|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
417-902 |
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: 1009.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLM 496
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 497 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYP 576
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 577 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 656
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 657 HIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07140 241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 737 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 816
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 817 DGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:cd07140 401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
....*.
gi 21614513 897 TVTFEY 902
Cdd:cd07140 481 TVTIEY 486
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
420-900 |
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: 778.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 420 MPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQH 499
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 500 QEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMM 579
Cdd:cd07091 82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPID----GNFLAYTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 580 LSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIM 659
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 660 KSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNP 739
Cdd:cd07091 238 EAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 740 LDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 819
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK--T 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 820 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
.
gi 21614513 900 F 900
Cdd:cd07091 476 I 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
430-898 |
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: 621.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 430 FVDAEGaKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEAL 509
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 510 DAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLA 589
Cdd:pfam00171 78 ENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGR----LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 590 AGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKK 669
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 670 VSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQ 749
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 750 NHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANA 829
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAND 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 830 TEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
422-899 |
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: 620.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGR-WGKISARDRGRLMYRLADLMEQHQ 500
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 501 EELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMML 580
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMD----GDFFTYTRHEPVGVCGQIIPWNFPLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07141 163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 661 SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:cd07141 243 AAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 820
Cdd:cd07141 323 DPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK--TI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
421-902 |
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: 604.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQ 500
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 501 EELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRnLTLTRKEPVGVCGIIIPWNYPLMML 580
Cdd:COG1012 83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 661 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:COG1012 239 AAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 819
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD--D 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 820 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:COG1012 396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
....
gi 21614513 899 TFEY 902
Cdd:COG1012 476 TIRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
477-900 |
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: 566.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarPNRNL 556
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIPSP---DPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 637 LSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVE 716
Cdd:cd07078 170 LASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 717 DSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVE 795
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTVLTDVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK-TDVAAPFGG 874
Cdd:cd07078 329 PDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFGG 406
|
410 420
....*....|....*....|....*.
gi 21614513 875 FKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07078 407 VKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
415-898 |
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: 547.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 415 KRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgRWGKISARDRGRLMYRLAD 494
Cdd:cd07144 1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 495 LMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWN 574
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS----PNKLAYTLHEPYGVCGQIIPWN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 575 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEV 654
Cdd:cd07144 156 YPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 655 GKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRK- 733
Cdd:cd07144 236 GRLVMKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQn 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 734 MKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGN---QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVM 810
Cdd:cd07144 315 YKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 811 IISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALN 890
Cdd:cd07144 395 VISKFK--TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLE 472
|
....*...
gi 21614513 891 EYLRVKTV 898
Cdd:cd07144 473 TYTQTKAV 480
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
441-900 |
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: 544.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALK 520
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQGSTIPINqaRPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAVIPVD--KGDY-LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKSPL 680
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARA-AAENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 761 YCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLAS 836
Cdd:cd07114 316 YVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE-EAI-ALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21614513 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
425-898 |
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: 540.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 505 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinqaRPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYD----VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 664
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 744
Cdd:cd07119 235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 745 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDl 820
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE- 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21614513 821 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07119 394 EAI-RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
437-898 |
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: 537.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 437 KTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYT 516
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 517 LALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVI 596
Cdd:cd07112 82 DALAVDVPSAANTFRWYAEAIDKVYGEVAPT----GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 597 KPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGG 676
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 677 KSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 755
Cdd:cd07112 238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 756 VKLMEYCQHGVKEGATLVCGGNQV--PRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFG 833
Cdd:cd07112 318 DKVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE-EAV-ALANDSVYG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 834 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07112 396 LAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
421-898 |
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: 535.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQ 500
Cdd:cd07142 3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 501 EELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLTLtrKEPVGVCGIIIPWNYPLMML 580
Cdd:cd07142 83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADG--PHHVYTL--HEPIGVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07142 159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 661 SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:cd07142 239 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 820
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK--TV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21614513 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
417-898 |
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: 532.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGrWG-KISARDRGRLMYRLADL 495
Cdd:cd07143 2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETD-WGlKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 496 MEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNY 575
Cdd:cd07143 81 MERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKK----LTYTRHEPIGVCGQIIPWNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 576 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVG 655
Cdd:cd07143 157 PLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 656 KHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMK 735
Cdd:cd07143 237 RKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 736 VGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRF 815
Cdd:cd07143 317 VGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 816 ADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRV 895
Cdd:cd07143 397 KTE--EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQI 474
|
...
gi 21614513 896 KTV 898
Cdd:cd07143 475 KAV 477
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
441-898 |
3.91e-180 |
|
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: 527.39 E-value: 3.91e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK 520
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQGSTIPInqaRPnRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPV---RG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 761 YCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFT 840
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21614513 841 RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07115 392 RDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
442-900 |
9.72e-177 |
|
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: 518.53 E-value: 9.72e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 522 HVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIP--SPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 602 TPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 681
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 762 CQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTR 841
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFD--TEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 842 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
414-898 |
2.82e-175 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 517.07 E-value: 2.82e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 414 NKRTVRMPH----QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLM 489
Cdd:PLN02766 9 GASGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 490 YRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRNLTLtrKEPVGVCGI 569
Cdd:PLN02766 89 MKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM--SRQLQGYTL--KEPIGVVGH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 570 IIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFT 649
Cdd:PLN02766 165 IIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 650 GSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVE 729
Cdd:PLN02766 245 GSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 730 EVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPV 809
Cdd:PLN02766 325 KAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 810 MIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAAL 889
Cdd:PLN02766 405 MSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDAL 482
|
....*....
gi 21614513 890 NEYLRVKTV 898
Cdd:PLN02766 483 DKYLQVKSV 491
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
441-899 |
4.26e-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: 4.26e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK 520
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQGSTIPinqaRPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYP----QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 761 YCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdlDAVLSRANATEFGLAS 836
Cdd:cd07093 314 YVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21614513 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07093 392 YVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
441-898 |
6.78e-168 |
|
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: 496.06 E-value: 6.78e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPL----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07090 154 FTPLTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 761 YCQHGVKEGATLVCGGNQVP-----RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 835
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFD--TEEEVIRRANDTTYGLA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21614513 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
423-898 |
1.03e-166 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 496.25 E-value: 1.03e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLTLtrKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADG--PHHVQTL--HEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 663 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:PLN02466 295 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDA 822
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK--DLDE 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21614513 823 VLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
425-896 |
8.25e-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: 478.54 E-value: 8.25e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 505 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 664
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 744
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 745 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdl 820
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE-- 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21614513 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
419-898 |
2.09e-157 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 470.52 E-value: 2.09e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 419 RMP-HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLME 497
Cdd:PRK13252 3 RQPlQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 498 QHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQArpnrNLTLTRKEPVGVCGIIIPWNYPL 577
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGG----SFVYTRREPLGVCAGIGAWNYPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 578 MMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKH 657
Cdd:PRK13252 157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 658 IMKSCAISnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 737
Cdd:PRK13252 236 VMAAAAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 738 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR----PGFFFEPTVFTDVEDHMFIAKEESFGPVMIIS 813
Cdd:PRK13252 315 DPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 814 RFADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYL 893
Cdd:PRK13252 395 TFDDE--DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
....*
gi 21614513 894 RVKTV 898
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
424-900 |
5.44e-155 |
|
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: 463.51 E-value: 5.44e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGwcdkiQGSTIPINQARPNrnlTLTRKEPVGVCGIIIPWNYPLMMLSWK 583
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAAD-----ALKDFEFEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScA 663
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA-A 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 664 ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 743
Cdd:cd07138 230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 744 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR---PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDl 820
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 821 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07138 389 EAI-AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
472-900 |
1.40e-154 |
|
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: 461.81 E-value: 1.40e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 472 FENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIpiNQAR 551
Cdd:cd07118 32 FDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEIEGAADLWRYAASLARTLHGDSY--NNLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 552 PNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGS 631
Cdd:cd07118 109 DDM-LGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 632 LVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAG 711
Cdd:cd07118 188 TVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 712 RLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP-RPGFFFEPTV 790
Cdd:cd07118 267 RLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLAsAAGLFYQPTI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 791 FTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAA 870
Cdd:cd07118 347 FTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPEL 424
|
410 420 430
....*....|....*....|....*....|
gi 21614513 871 PFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07118 425 PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
1-203 |
1.06e-153 |
|
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: 449.59 E-value: 1.06e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647 1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08647 81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21614513 161 STLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGI 203
Cdd:cd08647 161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
442-900 |
1.54e-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: 1.54e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEnGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE-SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 522 HVGMSIQTFRYFAGWCDKIQGSTIPINQArpnrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPG----YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 602 TPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 681
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDrDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 762 CQHGVKEGATLVCGGNQV---PRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGV 838
Cdd:cd07109 314 VARARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21614513 839 FTRDINKALYVSDKLQAGTVFVNTYNKT-DVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
477-900 |
2.28e-151 |
|
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: 450.14 E-value: 2.28e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPINqarPNRNL 556
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSP---DPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:cd06534 86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 637 LSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVE 716
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 717 DSIHDEFVRRVVeevrkmkvgnpldrdtdhgpqnhhahlvklmeycqhgvkegatlvcggnqvprpgfffepTVFTDVED 796
Cdd:cd06534 245 ESIYDEFVEKLV------------------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 797 HMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK-TDVAAPFGGF 875
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGV 342
|
410 420
....*....|....*....|....*
gi 21614513 876 KQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd06534 343 KNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
420-900 |
8.55e-150 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 450.13 E-value: 8.55e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 420 MPHQLFIGGEFVDAEGAkTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQH 499
Cdd:PRK13473 1 MQTKLLINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP--EWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 500 QEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQG-----------STIpinqarpnrnltltRKEPVGVCG 568
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGkaageyleghtSMI--------------RRDPVGVVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 569 IIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGF 648
Cdd:PRK13473 144 SIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 649 TGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 728
Cdd:PRK13473 223 TGSIATGKHVLSAAA-DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 729 EEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEG-ATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFG 807
Cdd:PRK13473 302 AAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 808 PVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEA 887
Cdd:PRK13473 382 PVVSVTPFD--DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLY 459
|
490
....*....|...
gi 21614513 888 ALNEYLRVKTVTF 900
Cdd:PRK13473 460 GLEDYTVVRHVMV 472
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
424-900 |
3.81e-149 |
|
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: 448.56 E-value: 3.81e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWcdkiqGSTIPINQARP--NRNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAAL-----ARDFPFEERRPgsGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 662 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07139 235 CG-ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP--GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGD 819
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 820 lDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYnKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07139 394 -DAV-RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
.
gi 21614513 900 F 900
Cdd:cd07139 471 L 471
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
425-898 |
6.69e-149 |
|
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: 447.85 E-value: 6.69e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVdaEGAKTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07097 4 YIDGEWV--AGGDGEENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGAvyTLAL-KTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLTlTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:cd07097 80 ARLLTREEGK--TLPEaRGEVTRAGQIFRYYAGEALRLSGETLP--STRPGVEVE-TTREPLGVVGLITPWNFPIAIPAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSc 662
Cdd:cd07097 155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 663 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:cd07097 234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP--GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 820
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR--DY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDVAAPFGGFKQSGFG-KDLGEAALNEYLRVKTV 898
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
442-900 |
7.15e-148 |
|
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: 444.46 E-value: 7.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgkISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRR--TTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 522 HVGMSIQTFRYFAGWCDKIQGSTIpiNQARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAA--GEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 602 TPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKSPLI 681
Cdd:cd07092 157 TPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 762 CQhGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTR 841
Cdd:cd07092 315 VE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 842 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
425-898 |
6.52e-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: 437.47 E-value: 6.52e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 505 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLTLtRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07088 79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIP--SDRPNENIFI-FKVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 664
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 744
Cdd:cd07088 234 ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 745 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP-RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAV 823
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS--SLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 824 LSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
422-902 |
7.35e-145 |
|
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: 437.93 E-value: 7.35e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQE 501
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK--TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarpnRNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE----DTLSYHFHEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 662 cAISNVKKVSLELGGKSPLIIFAD-----CDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07559 234 -AAENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 737 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMII 812
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 813 SRFADgdLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 892
Cdd:cd07559 393 ITFKD--EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
490
....*....|
gi 21614513 893 LRVKTVTFEY 902
Cdd:cd07559 471 QQTKNILVSY 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
442-900 |
2.73e-142 |
|
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: 430.13 E-value: 2.73e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 522 HVGMSIQTFRYFAGWCDKIQGS-TIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 761 YCQHGVKEGATLVCGGNQVPR--PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFaDGDLDAVlsR-ANATEFGLASG 837
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPY-DDDDEAV--RiANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21614513 838 VFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
424-894 |
3.81e-142 |
|
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: 430.66 E-value: 3.81e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQgstipinQARPNRnltltrkEPVGVCGIIIPWNYPLMMLSWK 583
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-------TELAGW-------KPVGVVGQIVPWNFPLLMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 663
Cdd:cd07111 168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 664 ISnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 743
Cdd:cd07111 247 GT-GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 744 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAV 823
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFR--TAKEA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21614513 824 LSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 894
Cdd:cd07111 404 VALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
423-898 |
1.88e-141 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 429.50 E-value: 1.88e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPF--PDRRL-LVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 663 AiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:PLN02278 260 A-ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDA 822
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT-EEEA 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21614513 823 VLSrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PLN02278 418 IAI-ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
441-899 |
1.00e-138 |
|
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: 420.99 E-value: 1.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALk 520
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQgstipinqARPNRNLTL--------TRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGN 592
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLD--------AKAERAVPLpsedfkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 593 TVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSL 672
Cdd:cd07110 150 TVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 673 ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHH 752
Cdd:cd07110 229 ELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 753 AHLVKLMEYCQHGVKEGATLVCGGN--QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVLSrANAT 830
Cdd:cd07110 309 AQYEKVLSFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED-EAIAL-ANDS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 831 EFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07110 387 EYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
475-899 |
9.32e-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: 418.69 E-value: 9.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 475 GRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAvytlALKTH----VGMSIQTFRYFAGWCDKIQGSTIPinqA 550
Cdd:cd07108 33 PEWAATPARERGKLLARIADALEARSEELARLLALETGN----ALRTQarpeAAVLADLFRYFGGLAGELKGETLP---F 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 551 RPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSG 630
Cdd:cd07108 106 GPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEI-LAQVLPAGVLNVITGYG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 631 SLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQ---MGMSsvFFNKGENC 707
Cdd:cd07108 184 EECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGGKSPMIVFPDADLDDAVDgaiAGMR--FTRQGQSC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 708 IAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKE-GATLVCGGNQVP----RP 782
Cdd:cd07108 261 TAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPLPGegplAD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 783 GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNT 862
Cdd:cd07108 341 GFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWK--DEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ 418
|
410 420 430
....*....|....*....|....*....|....*...
gi 21614513 863 YNKTDVAAPFGGFKQSGFGKDLG-EAALNEYLRVKTVT 899
Cdd:cd07108 419 GGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVN 456
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
424-902 |
2.59e-137 |
|
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: 418.00 E-value: 2.59e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEnGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPN--RNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQgeRYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 662 cAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07113 240 -AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPT--VFTDVEDHMFiaKEESFGPVMIISRFADGd 819
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDE- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 820 lDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07113 396 -EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
...
gi 21614513 900 FEY 902
Cdd:cd07113 475 IRY 477
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
422-898 |
3.71e-134 |
|
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: 409.92 E-value: 3.71e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQE 501
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarpnRNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE----DTLSIVLREPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 662 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07117 234 AA-KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAd 817
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 818 gDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKT 897
Cdd:cd07117 392 -TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKN 470
|
.
gi 21614513 898 V 898
Cdd:cd07117 471 I 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
425-902 |
5.93e-134 |
|
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: 409.43 E-value: 5.93e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGAKTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWK 583
Cdd:cd07131 80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVP--SELPNKDA-MTRRQPIGVVALITPWNFPVAIPSWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 663
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 664 ISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 743
Cdd:cd07131 236 RPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 744 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR----PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGD 819
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV--SS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 820 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtyNKT---DVAAPFGGFKQSGFG-KDLGEAALNEYLRV 895
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEW 470
|
....*..
gi 21614513 896 KTVTFEY 902
Cdd:cd07131 471 KAVYVDY 477
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
441-899 |
1.36e-133 |
|
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: 407.53 E-value: 1.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALK 520
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07107 78 GDVMVAAALLDYFAGLVTELKGETIPV----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07107 154 QAPLSALRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA-EGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 681 IIFADCDLNKAVQ---MGMSsvFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 757
Cdd:cd07107 232 IVFPDADPEAAADaavAGMN--FTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 758 LMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgdLDAVLSRANATEFG 833
Cdd:cd07107 310 VMHYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRD--EAEMVAQANGVEYG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21614513 834 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
477-900 |
2.88e-133 |
|
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: 406.53 E-value: 2.88e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGwcdkiqgSTIP--INQARPNR 554
Cdd:cd07106 35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGGAVAWLRYTAS-------LDLPdeVIEDDDTR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 555 NLTLTRKePVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLvG 634
Cdd:cd07106 107 RVELRRK-PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGEL-AQEVLPPGVLNVVSGGDEL-G 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 635 QRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAV-QMGMSSvFFNKGENCIAAGRL 713
Cdd:cd07106 184 PALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPDVDIDAVApKLFWGA-FINSGQVCAAIKRL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 714 FVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTD 793
Cdd:cd07106 262 YVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 794 VEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFG 873
Cdd:cd07106 342 PPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFG 419
|
410 420
....*....|....*....|....*..
gi 21614513 874 GFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07106 420 GHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
423-898 |
3.31e-132 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 405.43 E-value: 3.31e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:PRK09847 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS----SHELAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 663 AISNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:PRK09847 257 GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGfFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdGDLD 821
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFT-SEEQ 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21614513 822 AvLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PRK09847 414 A-LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
440-900 |
5.16e-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: 403.51 E-value: 5.16e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL 519
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 520 KtHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07149 80 K-EVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 599 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHImksCAISNVKKVSLELGGKS 678
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI---ARKAGLKKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 679 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 758
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 759 MEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGV 838
Cdd:cd07149 316 EEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD--TLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 839 FTRDINKALYVSDKLQAGTVFVN---TYnKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINdssTF-RVD-HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
443-899 |
3.86e-128 |
|
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: 393.23 E-value: 3.86e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 443 NPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL-KT 521
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWfET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 522 HVGMSIqtFRYFAGWCDKIQGSTIPinQARPNRnLTLTRKEPVGVCGIIIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQ 600
Cdd:cd07150 83 TFTPEL--LRAAAGECRRVRGETLP--SDSPGT-VSMSVRRPLGVVAGITPFNYPLI-LATKKVAfALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 761 YCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAvLSRANATEFGLASGVFT 840
Cdd:cd07150 316 QVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKD-AEEA-LELANDTEYGLSAAILT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 841 RDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
477-899 |
3.52e-127 |
|
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: 389.97 E-value: 3.52e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYtlaLKTH--VGMSIQTFRYFAGWCDKIQGSTIPinQARPNR 554
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR---PKAAfeVGAAIAILREAAGLPRRPEGEILP--SDVPGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 555 nLTLTRKEPVGVCGIIIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQVTPLT-ALKFAELTLKAGIPKGVVNVLPGSGSL 632
Cdd:cd07104 91 -ESMVRRVPLGVVGVISPFNFPLI-LAMRSVApALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 633 VGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGR 712
Cdd:cd07104 169 IGDALVEHPRVRMISFTGSTAVGRHIGELAG-RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 713 LFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqvPRPGFFFEPTVFT 792
Cdd:cd07104 248 ILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYEGLFYQPTVLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 793 DVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKtDVAA 870
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDD-DEEAV-ELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdqTVND-EPHV 401
|
410 420
....*....|....*....|....*....
gi 21614513 871 PFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07104 402 PFGGVKASGGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
440-898 |
5.91e-127 |
|
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: 390.56 E-value: 5.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAl 519
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 520 KTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07145 79 RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 599 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKS 678
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 679 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 758
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 759 MEYCQHGVKEGATLVCGGNQVprPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLASGV 838
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDE-EAV-EIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21614513 839 FTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
423-899 |
2.83e-125 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 387.94 E-value: 2.83e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGR---WGKISARDRGRLMYRLADLMEQH 499
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKgkdWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 500 QEELATIEALDAGAVYTLALKTHVGMSiQTFRYFAGWCDKIQGS-----TIPINQARPNrnltlTRKEPVGVCGIIIPWN 574
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVA-GCFEYYADLAEALDAKqkapvSLPMETFKGY-----VLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 575 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEV 654
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 655 GKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKM 734
Cdd:PLN02467 243 GRKIMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 735 KVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGN--QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMII 812
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 813 SRFADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 892
Cdd:PLN02467 402 KTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENY 479
|
....*..
gi 21614513 893 LRVKTVT 899
Cdd:PLN02467 480 LSVKQVT 486
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
441-899 |
1.05e-119 |
|
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: 371.68 E-value: 1.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQGSTIpinQARPNrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMI---EPEPG-SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 601 VTPLTALKFAELTLKA-GIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSP 679
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 680 LIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLM 759
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 760 EYCQHGVKEGATLVCGGNQVPR---PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLAS 836
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA-EAV-ALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21614513 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
425-902 |
9.88e-117 |
|
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: 364.58 E-value: 9.88e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAeGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 505 TIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07086 79 RLVSLEMGKILPEGL-GEVQEMIDICDYAVGLSRMLYGLTIP--SERPGHRL-MEQWNPLGVVGVITAFNFPVAVPGWNA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKA----GIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07086 155 AIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 661 SCAISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:cd07086 234 TVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR--PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadG 818
Cdd:cd07086 313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF--D 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 819 DLDAVLSRANATEFGLASGVFTRDINKAL-YVSDK-LQAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRV 895
Cdd:cd07086 391 SLEEAIAINNDVPQGLSSSIFTEDLREAFrWLGPKgSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRR 470
|
....*..
gi 21614513 896 KTVTFEY 902
Cdd:cd07086 471 STCTINY 477
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
422-896 |
1.76e-116 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 364.23 E-value: 1.76e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQE 501
Cdd:PRK11241 11 QQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 502 ELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLtLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:PRK11241 89 DLARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQ--ADKRL-IVIKQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 662 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:PRK11241 245 CA-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLD 821
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF--KDEA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 822 AVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
477-898 |
2.99e-114 |
|
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: 356.38 E-value: 2.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAgwcDKI----QGSTIPINQARp 552
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYA---ENAeaflADEPIETDAGK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 553 nrnlTLTRKEPVGVCGIIIPWNYPLmmlsWKT----AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPG 628
Cdd:cd07100 90 ----AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 629 SGSLVGQrLSDHPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCI 708
Cdd:cd07100 162 DSDQVEA-IIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 709 AAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEP 788
Cdd:cd07100 240 AAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 789 TVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAV-LsrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTD 867
Cdd:cd07100 320 TVLTDVTPGMPAYDEELFGPVAAVIKVKDEE-EAIaL--ANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSD 396
|
410 420 430
....*....|....*....|....*....|.
gi 21614513 868 VAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07100 397 PRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
440-900 |
2.52e-111 |
|
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: 349.42 E-value: 2.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL 519
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 520 KtHVGMSIQTFRYFAGWCDKIQGSTIP--INQARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIK 597
Cdd:cd07094 80 V-EVDRAIDTLRLAAEEAERIRGEEIPldATQGSDNR-LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 598 PAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMkscAISNVKKVSLELGGK 677
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALR---ANAGGKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 678 SPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 757
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 758 LMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASG 837
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 838 VFTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNdsSAFRTD-WMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
425-902 |
1.68e-110 |
|
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: 348.29 E-value: 1.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE--AWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 505 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEID----ENTVAYHFHEPLGVVGQIIPWNFPLLMATWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAI 664
Cdd:cd07116 158 APALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY-AS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 665 SNVKKVSLELGGKSPLIIFADCD------LNKAVQmGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGN 738
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFADVMdaddafFDKALE-GFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 739 PLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDvEDHMFIAKEESFGPVMIISR 814
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGgllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 815 FAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 894
Cdd:cd07116 394 FK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
....*...
gi 21614513 895 VKTVTFEY 902
Cdd:cd07116 472 TKNLLVSY 479
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
428-899 |
2.93e-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: 2.93e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 428 GEFVDAEGAKTSETINPTDGSVICQVSLAqvTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIE 507
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAA--SKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 508 ALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPIN-QARPNRnltlTRKEPVGVCGIIIPWNYPLMMLSWKTAA 586
Cdd:cd07151 79 IRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvPGKENR----VYREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 587 CLAAGNTVVIKPAQVTPLTA-LKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiS 665
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG-R 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 666 NVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTD 745
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 746 HGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqvPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFaDGDLDAVlS 825
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKA-DDEEEAL-E 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 826 RANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
424-899 |
5.80e-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: 337.27 E-value: 5.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGakTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07124 35 LVIGGKEVRTEE--KIESRNPADPSeVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGStiPINQARPNRNLTltRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:cd07124 111 LAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNRY--VYRPLGVGAVISPWNFPLAILAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:cd07124 186 MTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 663 A-----ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 737
Cdd:cd07124 266 AkvqpgQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 738 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNqVPRP---GFFFEPTVFTDVEDHMFIAKEESFGPVMIISR 814
Cdd:cd07124 346 DPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE-VLELaaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 815 FAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG-KDLGEA 887
Cdd:cd07124 424 AK--DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVG----NLYaNRKITGAlvgrqPFGGFKMSGTGsKAGGPD 497
|
490
....*....|..
gi 21614513 888 ALNEYLRVKTVT 899
Cdd:cd07124 498 YLLQFMQPKTVT 509
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
477-899 |
2.24e-105 |
|
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: 333.80 E-value: 2.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKI-QGSTIPINQARPNRN 555
Cdd:cd07099 34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVLLALEAIDWAARNAPRVlAPRKVPTGLLMPNKK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 556 LTLTRkEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQ 635
Cdd:cd07099 113 ATVEY-RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 636 RLSDHPdVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07099 191 ALIDAG-VDKVAFTGSVATGRKVMAAAA-ERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 716 EDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVE 795
Cdd:cd07099 269 HESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFG 873
Cdd:cd07099 349 HDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdvLLTAGIPALPFG 426
|
410 420
....*....|....*....|....*.
gi 21614513 874 GFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07099 427 GVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
489-902 |
1.68e-102 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 324.77 E-value: 1.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 489 MYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINqaRPNRNLtLTRKEPVGVCG 568
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSD--RPGENI-LLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 569 IIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGF 648
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 649 TGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 728
Cdd:PRK10090 157 TGSVSAGEKIMAAAA-KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 729 EEVRKMKVGNPLDRDT-DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFG 807
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 808 PVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEA 887
Cdd:PRK10090 316 PVLPVVAFD--TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393
|
410
....*....|....*
gi 21614513 888 ALNEYLRVKTVTFEY 902
Cdd:PRK10090 394 GLHEYLQTQVVYLQS 408
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
423-899 |
2.20e-102 |
|
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: 326.78 E-value: 2.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNlTLTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:cd07085 80 LARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLE--NVARGID-TYSYRQPLGVVAGITPFNFPAMIPLW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVgQRLSDHPDVRKIGFTGSTEVGKHIMKSc 662
Cdd:cd07085 156 MFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYER- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 663 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:cd07085 234 AAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRfADg 818
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR-VD- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 819 DLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynkTDVAAP-----FGGFKQSGFGkDL---GEAALN 890
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLhfyGKDGVR 466
|
....*....
gi 21614513 891 EYLRVKTVT 899
Cdd:cd07085 467 FYTQTKTVT 475
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
440-896 |
5.29e-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: 324.97 E-value: 5.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAl 519
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMR--ALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 520 KTHVGMSIQTFRYFAGWCDKIQGSTIPIN-QARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07147 79 RGEVARAIDTFRIAAEEATRIYGEVLPLDiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 599 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAisnVKKVSLELGGKS 678
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAG---KKKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 679 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 758
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 759 MEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGV 838
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21614513 839 FTRDINKALYVSDKLQAGTVFVNtynktDV------AAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVIN-----DVptfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
476-899 |
1.05e-99 |
|
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: 318.87 E-value: 1.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 476 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK--THVGMsiqTFRYFAGWCDKI-----QGSTIPIn 548
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEevLDVAI---VARYYARRAERLlkprrRRGAIPV- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 549 qarpnrnLTLTR--KEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL 626
Cdd:cd07101 109 -------LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 627 PGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGEN 706
Cdd:cd07101 182 TGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 707 CIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPG-FF 785
Cdd:cd07101 259 CVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGpYF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 786 FEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN---- 861
Cdd:cd07101 339 YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDD-EAI-ELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegya 416
|
410 420 430
....*....|....*....|....*....|....*....
gi 21614513 862 -TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07101 417 aAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
477-900 |
1.04e-98 |
|
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: 315.67 E-value: 1.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRnL 556
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA-GFNVDLAAGMLREAASLITQIIGGSIP--SDKPGT-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL---PGSGSLV 633
Cdd:cd07105 92 AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 634 GQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRL 713
Cdd:cd07105 172 VEALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 714 FVEDSIHDEFVRRVVEEVRKMKVGnpldrDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP-GFFFEPTVFT 792
Cdd:cd07105 251 IVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPsGTSMPPTILD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 793 DVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-AP 871
Cdd:cd07105 326 NVTPDMDIYSEESFGPVVSIIRVKD-EEEAV-RIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEPtLP 403
|
410 420
....*....|....*....|....*....
gi 21614513 872 FGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07105 404 HGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
424-899 |
1.61e-96 |
|
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: 312.57 E-value: 1.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAKTSetINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:TIGR01237 35 LVINGERVETENKIVS--INPCDKSeVVGTVSKASQEHAEHALQAAAKAFEA--WKKTDPEERAAILFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTiPINQARPNRNLTLTrkEPVGVCGIIIPWNYPLMMLSW 582
Cdd:TIGR01237 111 FSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGK-PVNSREGETNQYVY--TPTGVTVVISPWNFPFAIMVG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:TIGR01237 187 MTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 663 AI-----SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 737
Cdd:TIGR01237 267 AKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 738 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAd 817
Cdd:TIGR01237 347 PPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 818 gDLDAVLSRANATEFGLASGVFTRD---INKAlyvSDKLQAGTVFvntYNKTDVAA-----PFGGFKQSGFG-KDLGEAA 888
Cdd:TIGR01237 425 -DFDEALEIANNTEYGLTGGVISNNrdhINRA---KAEFEVGNLY---FNRNITGAivgyqPFGGFKMSGTDsKAGGPDY 497
|
490
....*....|.
gi 21614513 889 LNEYLRVKTVT 899
Cdd:TIGR01237 498 LALFMQAKTVT 508
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
476-899 |
1.38e-95 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 310.27 E-value: 1.38e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 476 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK--THVGMsiqTFRYFAGWCDKI-----QGSTIPIn 548
Cdd:PRK09407 69 AWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEevLDVAL---TARYYARRAPKLlaprrRAGALPV- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 549 qarpnrnLTLTR--KEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL 626
Cdd:PRK09407 145 -------LTKTTelRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 627 PGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGEN 706
Cdd:PRK09407 218 TGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAG-RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 707 CIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqVPRP--G- 783
Cdd:PRK09407 295 CISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGG--KARPdlGp 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 784 FFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-- 861
Cdd:PRK09407 373 LFYEPTVLTGVTPDMELAREETFGPVVSVYPVA--DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeg 450
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 21614513 862 ---TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:PRK09407 451 yaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
477-888 |
2.75e-94 |
|
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: 304.22 E-value: 2.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVytlALKTH--VGMSIQTFRYFAGWCDKIQGSTIPINQARpnr 554
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSI---RPKAGfeVGAAIGELHEAAGLPTQPQGEILPSAPGR--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 555 nLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTA-LKFAELTLKAGIPKGVVNVLPGsGSLV 633
Cdd:cd07152 103 -LSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GADA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 634 GQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRL 713
Cdd:cd07152 181 GEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 714 FVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTD 793
Cdd:cd07152 260 LVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YDGLFYRPTVLSG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 794 VEDHMFIAKEESFGPVMIISRFADGDLDAVLsrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKtDVAAP 871
Cdd:cd07152 337 VKPGMPAFDEEIFGPVAPVTVFDSDEEAVAL--ANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdqTVND-EPHNP 413
|
410
....*....|....*..
gi 21614513 872 FGGFKQSGFGKDLGEAA 888
Cdd:cd07152 414 FGGMGASGNGSRFGGPA 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
425-881 |
6.36e-94 |
|
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: 304.11 E-value: 6.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGaKTSETINPTDGSVICQVSLaqvTDVDKAVAAAKDAFENGRWGK--ISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07082 5 LINGEWKESSG-KTIEVYSPIDGEVIGSVPA---LSALEILEAAETAYDAGRGWWptMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07082 81 VANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKs 661
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 662 caISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07082 239 --QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 742 RDTDHGP---QNHHAHLVKLMEycqHGVKEGATLVCGGNQvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdg 818
Cdd:cd07082 317 NGVDITPlidPKSADFVEGLID---DAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN-- 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 819 DLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK--TDVaAPFGGFKQSGFG 881
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgPDH-FPFLGRKDSGIG 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
424-879 |
2.98e-93 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 303.78 E-value: 2.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAKTSetINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PRK03137 39 LIIGGERITTEDKIVS--INPANKSeVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKI-QGStiPINQaRPNRNLTLtRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:PRK03137 115 FSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGK--PVES-RPGEHNRY-FYIPLGVGVVISPWNFPFAIMA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:PRK03137 190 GMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYER 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 662 CAISN-----VKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:PRK03137 270 AAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 737 GNPLDrDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 816
Cdd:PRK03137 350 GNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21614513 817 dgDLDAVLSRANATEFGLASGVFTRD---INKA--------LYVSDKLQAGTVFVNtynktdvaaPFGGFKQSG 879
Cdd:PRK03137 428 --DFDHALEIANNTEYGLTGAVISNNrehLEKArrefhvgnLYFNRGCTGAIVGYH---------PFGGFNMSG 490
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
477-900 |
1.07e-91 |
|
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: 298.06 E-value: 1.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavytlalKTHVGMS---IQTFryfagwCDKIQ-----GSTIPIN 548
Cdd:cd07098 34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG-------KTMVDASlgeILVT------CEKIRwtlkhGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 549 QARPNRNLTLTRK-----EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKA----GIP 619
Cdd:cd07098 101 ESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 620 KGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKsCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSV 699
Cdd:cd07098 181 PDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMA-AAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 700 FFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQV 779
Cdd:cd07098 259 FQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 780 PRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQA 855
Cdd:cd07098 339 PHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASD-DEEAV-EIANSTEYGLGASVFGKDIKRARRIASQLET 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 21614513 856 GTVFVNTYNKT--DVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07098 417 GMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
440-899 |
8.74e-91 |
|
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: 295.04 E-value: 8.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 440 ETINPTDGSVIcqvslAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavytLAL 519
Cdd:cd07146 2 EVRNPYTGEVV-----GTVPAGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESG----LCL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 520 KT---HVGMSIQTFRYFAGWCDKIQGSTIPINQARP-NRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVV 595
Cdd:cd07146 73 KDtryEVGRAADVLRFAAAEALRDDGESFSCDLTANgKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 596 IKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHImksCAISNVKKVSLELG 675
Cdd:cd07146 153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 676 GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 755
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 756 VKLMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 835
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21614513 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLG-EAALNEYLRVKTVT 899
Cdd:cd07146 385 SGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGGKEGvREAMKEMTNVKTYS 450
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
442-900 |
1.23e-84 |
|
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: 278.75 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 522 HVGMsIQTFRYFAGWCDKIQGSTIPINQARPNRNLtltRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07102 79 IRGM-LERARYMISIAEEALADIRVPEKDGFERYI---RREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 602 TPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 681
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAA-GRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 762 CQHGVKEGATLVCGGNQVPRP---GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAVLsRANATEFGLASGV 838
Cdd:cd07102 313 IADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKS-DAEAIA-LMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21614513 839 FTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
441-898 |
1.09e-82 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 273.92 E-value: 1.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYR--TTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSIQTFRYFAGWCDKIQGSTiPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLmmlsWKT----AACLAAGNTVVI 596
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADE-PADAAAVGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 597 KPAQVTPLTALKFAELTLKAGIPKGV-VNVLPGSGSlVGQRLSDhPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELG 675
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCfQTLLVGSGA-VEAILRD-PRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 676 GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 755
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 756 VKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 835
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVA--DIDEAIEIANATTFGLG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21614513 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
424-881 |
4.38e-78 |
|
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: 263.29 E-value: 4.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAktsETINPTDG-SVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07125 36 IINGEETETGEGA---PVIDPADHeRTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 503 LATIEALDAGAvyTLAlKTHVGMS--IQTFRYFAGWCDKIQGSTIPINQARPNRNLTLtrkEPVGVCGIIIPWNYPLMML 580
Cdd:cd07125 111 LIALAAAEAGK--TLA-DADAEVReaIDFCRYYAAQARELFSDPELPGPTGELNGLEL---HGRGVFVCISPWNFPLAIF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07125 185 TGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 661 SCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGN 738
Cdd:cd07125 265 ALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 739 PLDRDTDHGP-------QNHHAHlvklmeyCQHGVKEgATLVCggnQVPRP---GFFFEPTVFTDVEDhmFIAKEESFGP 808
Cdd:cd07125 345 PWDLSTDVGPlidkpagKLLRAH-------TELMRGE-AWLIA---PAPLDdgnGYFVAPGIIEIVGI--FDLTTEVFGP 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 809 VMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG 881
Cdd:cd07125 412 ILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYiNRNITGAivgrqPFGGWGLSGTG 486
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
1-309 |
4.77e-77 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 253.49 E-value: 4.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:COG0223 1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:COG0223 76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:COG0223 156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 235 TEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPGVVTKAG----LILFGndDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:COG0223 235 TTLDGKRLKIWKARV-----------LEEAGGGAPGTILAVDkdglLVACG--DGALRLLELQPAGKKRMSAADFLRGY 300
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
416-899 |
1.72e-73 |
|
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: 250.19 E-value: 1.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 416 RTVRMPH-QLFIGGEFVDAEGAKTSetINPTD-GSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLA 493
Cdd:cd07083 12 KEEFGRAyPLVIGGEWVDTKERMVS--VSPFApSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 494 DLMEQHQEELATIEALDAGAVYTLALKThVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCgiIIPW 573
Cdd:cd07083 88 DLLRRRRRELIATLTYEVGKNWVEAIDD-VAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVV--ISPW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 574 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTE 653
Cdd:cd07083 165 NFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 654 VGKHIMKSCA-----ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 728
Cdd:cd07083 245 TGKKIYEAAArlapgQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 729 EEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGP 808
Cdd:cd07083 325 KRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 809 VMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAA--PFGGFKQSGFG-KDLG 885
Cdd:cd07083 404 VLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGTNaKTGG 483
|
490
....*....|....
gi 21614513 886 EAALNEYLRVKTVT 899
Cdd:cd07083 484 PHYLRRFLEMKAVA 497
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
435-902 |
3.62e-72 |
|
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: 245.58 E-value: 3.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 435 GAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAV 514
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 515 YTLAL----------KTHVGMSIQtfryfagwcdkIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07130 88 LPEGLgevqemidicDFAVGLSRQ-----------LYGLTIP--SERPGHRM-MEQWNPLGVVGVITAFNFPVAVWGWNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 585 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 661 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQmgmsSVFF----NKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07130 233 AVA-ARFGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 737 GNPLDRDTDHGPQnHHAHLVKLMEYC-QHGVKEGATLVCGGNQVPRPGFFFEPTVFTdVEDHMFIAKEESFGPVMIISRF 815
Cdd:cd07130 308 GDPLDDGTLVGPL-HTKAAVDNYLAAiEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 816 AdgDLDAVLSRANATEFGLASGVFTRDINKAL-----YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAAL 889
Cdd:cd07130 386 D--TLEEAIAWNNEVPQGLSSSIFTTDLRNAFrwlgpKGSD---CGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAW 460
|
490
....*....|...
gi 21614513 890 NEYLRVKTVTFEY 902
Cdd:cd07130 461 KQYMRRSTCTINY 473
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
1-180 |
2.56e-66 |
|
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: 219.47 E-value: 2.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 1 MKIAVI--GQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGA 78
Cdd:pfam00551 1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 79 ELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDD 158
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|..
gi 21614513 159 TVSTLYNRFLFPEGiKGMVQAV 180
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
441-898 |
7.70e-66 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 228.21 E-value: 7.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 521 THVGMSiqtfryfAGWCDKIQGSTIPINQARPN---RNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIK 597
Cdd:PRK13968 88 AEVAKS-------ANLCDWYAEHGPAMLKAEPTlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 598 PAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDhPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELGGK 677
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 678 SPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 757
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 758 LMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISrfADGDLDAVLSRANATEFGLASG 837
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAIT--VAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21614513 838 VFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
440-881 |
1.77e-62 |
|
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: 218.44 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEN-GRWgkISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLA 518
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 519 lKTHVGMSIQTFRYFAGWCDKIQGSTIPIN--QARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVI 596
Cdd:cd07148 80 -KVEVTRAIDGVELAADELGQLGGREIPMGltPASAGR-IAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 597 KPAQVTPLTALKFAELTLKAGIPKGVVNVLPgSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNvkKVSLELGG 676
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 677 KSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLV 756
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 757 KLMEYCQHGVKEGATLVCGGNQVPRPgfFFEPTVFTDVEDHMFIAKEESFGPVMIIsrFADGDLDAVLSRANATEFGLAS 836
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCV--YSYDDLDEAIAQANSLPVAFQA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 21614513 837 GVFTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFG 881
Cdd:cd07148 391 AVFTKDLDVALKAVRRLDATAVMVNdhTAFRVD-WMPFAGRRQSGYG 436
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
560-886 |
7.85e-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: 210.55 E-value: 7.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVnVLPGsGSLVGQRLSD 639
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DAEVAQALLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 640 HPdVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSI 719
Cdd:cd07134 175 LP-FDHIFFTGSPAVGKIVMAAAA-KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 720 HDEFVRRVVEEVRKMKVGNPLDRDTDHGP----QNHHAHLVKLMEycqHGVKEGATLVCGGnQVPRPGFFFEPTVFTDVE 795
Cdd:cd07134 253 KDAFVEHLKAEIEKFYGKDAARKASPDLArivnDRHFDRLKGLLD---DAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA----- 870
Cdd:cd07134 329 PDMKIMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-----DVVLhflnp 401
|
330
....*....|....*...
gi 21614513 871 --PFGGFKQSGFGKDLGE 886
Cdd:cd07134 402 nlPFGGVNNSGIGSYHGV 419
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
560-898 |
9.78e-59 |
|
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: 206.99 E-value: 9.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSlVGQRLSD 639
Cdd:cd07087 97 IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-VATALLA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 640 HP-DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDS 718
Cdd:cd07087 175 EPfD--HIFFTGSPAVGKIVMEAAA-KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 719 IHDEFVRRVVEEVRKMkVGNPLDRDTDHGPQNHHAHLVKLMEYcqhgvKEGATLVCGGnQVPRPGFFFEPTVFTDVEDHM 798
Cdd:cd07087 252 IKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASL-----LDDGKVVIGG-QVDKEERYIAPTILDDVSPDS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 799 FIAKEESFGPVM-IISRfadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynktDV-------AA 870
Cdd:cd07087 325 PLMQEEIFGPILpILTY---DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN-----DVllhaaipNL 396
|
330 340
....*....|....*....|....*...
gi 21614513 871 PFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07087 397 PFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
477-879 |
2.62e-58 |
|
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: 205.97 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGA--------VYTLALKthVGMSIQTFRYFAGwcDKiqgsTIPIN 548
Cdd:cd07095 16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqteVAAMAGK--IDISIKAYHERTG--ER----ATPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 549 QARpnrnlTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPG 628
Cdd:cd07095 88 QGR-----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 629 SGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCI 708
Cdd:cd07095 163 GRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 709 AAGRLFVEDS-IHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFE 787
Cdd:cd07095 242 CARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 788 PTVF--TDVEDHmfiAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDinKALY--VSDKLQAGTVFVN-T 862
Cdd:cd07095 322 PGIIdvTDAADV---PDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDD--EALFerFLARIRAGIVNWNrP 394
|
410
....*....|....*..
gi 21614513 863 YNKTDVAAPFGGFKQSG 879
Cdd:cd07095 395 TTGASSTAPFGGVGLSG 411
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
425-881 |
4.39e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 203.89 E-value: 4.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGAKTsETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:PRK11904 551 WQAGPIINGEGEAR-PVVSPADRRrVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAEL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGavytlalKT-HVGMS-----IQTFRYFAgwcdkiqgstipiNQARpnRNLTLTRKEP-------------- 563
Cdd:PRK11904 628 IALCVREAG-------KTlQDAIAevreaVDFCRYYA-------------AQAR--RLFGAPEKLPgptgesnelrlhgr 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 564 -VGVCgiIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPD 642
Cdd:PRK11904 686 gVFVC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPR 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 643 VRKIGFTGSTEVGKHI-----MKSCAIsnvkkVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:PRK11904 764 IAGVAFTGSTETARIInrtlaARDGPI-----VPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFV 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 716 EDSIHDefvrRVVE----EVRKMKVGNPLDRDTDHGP---QNHHAhlvKLMEYCQHgVKEGATLVCggnQVPRP-----G 783
Cdd:PRK11904 839 QEDIAD----RVIEmlkgAMAELKVGDPRLLSTDVGPvidAEAKA---NLDAHIER-MKREARLLA---QLPLPagtenG 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 784 FFFEPTVFtdvE-DHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVnt 862
Cdd:PRK11904 908 HFVAPTAF---EiDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYV-- 982
|
490 500
....*....|....*....|....
gi 21614513 863 yNKTDVAA-----PFGGFKQSGFG 881
Cdd:PRK11904 983 -NRNQIGAvvgvqPFGGQGLSGTG 1005
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
477-885 |
1.12e-53 |
|
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: 195.13 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAgwcdkiqgstipiNQARpnRNL 556
Cdd:TIGR01238 90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI-AEVREAVDFCRYYA-------------KQVR--DVL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:TIGR01238 154 GEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 637 LSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLF 714
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLC 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 715 VEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGP-------QNHHAHLVKlMEYCQHGVKEgatLVCGGNQVPRPGFFFE 787
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPvidaeakQNLLAHIEH-MSQTQKKIAQ---LTLDDSRACQHGTFVA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 788 PTVFTdvEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTD 867
Cdd:TIGR01238 390 PTLFE--LDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYV---NRNQ 464
|
410 420
....*....|....*....|...
gi 21614513 868 VAA-----PFGGFKQSGFGKDLG 885
Cdd:TIGR01238 465 VGAvvgvqPFGGQGLSGTGPKAG 487
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
477-881 |
5.95e-52 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 198.17 E-value: 5.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAgwcdkiqgstipiNQARpnRNL 556
Cdd:PRK11905 606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAI-AEVREAVDFLRYYA-------------AQAR--RLL 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:PRK11905 670 NGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 637 LSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLF 714
Cdd:PRK11905 750 LVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLC 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 715 VEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLvcggNQVPRP-----GFFFEPT 789
Cdd:PRK11905 830 LQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPaetekGTFVAPT 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 790 VFtDVEDhmfIA--KEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTD 867
Cdd:PRK11905 906 LI-EIDS---ISdlEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYV---NRNI 978
|
410
....*....|....*....
gi 21614513 868 VAA-----PFGGFKQSGFG 881
Cdd:PRK11905 979 IGAvvgvqPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
476-881 |
9.23e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 197.47 E-value: 9.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 476 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAG------------AVytlalkthvgmsiqTF-RYFAgwcdkiqg 542
Cdd:COG4230 608 AWSATPVEERAAILERAADLLEAHRAELMALLVREAGktlpdaiaevreAV--------------DFcRYYA-------- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 543 stipiNQARpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGV 622
Cdd:COG4230 666 -----AQAR-RLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADV 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 623 VNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLI---------IFADCdlnka 691
Cdd:COG4230 740 LQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIvdssalpeqVVDDV----- 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 692 vqmgMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGP------QNhhahlvKLMEYCQHG 765
Cdd:COG4230 815 ----LASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPvidaeaRA------NLEAHIERM 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 766 VKEGATLVcggnQVPRP-----GFFFEPTVF--TDVEDhmfiAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGV 838
Cdd:COG4230 885 RAEGRLVH----QLPLPeecanGTFVAPTLIeiDSISD----LEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGV 956
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 21614513 839 FTRdINK-ALYVSDKLQAGTVFVntyNKTDVAA-----PFGGFKQSGFG 881
Cdd:COG4230 957 HSR-IDEtIDRVAARARVGNVYV---NRNIIGAvvgvqPFGGEGLSGTG 1001
|
|
| FDH_Hydrolase_C |
cd08703 |
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ... |
206-306 |
3.64e-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: 174.46 E-value: 3.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 206 KETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDK 285
Cdd:cd08703 1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGK 79
|
90 100
....*....|....*....|.
gi 21614513 286 MLLVKNIQLEDGKMILASNFF 306
Cdd:cd08703 80 MVNVKRLQFEDGKMIPASKYG 100
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
3-182 |
2.53e-50 |
|
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: 174.78 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 3 IAVIGQSLFGQEVYCHLR-KEGHEVVGVFTVPDKDGKADPLGLEAEKDGVpvfkysrWRAKGQALPDVVAKYQALGAELN 81
Cdd:cd08369 1 IVILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSPRGTAQLSLELVGGKV-------YLDSNINTPELLELLKEFAPDLI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 82 VLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVS 161
Cdd:cd08369 74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAG 153
|
170 180
....*....|....*....|.
gi 21614513 162 TLYNRfLFPEGIKGMVQAVRL 182
Cdd:cd08369 154 TLYQR-LIELGPKLLKEALQK 173
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
481-881 |
2.68e-50 |
|
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: 183.46 E-value: 2.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 481 SARDRGRLMYRLADLMEQHQEELAtiEALDA-----GAVYTLALKthVGMSIQTFRY----FAGWCdkiqgstipinqaR 551
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALA--EAISAdfghrSRHETLLAE--ILPSIAGIKHarkhLKKWM-------------K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 552 PNR---NLTLT------RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGV 622
Cdd:cd07133 81 PSRrhvGLLFLpakaevEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 623 VNVLPGsGSLVGQRLS----DHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSS 698
Cdd:cd07133 160 VAVVTG-GADVAAAFSslpfDH-----LLFTGSTAVGRHVMRAAA-ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 699 VFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKM---KVGNPldrdtDHGPQNHHAHLVKLMEYCQHGVKEGATLV-C 774
Cdd:cd07133 233 KLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 775 GGNQVPRPGF-FFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKL 853
Cdd:cd07133 308 NPAGEDFAATrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385
|
410 420 430
....*....|....*....|....*....|....*
gi 21614513 854 QAGTVFVNtynktDVA-------APFGGFKQSGFG 881
Cdd:cd07133 386 HSGGVTIN-----DTLlhvaqddLPFGGVGASGMG 415
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
425-881 |
1.12e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 183.42 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFVDAEGAKTSETINPTDGSVicQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKT--QYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 505 tiEALdagaVYTLA-----LKTHVGMSIQTFRYFA-------GWCDKIQGSTIPINQarpnRN-LTLTRKEPVGVCGIII 571
Cdd:PLN00412 97 --ECL----VKEIAkpakdAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNE----RNkYCLTSKIPLGVVLAIP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 572 PWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGS 651
Cdd:PLN00412 167 PFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 652 tEVGKHIMKSCAISNVKkvsLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEV 731
Cdd:PLN00412 247 -DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 732 RKMKVGNPLDrDTDHGP------QNHHAHLVKlmeycqHGVKEGATLVcggNQVPRPGFFFEPTVFTDVEDHMFIAKEES 805
Cdd:PLN00412 323 AKLTVGPPED-DCDITPvvsessANFIEGLVM------DAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEP 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21614513 806 FGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTY-NKTDVAAPFGGFKQSGFG 881
Cdd:PLN00412 393 FGPVLPVIRI--NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIG 467
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
1-310 |
1.26e-49 |
|
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: 177.98 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDG------KADPLGLEAEKDGVPVFKYsrwraKGQALPDVVAKYQ 74
Cdd:TIGR00460 1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP-----EKQRQLEELPLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:TIGR00460 76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:TIGR00460 156 EEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 235 TEACEQKLTFFnstlntsglvpEGDALPIPG-AHRPGVV---TKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAA 310
Cdd:TIGR00460 235 LTFEGKNIKIH-----------KAKVIDLSTyKAKPGEIvyhNKKGILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSR 303
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
560-898 |
3.58e-49 |
|
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: 180.49 E-value: 3.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPG----SGSLVGQ 635
Cdd:cd07135 105 RKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGgvpeTTALLEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 636 RLSdhpdvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07135 184 KFD------KIFYTGSGRVGRIIAEAAA-KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 716 EDSIHDEFVRRVVEEVRKMkVGNPLDRDTDHG---PQNHHAHLVKLMEycqhgvKEGATLVCGG--NQVPRpgfFFEPTV 790
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEF-YPGGANASPDYTrivNPRHFNRLKSLLD------TTKGKVVIGGemDEATR---FIPPTI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 791 FTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDV- 868
Cdd:cd07135 327 VSDVSWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVd 404
|
330 340 350
....*....|....*....|....*....|
gi 21614513 869 AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07135 405 NAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
560-898 |
4.08e-49 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 181.77 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGsGSLVGQRLSD 639
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 640 HP-DVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDS 718
Cdd:PTZ00381 184 EPfDH--IFFTGSPRVGKLVMQAAA-ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 719 IHDEFVRRVVEEVRKMKVGNPLdRDTDHGPQNHHAHLVKLME-YCQHGVKegatLVCGGnQVPRPGFFFEPTVFTDVEDH 797
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPK-KSEDYSRIVNEFHTKRLAElIKDHGGK----VVYGG-EVDIENKYVAPTIIVNPDLD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 798 MFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFGGF 875
Cdd:PTZ00381 335 SPLMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGV 412
|
330 340
....*....|....*....|...
gi 21614513 876 KQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPV 435
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
419-902 |
5.24e-49 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 183.79 E-value: 5.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 419 RMPHqlFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQ 498
Cdd:PLN02419 113 RVPN--LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 499 HQEELATIEALDAGAVytlaLKTHVGMSIQTFRYFAGWCDKiqgSTIPINQARPNRNL---TLTRKEPVGVCGIIIPWNY 575
Cdd:PLN02419 189 NMDKLAMNITTEQGKT----LKDSHGDIFRGLEVVEHACGM---ATLQMGEYLPNVSNgvdTYSIREPLGVCAGICPFNF 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 576 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQrLSDHPDVRKIGFTGSTEVG 655
Cdd:PLN02419 262 PAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 656 KHIMKSCAISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGR-LFVEDSihDEFVRRVVEEVRKM 734
Cdd:PLN02419 341 MHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERAKAL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 735 KVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGF----FFEPTVFTDVEDHMFIAKEESFGPVM 810
Cdd:PLN02419 418 KVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVL 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 811 IISRfaDGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTynKTDVAAPFGGF--KQSGFGKDL---G 885
Cdd:PLN02419 498 VCMQ--ANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgNKASFAGDLnfyG 573
|
490
....*....|....*..
gi 21614513 886 EAALNEYLRVKTVTFEY 902
Cdd:PLN02419 574 KAGVDFFTQIKLVTQKQ 590
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
560-881 |
7.27e-48 |
|
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: 176.93 E-value: 7.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPG----SGSLVGQ 635
Cdd:cd07136 97 YYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGgveeNQELLDQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 636 RLsDHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07136 176 KF-DY-----IFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 716 EDSIHDEFVRRVVEEVRKMKVGNPLDRDtDHGPQNHHAHLVKLMEYCQHGvkegaTLVCGGNqVPRPGFFFEPTVFTDVE 795
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----KIVFGGN-TDRETLYIEPTILDNVT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAG------TV--FVNTYnktd 867
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggcindTImhLANPY---- 395
|
330
....*....|....
gi 21614513 868 vaAPFGGFKQSGFG 881
Cdd:cd07136 396 --LPFGGVGNSGMG 407
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
1-200 |
3.15e-45 |
|
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: 161.46 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:cd08646 1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPrgrGKkltPSPVKELALELGLPVLQPEKLKD-----EEFLEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:cd08646 76 ALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21614513 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATY 200
Cdd:cd08646 156 DPDDTAGELLDK-LAELGADLLLEVLDDIEAGKLNPVPQDESEATY 200
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
424-879 |
4.45e-45 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 169.75 E-value: 4.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 424 LFIGGEFVDAEGAkTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:PRK09457 3 LWINGDWIAGQGE-AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 504 ATIEALDAGA--------VYTLALKthVGMSIQTFRYFAGwcdkiqgstipiNQARPNRNLTLT-RKEPVGVCGIIIPWN 574
Cdd:PRK09457 80 AEVIARETGKplweaateVTAMINK--IAISIQAYHERTG------------EKRSEMADGAAVlRHRPHGVVAVFGPYN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 575 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEV 654
Cdd:PRK09457 146 FPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 655 GKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH-DEFVRRVVEEVRK 733
Cdd:PRK09457 225 GYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 734 MKVGNPlDRDTD--HGPQNHHAHLVKLMEYCQHGVKEGA------TLVCGGNQVPRPGfFFEPTVFTDVEDhmfiakEES 805
Cdd:PRK09457 305 LTVGRW-DAEPQpfMGAVISEQAAQGLVAAQAQLLALGGksllemTQLQAGTGLLTPG-IIDVTGVAELPD------EEY 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21614513 806 FGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNK----TDVAAPFGGFKQSG 879
Cdd:PRK09457 377 FGPLLQVVRYD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPFGGVGASG 449
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
425-902 |
1.96e-43 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 165.39 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 425 FIGGEFvdAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 505 TIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:PLN02315 100 RLVSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIP--SERPN-HMMMEVWNPLGIVGVITAFNFPCAVLGWNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 585 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEVGkhIMK 660
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG--LMV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 661 SCAI-SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNP 739
Cdd:PLN02315 253 QQTVnARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 740 LDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVfTDVEDHMFIAKEESFGPVMIISRFAdgD 819
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFK--T 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 820 LDAVLSRANATEFGLASGVFTRD---INKAL--YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYL 893
Cdd:PLN02315 410 LEEAIEINNSVPQGLSSSIFTRNpetIFKWIgpLGSD---CGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486
|
....*....
gi 21614513 894 RVKTVTFEY 902
Cdd:PLN02315 487 RRSTCTINY 495
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
1-201 |
4.92e-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: 154.93 E-value: 4.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKAdplgLEAEKDGVPVFKysrwrakGQALPDVVAKYQALGAEL 80
Cdd:cd08822 1 MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLA----AAARTAGSRGLP-------RAGVAVLPADAIPPGTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08822 70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21614513 161 STLYNRFLFPEGIKGMVQAV-RLIAEGKAPRLPQPEEGATYE 201
Cdd:cd08822 150 AELWRRALAPMGVKLLTQVIdALLRGGNLPAQPQDERLATWE 191
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
484-881 |
7.51e-41 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 163.22 E-value: 7.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 484 DRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGwcdkiqgstipinQARPN-RNLTltrKE 562
Cdd:PRK11809 705 ERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI-AEVREAVDFLRYYAG-------------QVRDDfDNDT---HR 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 563 PVG--VCgiIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDH 640
Cdd:PRK11809 768 PLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVAD 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 641 PDVRKIGFTGSTEVGKHIMKSCA---ISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:PRK11809 846 ARVRGVMFTGSTEVARLLQRNLAgrlDPQGRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 716 EDSIHDEFVRRVVEEVRKMKVGNPlDR-DTDHGP-------QNHHAHlVKLMEYCQHGVkegatlvcggNQVPRP----- 782
Cdd:PRK11809 926 QDDVADRTLKMLRGAMAECRMGNP-DRlSTDIGPvidaeakANIERH-IQAMRAKGRPV----------FQAAREnsedw 993
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 783 --GFFFEPTVftdVE-DHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTR-DINKAlYVSDKLQAGTV 858
Cdd:PRK11809 994 qsGTFVPPTL---IElDSFDELKREVFGPVLHVVRYNRNQLDELIEQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNL 1069
|
410 420
....*....|....*....|....*...
gi 21614513 859 FVntyNKTDVAA-----PFGGFKQSGFG 881
Cdd:PRK11809 1070 YV---NRNMVGAvvgvqPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
591-879 |
3.37e-40 |
|
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: 156.21 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 591 GNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA--ISNVK 668
Cdd:cd07123 197 GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenLDRYR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 669 ---KVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTD 745
Cdd:cd07123 277 typRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 746 HGPQNHHAHLVKLMEYCQHGVKE-GATLVCGGNQVPRPGFFFEPTVF--TDVEDHMFiaKEESFGPVMIISRFADGDLDA 822
Cdd:cd07123 357 MGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIetTDPKHKLM--TEEIFGPVLTVYVYPDSDFEE 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 823 VLSRAN-ATEFGLASGVFTRD---INKAlyvSDKLQ--AGTVFVNTYNKTDVAA--PFGGFKQSG 879
Cdd:cd07123 435 TLELVDtTSPYALTGAIFAQDrkaIREA---TDALRnaAGNFYINDKPTGAVVGqqPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
551-882 |
1.70e-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: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 551 RPNRNLT------LTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtlkagIPK---- 620
Cdd:cd07132 82 PVKKNLAtllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKyldk 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 621 ---GVVNV-LPGSGSLVGQRLsDHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGM 696
Cdd:cd07132 157 ecyPVVLGgVEETTELLKQRF-DY-----IFYTGSTSVGKIVMQAAA-KHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 697 SSVFFNKGENCIAAGRLFVEDSIHDEFV---RRVVEEVrkmkVGNPLDRDTDHGP---QNHHAHLVKLMeycqhgvkEGA 770
Cdd:cd07132 230 WGKFINAGQTCIAPDYVLCTPEVQEKFVealKKTLKEF----YGEDPKESPDYGRiinDRHFQRLKKLL--------SGG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 771 TLVCGGNQVPRPGfFFEPTVFTDVEDHMFIAKEESFGPVMIIsrFADGDLDAVLSRANATEFGLASGVFTRD---INKAL 847
Cdd:cd07132 298 KVAIGGQTDEKER-YIAPTVLTDVKPSDPVMQEEIFGPILPI--VTVNNLDEAIEFINSREKPLALYVFSNNkkvINKIL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 21614513 848 yvsDKLQAGTVFVNtynktDV-------AAPFGGFKQSGFGK 882
Cdd:cd07132 375 ---SNTSSGGVCVN-----DTimhytldSLPFGGVGNSGMGA 408
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
2-166 |
3.71e-31 |
|
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: 120.45 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 2 KIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADP----LGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQALG 77
Cdd:cd08651 1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSdyldLDSFARKNGIPYYKFTDIND-----EEIIEWIKEAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 78 AELNvlpFC---SQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:cd08651 76 PDII---FVfgwSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPI 152
|
170
....*....|..
gi 21614513 155 LPDDTVSTLYNR 166
Cdd:cd08651 153 DKDDTANSLYDK 164
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
562-898 |
4.86e-29 |
|
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: 120.98 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHP 641
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 642 DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 720
Cdd:cd07137 179 D--KIFFTGSPRVGRIIMAAAA-KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 721 DEFVRRVVEEVRKMKVGNPldRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnQVPRPGFFFEPTVFTDVEDHMFI 800
Cdd:cd07137 256 PTLIDALKNTLEKFFGENP--KESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG-ERDEKNLYIEPTILLDPPLDSSI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 801 AKEESFGPVM-IIS-RFADGDLDAVLSRANAtefgLASGVFTRdiNKALY--VSDKLQAGTVFVNtynktDVAA------ 870
Cdd:cd07137 333 MTEEIFGPLLpIITvKKIEESIEIINSRPKP----LAAYVFTK--NKELKrrIVAETSSGGVTFN-----DTVVqyaidt 401
|
330 340
....*....|....*....|....*....
gi 21614513 871 -PFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07137 402 lPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
475-894 |
2.15e-27 |
|
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: 116.57 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 475 GRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKthVGMSIQTFRYFAGWCDKIQGSTIPINQARPNR 554
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAEN--ICGDQVQLRARAFVIYSYRIPHEPGNHLGQGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 555 NLTLTRKE-PVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVLPGSGSL 632
Cdd:cd07084 91 KQQSHGYRwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 633 vGQRLSDHPDVRKIGFTGSTEVGKHImkscaISNVK--KVSLELGGKSPLIIFADCDLNKAV------QMGMSSvffnkG 704
Cdd:cd07084 171 -MQALLLHPNPKMVLFTGSSRVAEKL-----ALDAKqaRIYLELAGFNWKVLGPDAQAVDYVawqcvqDMTACS-----G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 705 ENCIAAGRLFV-EDSIHDEFVRRVVEEVRKMKVGNPL-----DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQ 778
Cdd:cd07084 240 QKCTAQSMLFVpENWSKTPLVEKLKALLARRKLEDLLlgpvqTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYGAC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 779 VPRPGFFFEPTVFTDVEDHMfiakEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQ-AGT 857
Cdd:cd07084 320 VASALFVPIDEILKTYELVT----EEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 21614513 858 VFVNTYNKTDVAAP---FGGFKQSGFGKDLGEA-ALNEYLR 894
Cdd:cd07084 396 TYAILRGRTGVAPNqnhGGGPAADPRGAGIGGPeAIKLVWR 436
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
46-305 |
1.34e-26 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 111.32 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 46 AEKDGVPVFKYSrwrakGQALPDVVAKYQALGAELnVLPFCSQF-IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLI 124
Cdd:PRK06988 51 AAEHGIPVITPA-----DPNDPELRAAVAAAAPDF-IFSFYYRHmIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 125 HGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNrflfpegiKGMVQAVRLIAE-------GKAPRLPQPEEG 197
Cdd:PRK06988 125 NGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD--------KVTVAAEQTLWRvlpallaGEAPHLPNDLAQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 198 ATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTLNTSGlvPEGDALPIPGAHrpgVVTKAG 276
Cdd:PRK06988 197 GSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTRFVVARARLAAPG--AAAARDLPPGLH---VSDNAL 271
|
250 260 270
....*....|....*....|....*....|.
gi 21614513 277 LILFGNDDKMLL--VKNIQLEDGKMILASNF 305
Cdd:PRK06988 272 FGVCGDGRAVSIleLRRQQDGGETVVTPAQF 302
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
562-900 |
2.94e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 113.60 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHP 641
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 642 DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 720
Cdd:PLN02174 190 D--KIFYTGSSKIGRVIMAAAA-KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 721 DEFVRRVVEEVRKMKVGNPLD-RDTDH-GPQNHHAHLVKLMEYcqhgvKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHM 798
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPMEsKDMSRiVNSTHFDRLSKLLDE-----KEVSDKIVYGGEKDRENLKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 799 FIAKEESFGPVMIISRFADGD--LDAVLSRANAtefgLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA------ 870
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEesFDVIRSRPKP----LAAYLFTHNKKLKERFAATVSAGGIVVN-----DIAVhlalht 412
|
330 340 350
....*....|....*....|....*....|.
gi 21614513 871 -PFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:PLN02174 413 lPFGGVGESGMGAYHGKFSFDAFSHKKAVLY 443
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
562-882 |
1.93e-25 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 110.97 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTAlKFaeltLKAGIPK----GVVNVLPGsGSLVGQRL 637
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AF----LAANIPKyldsKAVKVIEG-GPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 638 SDHP-DvrKIGFTGSTEVGKHIMkSCAISNVKKVSLELGGKSPLIIfaDC-DLNKAVQMGMSSVFFNK-----GENCIAA 710
Cdd:PLN02203 181 LQHKwD--KIFFTGSPRVGRIIM-TAAAKHLTPVALELGGKCPCIV--DSlSSSRDTKVAVNRIVGGKwgscaGQACIAI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 711 GRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHaHLVKLMEYCQHGVKEgATLVCGGNQVPRpGFFFEPTV 790
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKK-HFQRLSNLLKDPRVA-ASIVHGGSIDEK-KLFIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 791 FTDVEDHMFIAKEESFGPVM-IISRFADGDLDAVLsraNATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNKTDV- 868
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLpIITVKKIEDSIAFI---NSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAIIq 406
|
330
....*....|....*...
gi 21614513 869 ----AAPFGGFKQSGFGK 882
Cdd:PLN02203 407 yacdSLPFGGVGESGFGR 424
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
1-202 |
1.77e-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: 93.18 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKA---DPLGLEAEKDGVPVFkysrwRAKGQALPDVVAKYQALG 77
Cdd:cd08644 1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENiwfGSVAQLAREHGIPVF-----TPDDINHPEWVERLRALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 78 AELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPD 157
Cdd:cd08644 76 PDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21614513 158 DTVSTLYNRFLFPEGIKgMVQAVRLIAEGKAPRLPQPEEGATYEG 202
Cdd:cd08644 156 DTAKSLFHKLCVAARRL-LARTLPALKAGKARERPQDETQASYFG 199
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
19-248 |
1.20e-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: 97.36 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 19 LRKEGHEVVGVFTVPDKDGKADPLG----LEAEKdGVPVF-----KYSRWRAKGQAL-PDVVAK--YQALGAElnvlpfc 86
Cdd:PRK08125 19 LLAAGYEIAAVFTHTDNPGENHFFGsvarLAAEL-GIPVYapedvNHPLWVERIRELaPDVIFSfyYRNLLSD------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 87 sqfipmEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNR 166
Cdd:PRK08125 91 ------EILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 167 FLFPEGiKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFF 245
Cdd:PRK08125 165 LCHAAR-QLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAvTDPWPGAFSYVGEQKFTVW 243
|
...
gi 21614513 246 NST 248
Cdd:PRK08125 244 SSR 246
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
25-187 |
3.98e-19 |
|
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: 86.63 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 25 EVVGVFTvpdkDgKADPLGLE-AEKDGVPVF-----KYSRWRAKGQALPDVVAKYQAlgaELNVL---------PFCSQF 89
Cdd:COG0299 30 EIVLVIS----N-RPDAYGLErARAAGIPTFvldhkDFPSREAFDAALLEALDAYGP---DLVVLagfmriltpEFVRAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 90 ipmeiisaprHGSII-YHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFL 168
Cdd:COG0299 102 ----------PGRIInIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARIL 171
|
170
....*....|....*....
gi 21614513 169 fPEGIKGMVQAVRLIAEGK 187
Cdd:COG0299 172 -EQEHRLYPEAIRLLAEGR 189
|
|
| Formyl_trans_C |
pfam02911 |
Formyl transferase, C-terminal domain; |
205-309 |
6.99e-18 |
|
Formyl transferase, C-terminal domain;
Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 79.63 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 205 KKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPG--VVTKAGLILFGN 282
Cdd:pfam02911 3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKASV-----------LDQESGAAPGtiVTVDKGGLLVAC 71
|
90 100
....*....|....*....|....*..
gi 21614513 283 DDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:pfam02911 72 GDGALLILELQLEGKKPMSAEDFLNGF 98
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
25-233 |
3.71e-17 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 83.59 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 25 EVVGVFTVPDKDGK------ADPLGLEAEKDGVP---VFKYSRWRAkgqalPDVVAKYQALGAELNVLPFCSQFIPMEII 95
Cdd:PLN02285 37 EVAAVVTQPPARRGrgrklmPSPVAQLALDRGFPpdlIFTPEKAGE-----EDFLSALRELQPDLCITAAYGNILPQKFL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 96 SAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRfLFPEGIKG 175
Cdd:PLN02285 112 DIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPL-LFELGTKL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 176 MVQAVRLIAEGKAPR--LPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGA 233
Cdd:PLN02285 191 LLRELPSVLDGSAKDkaTPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGWPGT 250
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
477-826 |
9.93e-17 |
|
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: 83.74 E-value: 9.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavYTLALKT-HVGMSIQTFRYFA------GWCDKIQGSTIPINQ 549
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFAdlvregSWLDARIDPADPDRQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 550 ARPNRNLTLtRKEPVGVCGIIIPWNYPLM--MLSWKTAACLAAGNTVVIK--PAQvtPLTALKFAELTLKA----GIPKG 621
Cdd:cd07129 93 PLPRPDLRR-MLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAH--PGTSELVARAIRAAlratGLPAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 622 VVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNV-KKVSLELGGKSPLIIFADCDLNKAVQMGMS--- 697
Cdd:cd07129 170 VFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILPGALAERGEAIAQGfvg 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 698 SVFFNKGENCIAAGRLFVEDSIH-DEFVRRVVEEVRKMKVGNPLdrdtDHGPQNHHahlvklmeycQHGVKE-----GAT 771
Cdd:cd07129 250 SLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTML----TPGIAEAY----------RQGVEAlaaapGVR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21614513 772 LVCGGNQvPRPGFFFEPTVF-TDVEDhmFIAK----EESFGPVMIISRFAD-GDLDAVLSR 826
Cdd:cd07129 316 VLAGGAA-AEGGNQAAPTLFkVDAAA--FLADpalqEEVFGPASLVVRYDDaAELLAVAEA 373
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
38-174 |
6.14e-16 |
|
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: 76.66 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 38 KADPLGLE-AEKDGVPVF-----KYSRWRAKGQALPDVVAKYQAlgaELNVL---------PFCSQFipmeiisaprHGS 102
Cdd:cd08645 36 NPDAYGLErAKKAGIPTFvinrkDFPSREEFDEALLELLKEYKV---DLIVLagfmrilspEFLEAF----------PGR 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 103 II-YHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRF------LFPEGIK 174
Cdd:cd08645 103 IInIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIhalehrLYPEAIK 181
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
67-181 |
3.39e-15 |
|
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: 73.79 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 67 PDVVAKYQALGAELNVLPFCSqFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGD-KKGGFSIFWADDGLDTGD 145
Cdd:cd08653 37 PEVVAALRALAPDVVSVYGCG-IIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDTGD 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 21614513 146 LLLQKECEVLPDDTVSTLYNRfLFPEGIKGMVQAVR 181
Cdd:cd08653 116 VLAQARPPLAAGDTLLSLYLR-LYRAGVELMVEAIA 150
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
480-817 |
2.41e-13 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 73.59 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 480 ISARDRGRLMYRLADLMEQHQEELATI-----------EALDA-GAVYTLALKTHVGMSIQTFRYFAGwCDKIQGSTIPI 547
Cdd:PRK11903 60 LTYAQRAALLAAIVKVLQANRDAYYDIatansgttrndSAVDIdGGIFTLGYYAKLGAALGDARLLRD-GEAVQLGKDPA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 548 NQARpnRNLTLTRkepvGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVL 626
Cdd:PRK11903 139 FQGQ--HVLVPTR----GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 627 PGSGSlvgqRLSDH---PDVrkIGFTGSTEVGKHIMKSCA-ISNVKKVSLElggkspliifADcDLNKAV---QMGMSSV 699
Cdd:PRK11903 213 CGSSA----GLLDHlqpFDV--VSFTGSAETAAVLRSHPAvVQRSVRVNVE----------AD-SLNSALlgpDAAPGSE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 700 FFN-------------KGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHgV 766
Cdd:PRK11903 276 AFDlfvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-L 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 767 KEGATLVCGGNQV------PRPGFFFEPTVF--TDVEDHMFIAKEESFGPVMIISRFAD 817
Cdd:PRK11903 355 RAQAEVLFDGGGFalvdadPAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRD 413
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
18-163 |
3.67e-13 |
|
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: 68.05 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 18 HLRKEGHEVVGVFTvPDkdgkadplgleaekdgvPVFKysRWrAKGQALPdVVAKYQALGAELNVLPFCSQF-------I 90
Cdd:cd08649 17 QLLAAGHRIAAVVS-TD-----------------PAIR--AW-AAAEGIA-VLEPGEALEELLSDEPFDWLFsivnlriL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21614513 91 PMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTL 163
Cdd:cd08649 75 PSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
38-178 |
4.29e-13 |
|
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: 68.55 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 38 KADPLGLE-AEKDGVPVFKYSR--WRAKGQALPDVVAKYQALGAELNVlpfCSQFipMEIISAP---RHGSIIY--HPSL 109
Cdd:TIGR00639 37 KPDAYGLErAAQAGIPTFVLSLkdFPSREAFDQAIIEELRAHEVDLVV---LAGF--MRILGPTflsRFAGRILniHPSL 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 110 LPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRF------LFPEGIKGMVQ 178
Cdd:TIGR00639 112 LPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIhkqehrIYPLAIAWFAQ 186
|
|
| Met_tRNA_FMT_C |
cd08704 |
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
207-302 |
1.25e-12 |
|
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: 64.09 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 207 ETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpGVVTKAGLILFGNDDkM 286
Cdd:cd08704 1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAE-----VLEESGEAAPGTI---LAVDKKGLLVACGDG-A 71
|
90
....*....|....*.
gi 21614513 287 LLVKNIQLEDGKMILA 302
Cdd:cd08704 72 LEILELQPEGKKRMSA 87
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
84-184 |
2.06e-11 |
|
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: 63.62 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 84 PFCSQF---IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08823 75 VVVFTFpyrIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154
|
90 100
....*....|....*....|....
gi 21614513 161 STLYNRfLFPEGIKGMVQAVRLIA 184
Cdd:cd08823 155 GLLCSR-LAMLAVGLLEELYQNLA 177
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
492-739 |
3.18e-11 |
|
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: 66.09 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 492 LADLMEQHQEELATIEALDAGA-VYTLALKTHVGMSIQ---------TFRYFAGWCDKIQGSTipinqaRPNRNLTLTRK 561
Cdd:cd07077 25 IANALYDTRQRLASEAVSERGAyIRSLIANWIAMMGCSesklyknidTERGITASVGHIQDVL------LPDNGETYVRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 562 EPVGVCGIIIPWNYPLMMLSwKTAACLAAGNTVVIKPAQVTPLTALKFAELT---LKAGIPKGVVNVLPGSGSLVGQRLS 638
Cdd:cd07077 99 FPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaDAAHGPKILVLYVPHPSDELAEELL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 639 DHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSlelGGKSPLIIFADCDLNKAVQMGMSSVFFNkGENCIAAGRLFVEDS 718
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFG---AGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDD 253
|
250 260
....*....|....*....|.
gi 21614513 719 IHDEFVRRVVEEVRKMKVGNP 739
Cdd:cd07077 254 VLDPLYEEFKLKLVVEGLKVP 274
|
|
| FMT_core_HypX_N |
cd08650 |
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ... |
13-180 |
7.38e-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: 61.09 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 13 QEVYCHLRKEGHEVVGVFTVPDkdgkadplglEAEKDGVPVFKysrwrakgqalPDVVakyqalgaelnVLPFCSQFIPM 92
Cdd:cd08650 15 QRAFLELRERGHEVSVEYALSD----------DEMREAVALFA-----------PDLI-----------ICPFLKKRIPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 93 EIISapRHGSIIYHPSLlPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEG 172
Cdd:cd08650 63 EIWS--NYPCLIVHPGI-VGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYRGEVTDAA 139
|
....*...
gi 21614513 173 IKGMVQAV 180
Cdd:cd08650 140 VKAVLEAV 147
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
477-889 |
2.08e-10 |
|
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: 64.42 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK---THV---GMSIQTFRYFAgwCDKIQGSTIPINQA 550
Cdd:cd07127 100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQaggPHAqdrGLEAVAYAWRE--MSRIPPTAEWEKPQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 551 RPNRNLTLTRK---EPVGV-----CGIIIPWN-YPLMMlswktaACLAAGNTVVIKP--AQVTPLT-ALKFAELTL-KAG 617
Cdd:cd07127 178 GKHDPLAMEKTftvVPRGValvigCSTFPTWNgYPGLF------ASLATGNPVIVKPhpAAILPLAiTVQVAREVLaEAG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 618 I-PKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisNVKKVSLELGGKSPLIIFADCDLNKAVQ-MG 695
Cdd:cd07127 252 FdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA---RQAQVYTEKAGVNTVVVDSTDDLKAMLRnLA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 696 MSSVFFNkGENCIAAGRLFV-EDSI--------HDEFVRRVVEEVRKMkVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGv 766
Cdd:cd07127 329 FSLSLYS-GQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLG- 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 767 kegatlvcggnQVPRPGFFFEPTVFTDVEDH--MFIA---------KEESFGPVMIISRFADGDLDAVLSRANATEFG-L 834
Cdd:cd07127 406 -----------EVLLASEAVAHPEFPDARVRtpLLLKldasdeaayAEERFGPIAFVVATDSTDHSIELARESVREHGaM 474
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21614513 835 ASGVFTRD-------INKALYVSDKLQ---AGTVFVNTynktdvAAPFGGFKQSGfGKDLGEAAL 889
Cdd:cd07127 475 TVGVYSTDpevvervQEAALDAGVALSinlTGGVFVNQ------SAAFSDFHGTG-ANPAANAAL 532
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
556-862 |
2.31e-10 |
|
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: 63.82 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 556 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGS 631
Cdd:cd07081 88 GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 632 LVGQRLSDHPDVRKIGFTGstevGKHIMKScAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAG 711
Cdd:cd07081 168 ELAQRLMKFPGIGLLLATG----GPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 712 RLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNH--HAHLVklmeycqhGVKEGATLVCGGNQVPRPG--FFFE 787
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGdvNRDIV--------GQDAYKIAAAAGLKVPQETriLIGE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 788 PTVftdVEDHMFIAKEEsFGPVMIISR---FADGDLDAvLSRANATEFGLASGVFTRDIN---KALYVSDKLQAGTVFVN 861
Cdd:cd07081 315 VTS---LAEHEPFAHEK-LSPVLAMYRaanFADADAKA-LALKLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRFVKN 389
|
.
gi 21614513 862 T 862
Cdd:cd07081 390 G 390
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
563-863 |
4.03e-10 |
|
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: 63.28 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 563 PVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDhPD 642
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-AN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 643 VRKIGFTGSTEVGKHImkscAISNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFV-EDSIH 720
Cdd:cd07126 221 PRMTLFTGSSKVAERL----ALELHGKVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAhENWVQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 721 DEFVRRVVE--EVRKMK---VGNPLDRDTdhgpQNHHAHLVKLMEYcqhgvkEGATLVCGGNQVP-----------RPGF 784
Cdd:cd07126 297 AGILDKLKAlaEQRKLEdltIGPVLTWTT----ERILDHVDKLLAI------PGAKVLFGGKPLTnhsipsiygayEPTA 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 785 FFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINkalyVSDKLQAGTVFVNTY 863
Cdd:cd07126 367 VFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIR----FLQEVLANTVNGTTY 441
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
85-164 |
3.25e-09 |
|
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: 57.07 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 85 FCSQF---IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVS 161
Cdd:cd08820 74 ISVQYhwiLPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVI 153
|
...
gi 21614513 162 TLY 164
Cdd:cd08820 154 SLY 156
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
574-842 |
3.55e-08 |
|
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: 56.89 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 574 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVLPGS-GSLVGQRlsDHPDVrkIGFTGS 651
Cdd:cd07128 155 NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSvGDLLDHL--GEQDV--VAFTGS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 652 TEVGKHIMkscAISNVKKVSLelggksPLIIFADcDLNKAV-----QMGMSSV-FFNK----------GENCIAAGRLFV 715
Cdd:cd07128 231 AATAAKLR---AHPNIVARSI------RFNAEAD-SLNAAIlgpdaTPGTPEFdLFVKevaremtvkaGQKCTAIRRAFV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 716 EDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPqnhhahLVKLMEycQHGVKEG-------ATLVCGGNQVPRP------ 782
Cdd:cd07128 301 PEARVDAVIEALKARLAKVVVGDPRLEGVRMGP------LVSREQ--REDVRAAvatllaeAEVVFGGPDRFEVvgadae 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614513 783 -GFFFEPTVF--------TDVEDHmfiakeESFGPVMIIsrFADGDLDAVLSRANATEFGLASGVFTRD 842
Cdd:cd07128 373 kGAFFPPTLLlcddpdaaTAVHDV------EAFGPVATL--MPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
562-725 |
6.38e-07 |
|
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: 52.88 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP---AQVTPLTALKF-AELTLKAGIPKGVVNVLPGSGSLVGQRL 637
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 638 SDHPDVRKIGFTGSTevgkhimkscaiSNVK------KVSLELG-GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAA 710
Cdd:cd07122 174 MKHPDVDLILATGGP------------GMVKaayssgKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASE 241
|
170
....*....|....*
gi 21614513 711 GRLFVEDSIHDEFVR 725
Cdd:cd07122 242 QSVIVDDEIYDEVRA 256
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
86-215 |
8.96e-07 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 51.06 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 86 CSQFIPMEIISAPRhgSIIYHPSLLPRHRGASAINWTLIHGDKKGGfSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYN 165
Cdd:PRK07579 74 CKQRFPAKLVNGVR--CINIHPGFNPYNRGWFPQVFSIINGLKIGA-TIHEMDEQLDHGPIIAQREVEIESWDSSGSVYA 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 21614513 166 RFLFPEgIKGMVQAVRLIAEGKAPRLpQPEEGATYEGIQK-KETAKINWDQ 215
Cdd:PRK07579 151 RVMDIE-RELVLEHFDAIRDGSYTAK-KPATEGNLNSKKDfKQLREIDLDE 199
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
556-730 |
9.02e-07 |
|
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: 52.24 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 556 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVL--PGS 629
Cdd:cd07121 90 LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAEAGGPDNLVVTVeePTI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 630 GSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisnvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIA 709
Cdd:cd07121 170 ETT--NELMAHPDINLLVVTGGPAVVKAALSSG-----KKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIA 242
|
170 180
....*....|....*....|.
gi 21614513 710 AGRLFVEDSIHDEFVRRVVEE 730
Cdd:cd07121 243 EKEVIAVDSVADYLIAAMQRN 263
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
556-730 |
1.25e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 51.83 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 556 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVL--PGS 629
Cdd:PRK15398 122 LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVaePTI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 630 GSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisnvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIA 709
Cdd:PRK15398 202 ETA--QRLMKHPGIALLVVTGGPAVVKAAMKSG-----KKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIA 274
|
170 180
....*....|....*....|.
gi 21614513 710 AGRLFVEDSIHDEFVRRVVEE 730
Cdd:PRK15398 275 EKEVIVVDSVADELMRLMEKN 295
|
|
| Arna_FMT_C |
cd08702 |
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ... |
210-305 |
3.78e-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: 46.08 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 210 KINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpgVVTKAG---LILFGndDK 285
Cdd:cd08702 4 LIDWRMSAREIYNLVRAvTKPYPGAFTFVGGQKIKIWKAR-----PVDDAFYNGEPGK----VLSVDGdplIVACG--DG 72
|
90 100
....*....|....*....|
gi 21614513 286 MLLVKNIQLEDGKMILASNF 305
Cdd:cd08702 73 ALEILEAELDGGLPLAGEQL 92
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
46-171 |
3.29e-04 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 42.76 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 46 AEKDGVPVFKYSRWRAKGQALP--DVVAKYQALGAELNVLPFCSQFIPMEIISA-PRhgSII-YHPSLLPRH--RGASAI 119
Cdd:PLN02331 45 ARENGIPVLVYPKTKGEPDGLSpdELVDALRGAGVDFVLLAGYLKLIPVELVRAyPR--SILnIHPALLPAFggKGYYGI 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 21614513 120 NwtlIH------GDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPE 171
Cdd:PLN02331 123 K---VHkaviasGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLHEE 177
|
|
| FMT_core_like_1 |
cd08821 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
84-225 |
8.63e-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: 38.45 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614513 84 PFCSQFIPMEIISapRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLpdDTVSTL 163
Cdd:cd08821 51 PHWSWIIPKEIFE--NFECVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLKRDLSLK--GTAEEI 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21614513 164 YNRflFPEGIKGMVqaVRLIAEGKAPrLPQPEEGATYEGiQKKETAKINWDQPAEAIHNWIR 225
Cdd:cd08821 127 YER--ASKISLKMI--PELVTKKPKP-IKQEGEPVTFKR-RTPEQSNISNEANLEKIYDFIR 182
|
|
| |
