGENCIAAGRLFVEEAIH 741
Cdd:PLN02174 190 D--KIFYTGSSKIGRVIM-AAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVrRIIAGKWGCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 742 DEFVTRVVEEIKKMKIGDPLDrSTDHG---PQNHRAHLEKLLQYCETGVQegatLVYGGRQvQRPGFFMEPTVFTGVEDH 818
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPME-SKDMSrivNSTHFDRLSKLLDEKEVSDK----IVYGGEK-DRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 819 MYLAKEESFGPIMVISKFQNGD--IDGVLQRANNteygLASGVFTRDINKAMYVSDKLEAGTVFINtynktDVAA----- 891
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEesFDVIRSRPKP----LAAYLFTHNKKLKERFAATVSAGGIVVN-----DIAVhlalh 411
|
330 340 350
....*....|....*....|....*....|
gi 283436218 892 --PFGGMKQSGFGKDLGEEALNEYLKIKTV 919
Cdd:PLN02174 412 tlPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
112-326 |
1.77e-25 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 107.86 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 112 IPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNrflf 191
Cdd:PRK06988 90 IPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 192 pegiKAMVEAVQLIA-------DGKAPRTPQPEEGATYEGIQKKENAEVSWDQPAEGLHNWIRG-HDKVPGAWAEINGQM 263
Cdd:PRK06988 166 ----KVTVAAEQTLWrvlpallAGEAPHLPNDLAQGSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTR 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 283436218 264 VTFYGSSLLtssVPSGEPLDirgAKKPGL-VTKNGLVLFGNDGKALMV---RNLQFEDGKMIPASQY 326
Cdd:PRK06988 242 FVVARARLA---APGAAAAR---DLPPGLhVSDNALFGVCGDGRAVSIlelRRQQDGGETVVTPAQF 302
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
48-326 |
1.13e-22 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 100.15 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 48 VVGVFTVPDKDGK------ADPLALAAEKDGTPvfkfPRWRLKGKTIKEVA--EAYQSVGAELNVLPFCTQFIPMDVIDS 119
Cdd:PLN02285 38 VAAVVTQPPARRGrgrklmPSPVAQLALDRGFP----PDLIFTPEKAGEEDflSALRELQPDLCITAAYGNILPQKFLDI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 120 PKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRfLFPEGIKAMV 199
Cdd:PLN02285 114 PKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPL-LFELGTKLLL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 200 EAVQLIADGKAPR--TPQPEEGATYEGIQKKENAEVSWDQPAEGLHNWIRGHDKVPGAWAEIngqMVTFYGSS------- 270
Cdd:PLN02285 193 RELPSVLDGSAKDkaTPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGWPGTRAKF---QLVDDGDGerevlel 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 283436218 271 -LLTSSVP--SGEPLDIRGAkkpGLVTKNGLVLFGNDGKALMVRNLQFEDGKMIPASQY 326
Cdd:PLN02285 270 kIITTRVCeaGGEQTGSADA---VTFKKDSLLVPCGGGTWLEVLEVQPPGKKVMKAKDF 325
|
|
| Formyl_trans_C |
pfam02911 |
Formyl transferase, C-terminal domain; |
227-327 |
1.72e-21 |
|
Formyl transferase, C-terminal domain;
Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 90.03 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 227 KKENAEVSWDQPAEGLHNWIRGHDKVPGAWAEINGQMVTFYGSslltssvpsgEPLDIRGAKKPGLV--TKNGLVLFGND 304
Cdd:pfam02911 3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKA----------SVLDQESGAAPGTIvtVDKGGLLVACG 72
|
90 100
....*....|....*....|...
gi 283436218 305 GKALMVRNLQFEDGKMIPASQYF 327
Cdd:pfam02911 73 DGALLILELQLEGKKPMSAEDFL 95
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
47-209 |
6.56e-21 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 91.63 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 47 RVVGVFTvpdkDgKADPLALA-AEKDGTPVFKFPRWRLKGKTI--KEVAEAYQSVGAELNVL---------PFCTQFipm 114
Cdd:COG0299 30 EIVLVIS----N-RPDAYGLErARAAGIPTFVLDHKDFPSREAfdAALLEALDAYGPDLVVLagfmriltpEFVRAF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 115 dvidspkHGSII-YHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRFLfPE 193
Cdd:COG0299 102 -------PGRIInIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARIL-EQ 173
|
170
....*....|....*.
gi 283436218 194 GIKAMVEAVQLIADGK 209
Cdd:COG0299 174 EHRLYPEAIRLLAEGR 189
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
39-224 |
7.17e-21 |
|
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.
Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 91.64 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 39 SQLLKEGHRVVGVFTVPDKDGKA---DPLALAAEKDGTPVF-----KFPRWRlkgktikevaEAYQSVGAELNVLPFCTQ 110
Cdd:cd08644 17 EALLAAGFEVVAVFTHTDNPGENiwfGSVAQLAREHGIPVFtpddiNHPEWV----------ERLRALKPDLIFSFYYRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 111 FIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRFL 190
Cdd:cd08644 87 MISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLC 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 283436218 191 FPEGikaMVEAVQL--IADGKAPRTPQPEEGATYEG 224
Cdd:cd08644 167 VAAR---RLLARTLpaLKAGKARERPQDETQASYFG 199
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
115-325 |
1.64e-20 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 96.98 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 115 DVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRFLFPEG 194
Cdd:PRK08125 91 EILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAAR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 195 iKAMVEAVQLIADGKAPRTPQPEEGATYEGIQKKENAEVSWDQPAEGLHNWIRG-HDKVPGAWaeingqmvTFYGSSLLT 273
Cdd:PRK08125 171 -QLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAvTDPWPGAF--------SYVGEQKFT 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 283436218 274 ssVPSGEPLDIRGAKKPGLV-TKNGLVLFGNDGkALMVRNLQFEDGKMIPASQ 325
Cdd:PRK08125 242 --VWSSRVLPDASGAQPGTVlSVAPLRIACGEG-ALEIVTGQAGDGLYMQGSQ 291
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
437-830 |
1.12e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 80.90 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 437 MTVKIPYqcFINGQFVDAEdGETYATVNPTDGTTICRVSYASLADVDRAvaaakdAFENGEWG----RMNARDRGRLMYR 512
Cdd:PRK11903 1 MTELLAN--YVAGRWQAGS-GAGTPLFDPVTGEELVRVSATGLDLAAAF------AFAREQGGaalrALTYAQRAALLAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 513 LADLMEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGStipinQARPNYNLTFTKKEPL------- 585
Cdd:PRK11903 72 IVKVLQANRDAYYDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDA-----RLLRDGEAVQLGKDPAfqgqhvl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 586 ----GACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAG-FPKGVINIIPGSGGVAGQRLsQ 660
Cdd:PRK11903 146 vptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHL-Q 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 661 HPDIrkLGFTGSTSVGKQIMKSCAV------SNLKKVSLE----LGGKSPLIIFSDCDLEKAVR-MGMGAvffnkGENCI 729
Cdd:PRK11903 225 PFDV--VSFTGSAETAAVLRSHPAVvqrsvrVNVEADSLNsallGPDAAPGSEAFDLFVKEVVReMTVKS-----GQKCT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 730 AAGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHRAHLEKLLQYCETgVQEGATLVYGGRQVQRP------ 803
Cdd:PRK11903 298 AIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFALVdadpav 376
|
410 420 430
....*....|....*....|....*....|....*
gi 283436218 804 GFFMEPTVF--------TGVEDHmylakeESFGPI 830
Cdd:PRK11903 377 AACVGPTLLgasdpdaaTAVHDV------EVFGPV 405
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
60-198 |
3.79e-15 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 74.35 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 60 KADPLALA-AEKDGTPVFKFPRWRLKGKTI--KEVAEAYQSVGAELNVL---------PFCTQFipmdvidspkHGSII- 126
Cdd:cd08645 36 NPDAYGLErAKKAGIPTFVINRKDFPSREEfdEALLELLKEYKVDLIVLagfmrilspEFLEAF----------PGRIIn 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 283436218 127 YHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRF------LFPEGIKAM 198
Cdd:cd08645 106 IHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIhalehrLYPEAIKLL 183
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
584-880 |
9.19e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 77.92 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 584 PLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAGFPKGVINIIpGSGGVAGQRLSQHPD 663
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLI-HSDGPTMNKILLEAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 664 IRKLGFTGSTSVGKQImkscAVSNLKKVSLELGGKSPLIIFSD----------CDLEkavrmgmgaVFFNKGENCIAAGR 733
Cdd:cd07126 221 PRMTLFTGSSKVAERL----ALELHGKVKLEDAGFDWKILGPDvsdvdyvawqCDQD---------AYACSGQKCSAQSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 734 LFVeeaiHDEFV-TRVVEEIKKMKIGDPLDRSTDhGP------QNHRAHLEKLLQYcetgvqEGATLVYGGRQVQ---RP 803
Cdd:cd07126 288 LFA----HENWVqAGILDKLKALAEQRKLEDLTI-GPvltwttERILDHVDKLLAI------PGAKVLFGGKPLTnhsIP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 804 GFF--MEPT-VF-----TGVEDHMYLAKEESFGPIMVISKFQNGDIDGVLQRANNTEYGLASGVFTRDINKAMYVSDKLE 875
Cdd:cd07126 357 SIYgaYEPTaVFvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTV 436
|
....*
gi 283436218 876 AGTVF 880
Cdd:cd07126 437 NGTTY 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
490-754 |
2.43e-14 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 76.43 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 490 KDAFEngEWGRMNARDRGRLMYRLADLMEENQEELATIEALDSGavYTLALKT-HIGMSVQTFRYFA------GWCDKIQ 562
Cdd:cd07129 9 AAAFE--SYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFAdlvregSWLDARI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 563 GSTIPINQARPNYNLTFTKKePLGACAIIIPWNYPLmmlAWK-----SAACLAAGNTLVLK--PAQvtPLTALKFAELTV 635
Cdd:cd07129 85 DPADPDRQPLPRPDLRRMLV-PLGPVAVFGASNFPL---AFSvaggdTASALAAGCPVVVKahPAH--PGTSELVARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 636 KA----GFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCAVSNL-KKVSLELGGKSPLIIFSDCDLE 710
Cdd:cd07129 159 AAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILPGALAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 283436218 711 KAV--------RMGMGAvffnkGENCIAAGRLFV-EEAIHDEFVTRVVEEIKK 754
Cdd:cd07129 239 RGEaiaqgfvgSLTLGA-----GQFCTNPGLVLVpAGPAGDAFIAALAEALAA 286
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
90-202 |
5.14e-14 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 70.32 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 90 EVAEAYQSVGAELNVLPFCtQFIPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGD-KKAGFSVFWADDGLDTGPI 168
Cdd:cd08653 38 EVVAALRALAPDVVSVYGC-GIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDTGDV 116
|
90 100 110
....*....|....*....|....*....|....
gi 283436218 169 LLQRSCDVKPNDTVDSLYNRfLFPEGIKAMVEAV 202
Cdd:cd08653 117 LAQARPPLAAGDTLLSLYLR-LYRAGVELMVEAI 149
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
40-185 |
6.06e-14 |
|
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.
Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 70.37 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 40 QLLKEGHRVVGVFTvpdkdgkADP-LALAAEKDGTPVFkfprwrlkgktikevaEAYQSVGAELNVLPFCTQF------- 111
Cdd:cd08649 17 QLLAAGHRIAAVVS-------TDPaIRAWAAAEGIAVL----------------EPGEALEELLSDEPFDWLFsivnlri 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436218 112 IPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSL 185
Cdd:cd08649 74 LPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
444-863 |
8.50e-14 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 75.00 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 444 QCFINGQFVdAEDGETYATVNPTDGTTICRVSYASLADvdravaaaKDAFEngeWGR---------MNARDRGRLMYRLA 514
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGLDF--------AAAVA---YARekggpalraLTFHERAAMLKALA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 515 DLMEENQEELATIeALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDK--------IQGSTIPINQarpnyNLTFTKKE--- 583
Cdd:cd07128 70 KYLMERKEDLYAL-SAATGATRRDS-WIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSK-----DGTFVGQHilt 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 584 PLGACAIII-PWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELTVKAG-FPKGVINIIPGSGGVAGQRLsQH 661
Cdd:cd07128 143 PRRGVAVHInAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHL-GE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 662 PDIrkLGFTGSTSVGKQIMKS-CAVSNLKKVSLELGGKSPLIIFSDC-------DL---EKAVRMGMGAvffnkGENCIA 730
Cdd:cd07128 222 QDV--VAFTGSAATAAKLRAHpNIVARSIRFNAEADSLNAAILGPDAtpgtpefDLfvkEVAREMTVKA-----GQKCTA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 731 AGRLFVEEAIHDEFVTRVVEEIKKMKIGDPLDRSTDHGP-------QNHRAHLEKLLQycetgvqeGATLVYGGRQVQRP 803
Cdd:cd07128 295 IRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPlvsreqrEDVRAAVATLLA--------EAEVVFGGPDRFEV 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436218 804 -------GFFMEPTVF--------TGVEDHmylakeESFGPimVISKFQNGDIDGVLQRANNTEYGLASGVFTRD 863
Cdd:cd07128 367 vgadaekGAFFPPTLLlcddpdaaTAVHDV------EAFGP--VATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| Met_tRNA_FMT_C |
cd08704 |
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
229-323 |
1.78e-13 |
|
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.
Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 66.79 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 229 ENAEVSWDQPAEGLHNWIRGHDKVPGAWAEINGQMVTFYGSSLLTSSVPSGEPLDIRgakkpglVTKNGLVLFGNDGkAL 308
Cdd:cd08704 1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAEVLEESGEAAPGTILA-------VDKKGLLVACGDG-AL 72
|
90
....*....|....*
gi 283436218 309 MVRNLQFEDGKMIPA 323
Cdd:cd08704 73 EILELQPEGKKRMSA 87
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
106-206 |
1.92e-12 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 66.70 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 106 PFCTQF---IPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTV 182
Cdd:cd08823 75 VVVFTFpyrIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154
|
90 100
....*....|....*....|....
gi 283436218 183 DSLYNRfLFPEGIKAMVEAVQLIA 206
Cdd:cd08823 155 GLLCSR-LAMLAVGLLEELYQNLA 177
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
128-208 |
2.08e-12 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 66.63 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 128 HPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRFLFPEGiKAMVEAVQLIAD 207
Cdd:TIGR00639 108 HPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIHKQEH-RIYPLAIAWFAQ 186
|
.
gi 283436218 208 G 208
Cdd:TIGR00639 187 G 187
|
|
| FMT_core_HypX_N |
cd08650 |
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ... |
83-206 |
3.71e-11 |
|
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.
Pssm-ID: 187719 [Multi-domain] Cd Length: 151 Bit Score: 62.25 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 83 LKGKTIKEVAEAYQsvgAELNVLPFCTQFIPMDVIDspKHGSIIYHPSLlPRHRGASAINWTLIMGDKKAGFSVFWADDG 162
Cdd:cd08650 34 LSDDEMREAVALFA---PDLIICPFLKKRIPEEIWS--NYPCLIVHPGI-VGDRGPSSLDWAILEGEKEWGVTVLQAVEE 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 283436218 163 LDTGPILLQRSCDVKPNDTVDSLYNRFLFPEGIKAMVEAVQLIA 206
Cdd:cd08650 108 MDAGPIWATRNFPLRRAATKSSLYRGEVTDAAVKAVLEAVENFE 151
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
491-895 |
1.76e-10 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 64.17 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 491 DAFENGEWGRMNARD--RGRLMYRLADLMEENQEELATIEALDSGAVYTLALKTHIGM----------SVQTFRYFAGWC 558
Cdd:cd07077 1 ESAKNAQRTLAVNHDeqRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMmgcsesklykNIDTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 559 DKIQGSTipinqaRPNYNLTFTKKEPLGACAIIIPWNYPLMMLAwKSAACLAAGNTLVLKPAQVTPLTALKFAELT---V 635
Cdd:cd07077 81 GHIQDVL------LPDNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 636 KAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKScavSNLKKVSLELGGKSPLIIFSDCDLEKAVRM 715
Cdd:cd07077 154 AAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 716 GMGAVFFNkGENCIAAGRLFVeeaiHDEFVTRVVEEIKkmkigdpldrsTDHGPQNHRAHLEKLLQYCETGVQEGATLVy 795
Cdd:cd07077 231 VHDSKFFD-QNACASEQNLYV----VDDVLDPLYEEFK-----------LKLVVEGLKVPQETKPLSKETTPSFDDEAL- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 796 ggrqvqrpgFFMEPT--VFTGVEDHMYLAKEesfgpIMVISKFQNgdidgvlqrannteyGLASGVFTRDINKAMYVSDK 873
Cdd:cd07077 294 ---------ESMTPLecQFRVLDVISAVENA-----WMIIESGGG---------------PHTRCVYTHKINKVDDFVQY 344
|
410 420
....*....|....*....|..
gi 283436218 874 LEAGTVFINTYNKTDVAAPFGG 895
Cdd:cd07077 345 IDTASFYPNESSKKGRGAFAGK 366
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
577-751 |
7.05e-09 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 59.20 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 577 LTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP----AQVTPLTALKFAELTVKAGFPKGVINIIPGSGG 652
Cdd:cd07081 88 GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 653 VAGQRLSQHPDIRKLGFTGSTSVGKQIMKScavsnlKKVSLELG-GKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAA 731
Cdd:cd07081 168 ELAQRLMKFPGIGLLLATGGPAVVKAAYSS------GKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASE 241
|
170 180
....*....|....*....|
gi 283436218 732 GRLFVEEAIHDEFVTRVVEE 751
Cdd:cd07081 242 QSVIVVDSVYDEVMRLFEGQ 261
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
577-751 |
6.66e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 56.09 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 577 LTFTKKEPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP----AQVTPLTALKFAELTVKAGFPKGVINIIPGSGG 652
Cdd:cd07121 90 LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAEAGGPDNLVVTVEEPTI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 653 VAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCavsnlKKVSLELGGKSPLIIFSDCDLEKAVR-MGMGAVFFNkgeN--CI 729
Cdd:cd07121 170 ETTNELMAHPDINLLVVTGGPAVVKAALSSG-----KKAIGAGAGNPPVVVDETADIEKAARdIVQGASFDN---NlpCI 241
|
170 180
....*....|....*....|..
gi 283436218 730 AAGRLFVEEAIHDEFVTRVVEE 751
Cdd:cd07121 242 AEKEVIAVDSVADYLIAAMQRN 263
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
609-751 |
8.31e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 55.68 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 609 LAAGNTLVLKP----AQVTPLTALKFAELTVKAGFPKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCa 684
Cdd:PRK15398 154 LAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSG- 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 685 vsnlKKVSLELGGKSPLIIFSDCDLEKAVR-MGMGAVFFNkgeN--CIAAGRLFVEEAIHDEFVTRVVEE 751
Cdd:PRK15398 233 ----KKAIGAGAGNPPVVVDETADIEKAARdIVKGASFDN---NlpCIAEKEVIVVDSVADELMRLMEKN 295
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
107-203 |
1.65e-07 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 52.06 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 107 FCTQF---IPMDVIDSPKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVD 183
Cdd:cd08820 74 ISVQYhwiLPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVI 153
|
90 100
....*....|....*....|
gi 283436218 184 SLYNRFLFpEGIKAMVEAVQ 203
Cdd:cd08820 154 SLYILAHY-AAIALFGEHIT 172
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
498-863 |
2.56e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 54.41 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 498 WGRMNARDRGRLMYRLADLMEENQEELATIEALDSGAVYTLALK---THI---GMSVQTFRYFAgwCDKIQGSTIPINQA 571
Cdd:cd07127 100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQaggPHAqdrGLEAVAYAWRE--MSRIPPTAEWEKPQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 572 RPNYNLTFTKK---EPLG-----ACAIIIPWN-YPLMMlawksaACLAAGNTLVLKPAqvtPLTALKFAeLTVK------ 636
Cdd:cd07127 178 GKHDPLAMEKTftvVPRGvalviGCSTFPTWNgYPGLF------ASLATGNPVIVKPH---PAAILPLA-ITVQvarevl 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 637 --AGF-PKGVINIIPGSGGVAGQRLSQHPDIRKLGFTGSTSVGKQIMKSCavsNLKKVSLELGGKSPLIIFSDCDLEKAV 713
Cdd:cd07127 248 aeAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA---RQAQVYTEKAGVNTVVVDSTDDLKAML 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 714 RMGMGAVFFNKGENCIAAGRLFV---------EEAIHDEFVTRVVEEIKKMkIGDPlDRSTD--HGPQNH--RAHLEKLL 780
Cdd:cd07127 325 RNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAIDGL-LADP-ARAAAllGAIQSPdtLARIAEAR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 781 QycetgvqeGATLVYGGRQVQRPGF----FMEPTVFTGVEDHMYLAKEESFGPIMVISKFQNGDIDGVLQRANNTEYG-L 855
Cdd:cd07127 403 Q--------LGEVLLASEAVAHPEFpdarVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVREHGaM 474
|
....*...
gi 283436218 856 ASGVFTRD 863
Cdd:cd07127 475 TVGVYSTD 482
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
108-230 |
2.62e-07 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 52.60 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 108 CTQFIPMDVIDSPKhgSIIYHPSLLPRHRGASAINWTLImGDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYN 187
Cdd:PRK07579 74 CKQRFPAKLVNGVR--CINIHPGFNPYNRGWFPQVFSII-NGLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYA 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 283436218 188 RFLFPEgIKAMVEAVQLIADGKAPRTpQPEEGATYEGIQKKEN 230
Cdd:PRK07579 151 RVMDIE-RELVLEHFDAIRDGSYTAK-KPATEGNLNSKKDFKQ 191
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
68-200 |
6.52e-07 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 50.85 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 68 AEKDGTPVFKFPRWR--LKGKTIKEVAEAYQSVGAELNVLPFCTQFIPMDVIDSPKHGSIIYHPSLLPRHRG----ASAI 141
Cdd:PLN02331 45 ARENGIPVLVYPKTKgePDGLSPDELVDALRGAGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyyGIKV 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 283436218 142 NWTLIM-GDKKAGFSVFWADDGLDTGPILLQRSCDVKPNDTVDSLYNRFL------FPEGIKAMVE 200
Cdd:PLN02331 125 HKAVIAsGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLheehqlYVEVVAALCE 190
|
|
| Arna_FMT_C |
cd08702 |
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ... |
235-320 |
4.76e-06 |
|
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.
Pssm-ID: 187730 Cd Length: 92 Bit Score: 45.69 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 235 WDQPAEGLHNWIRG-HDKVPGAWAEINGQMVTFYGSSLLTSSVPSGEpldirgakkPGLV---TKNGLVLFGNDGkALMV 310
Cdd:cd08702 7 WRMSAREIYNLVRAvTKPYPGAFTFVGGQKIKIWKARPVDDAFYNGE---------PGKVlsvDGDPLIVACGDG-ALEI 76
|
90
....*....|
gi 283436218 311 RNLQFEDGKM 320
Cdd:cd08702 77 LEAELDGGLP 86
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
583-754 |
2.81e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 44.40 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 583 EPLGACAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP---AQVTPLTALKF-AELTVKAGFPKGVINIIPGSGGVAGQRL 658
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 659 SQHPDIRKLGFTGSTSVGKQIMKScavsnlKKVSLELG-GKSPLIIFSDCDLEKAVRMGMGAVFFNKGENCIAAGRLFVE 737
Cdd:cd07122 174 MKHPDVDLILATGGPGMVKAAYSS------GKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVD 247
|
170
....*....|....*..
gi 283436218 738 EAIHDEfvtrVVEEIKK 754
Cdd:cd07122 248 DEIYDE----VRAELKR 260
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
344-417 |
2.87e-04 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 40.22 E-value: 2.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 283436218 344 VAETIKVIWARILSNTP-VIEDSTDFFKS-GASSMDVVRLVEEIRQSCgGLQLQNEDVYMATKFGDFIQKVVRRLR 417
Cdd:COG0236 6 LEERLAEIIAEVLGVDPeEITPDDSFFEDlGLDSLDAVELIAALEEEF-GIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
346-387 |
6.58e-04 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 38.70 E-value: 6.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 283436218 346 ETIKVIWARILS-NTPVIEDSTDFFKSGASSMDVVRLVEEIRQ 387
Cdd:pfam00550 1 ERLRELLAEVLGvPAEEIDPDTDLFDLGLDSLLAVELIARLEE 43
|
|
| FMT_core_like_1 |
cd08821 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
106-247 |
6.80e-03 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187723 [Multi-domain] Cd Length: 211 Bit Score: 38.84 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436218 106 PFCTQFIPMDVIDspKHGSIIYHPSLLPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRscDVKPNDTVDSL 185
Cdd:cd08821 51 PHWSWIIPKEIFE--NFECVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLKR--DLSLKGTAEEI 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 283436218 186 YNRflFPEGIKAMVeaVQLIADGKAPrTPQPEEGATYEGiQKKENAEVSWDQPAEGLHNWIR 247
Cdd:cd08821 127 YER--ASKISLKMI--PELVTKKPKP-IKQEGEPVTFKR-RTPEQSNISNEANLEKIYDFIR 182
|
|
| |
