|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
15-495 |
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: 1006.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 15 NLKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLAD 94
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 95 LMERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLL 174
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 175 MFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLI 254
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 255 KEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGN 334
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 335 PLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSI 414
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 415 DDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 14424442 495 K 495
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
19-492 |
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: 898.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 19 QHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMER 98
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 99 DRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIW 178
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 179 KIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 259 GKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ 338
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 339 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVI 418
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14424442 419 KRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
18-494 |
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: 736.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 18 IQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 98 RDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFI 177
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 178 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 258 AGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLT 337
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 338 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 417
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14424442 418 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
18-492 |
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: 706.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 18 IQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPW-RTMDASERGRLLNKLADLM 96
Cdd:cd07143 4 EQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWgLKVSGSKRGRCLSKLADLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 97 ERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMF 176
Cdd:cd07143 82 ERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 177 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 256
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 257 AAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 336
Cdd:cd07143 242 AAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 337 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 416
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 417 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
4-492 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 704.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 4 PAQPAVpaplanlKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDAS 83
Cdd:PLN02466 48 PITPPV-------QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 84 ERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVC 163
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 164 GQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVA 243
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 244 FTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKS 323
Cdd:PLN02466 280 FTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 324 VERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFG 403
Cdd:PLN02466 360 KARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 404 PVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGL 483
Cdd:PLN02466 440 PVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSL 519
|
....*....
gi 14424442 484 YEYTELKTV 492
Cdd:PLN02466 520 NNYLQVKAV 528
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-495 |
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: 685.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 19 QHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMER 98
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 99 DRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFI 177
Cdd:COG1012 81 RREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 178 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 258 AGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLT 337
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 338 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 416
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 417 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCY-MILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGtTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
19-492 |
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: 677.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 19 QHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMER 98
Cdd:cd07144 6 QPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 99 DRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIW 178
Cdd:cd07144 84 NRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 179 KIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 259 GkSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKK-YVLGNPLT 337
Cdd:cd07144 244 A-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 338 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGG---GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSI 414
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 415 DDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
29-492 |
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: 670.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 29 WHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEA 108
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 109 INGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGN 188
Cdd:pfam00171 77 LENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 189 TVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTL 268
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 269 ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDK 348
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 349 EQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL 428
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 429 AAGVFTKDLDRAITVSSALQAGVVWVNCYMILSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
17-496 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 667.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 17 KIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLM 96
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 97 ERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMF 176
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 177 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 256
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 257 AAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 336
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 337 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 416
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 417 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 496
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-492 |
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: 621.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 183
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNL 263
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 264 KRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQG 343
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 344 PQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 419
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14424442 420 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-494 |
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: 618.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 61 DKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAnAYLSDLGGSIKALKYCAGWADKI 140
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 141 HGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVV 219
Cdd:cd07078 77 HGEVIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 220 NIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQ 299
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 300 GQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN-K 378
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 379 GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYM 458
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 14424442 459 I-LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
35-492 |
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: 613.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 35 GKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKV 114
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 115 FANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 194
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKS 274
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 275 PCIVFADA-DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDK 353
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 354 ILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAG 431
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14424442 432 VFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
40-492 |
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: 593.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVfanay 119
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKAL----KYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 194
Cdd:cd07114 75 IRETRAQVRYLaewyRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKS 274
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 275 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKI 354
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 355 LDLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAA 430
Cdd:cd07114 314 ERYVARAREEGARVLTGGERpsgaDLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14424442 431 GVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
40-496 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 588.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 119
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGKSPCIVF 279
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDR 439
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 14424442 440 AITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 496
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
16-495 |
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: 579.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 16 LKIQHtKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADL 95
Cdd:cd07140 2 LKMPH-QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 96 MERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSD----GDIFTFTRREPIGVCGQIIPWNF 171
Cdd:cd07140 80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 172 PLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVG 251
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 252 KLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYV 331
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 332 LGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKF 411
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 412 KS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*.
gi 14424442 490 KTVAMK 495
Cdd:cd07140 480 KTVTIE 485
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
40-494 |
0e+00 |
|
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: 561.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 119
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 436 DLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-494 |
0e+00 |
|
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: 551.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 119
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQT 198
Cdd:cd07103 77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 199 PLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGK-LIKEAAgkSNLKRVTLELGGKSPCI 277
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 278 VFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDL 357
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 358 IESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDL 437
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 14424442 438 DRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
24-492 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 536.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLM-ERDRLL 102
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 103 lATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 182
Cdd:PRK13252 87 -AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 183 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSn 262
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 263 LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 342
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 343 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVI 418
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14424442 419 KRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
23-493 |
0e+00 |
|
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: 525.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 23 IFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMER--DR 100
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEAraDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 101 LLLATIEAINGGKVFANAY-----LSDLGGSIKALKYCAgWADKIHGQTIpsdgdiftftRREPIGVCGQIIPWNFPLLM 175
Cdd:cd07138 78 LAQAITLEMGAPITLARAAqvglgIGHLRAAADALKDFE-FEERRGNSLV----------VREPIGVCGLITPWNWPLNQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 176 FIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK 255
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 256 EAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP 335
Cdd:cd07138 227 EAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 336 LTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGG-GR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 413 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
.
gi 14424442 493 A 493
Cdd:cd07138 465 Q 465
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
40-492 |
0e+00 |
|
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: 523.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 119
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLECGGGRWGNK-----GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 435 KDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
41-494 |
0e+00 |
|
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: 522.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAyL 120
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 121 SDLGGSIKALKYCAGWADKIHGQTIPSDG-DIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07118 80 GEIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLD 438
Cdd:cd07118 319 AGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 439 RAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
24-490 |
0e+00 |
|
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: 520.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 183
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNL 263
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 264 KRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQG 343
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 344 PQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 419
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14424442 420 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-490 |
0e+00 |
|
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: 519.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 22 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 102 LLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 181
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKs 261
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 262 NLKRVTLELGGKSPCIVFADA-----DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 336
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 337 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 413 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-493 |
0e+00 |
|
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: 518.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 119
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 lSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07109 79 -ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLtQGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07109 316 RARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 437 LDRAITVSSALQAGVVWVNCYMILSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
40-492 |
4.43e-175 |
|
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: 500.34 E-value: 4.43e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 119
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LsDLGGSIKALKYCAGWADKIH---GQTIPSDGDIFT-FTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPA 195
Cdd:cd07110 78 W-DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 196 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 276 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 355
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 356 DLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 433
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 434 TKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-494 |
4.24e-173 |
|
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: 495.22 E-value: 4.24e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRtMDASERGRLLNKLADLMERDR-LLLATIEAINGGKVfANA 118
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKeELRALLVAEVGAPV-MTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 119 YLSDLGGSIKALKYCAGWADKIHG-QTIPSDGDIFTFT----RREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVK 193
Cdd:cd07089 78 RAMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 194 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGK 273
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 274 SPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFvrksVERAKKYV----LGNPLTQGINQGPQIDKE 349
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEV----VEALAAAFealpVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 350 QHDKILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYG 427
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14424442 428 LAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07089 393 LSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
65-494 |
3.00e-172 |
|
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: 489.43 E-value: 3.00e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 65 KAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAnAYLSDLGGSIKALKYCAGWADKIHGQT 144
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 145 IPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVP 223
Cdd:cd06534 77 LPSpDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 224 GYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCC 303
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 304 VAASRIFVEESVYDEFVRKSVerakkyvlgnpltqginqgpqidkeqhdkildliesgkkegaklecgggrwgnkgffvq 383
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 384 pTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMIL-SA 462
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 14424442 463 QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-492 |
8.51e-172 |
|
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: 492.74 E-value: 8.51e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 22 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 102 LLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 181
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKs 261
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 262 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 341
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 417
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 418 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-492 |
3.58e-170 |
|
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: 487.42 E-value: 3.58e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 119
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFP---GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LsDLGGSIKALKYCAGWADKIHgqTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07106 78 F-EVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAgFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDR 439
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 14424442 440 AITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-494 |
8.30e-168 |
|
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: 482.15 E-value: 8.30e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK---AWERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYLsDLGGSIKALKYCAGWADKIHGQTIPSDG---DIFTFtrREPIGVCGQIIPWNFPLLMFIWKI 180
Cdd:cd07088 78 AKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRpneNIFIF--KVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGK 260
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 261 sNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGI 340
Cdd:cd07088 235 -NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 341 NQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 419
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 420 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-499 |
8.50e-168 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 483.47 E-value: 8.50e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 8 AVPAPLANLkiqhtkiFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAF--QIGSPWRTMDASER 85
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 86 GRLLNKLADLMERDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHG-QTIPSDGDIFTF---TRREPIG 161
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAkQKAPVSLPMETFkgyVLKEPLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 162 VCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDK 241
Cdd:PLN02467 154 VVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 242 VAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVR 321
Cdd:PLN02467 234 IAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 322 KSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG--NKGFFVQPTVFSNVTDEMRIAKE 399
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 400 EIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELG 479
Cdd:PLN02467 393 EVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELG 472
|
490 500
....*....|....*....|
gi 14424442 480 EHGLYEYTELKTVAMKISQK 499
Cdd:PLN02467 473 EWGLENYLSVKQVTKYISDE 492
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-492 |
1.85e-167 |
|
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: 480.67 E-value: 1.85e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 119
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGqtiPSDGDIF----TFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPA 195
Cdd:cd07092 78 DDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 196 EQTPLTALHMASLIKEaGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 276 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 355
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 356 DLIEsGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 14424442 436 DLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-492 |
9.81e-167 |
|
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: 479.44 E-value: 9.81e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKkfPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAF---PAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 103 LATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 181
Cdd:cd07097 79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPStRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkS 261
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 262 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 341
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 419
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 420 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI-LSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-494 |
2.19e-166 |
|
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: 478.61 E-value: 2.19e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 23 IFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 103 LATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKI-HGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 181
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkS 261
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG-E 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 262 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 341
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIK 419
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 420 RANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMiLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-492 |
7.31e-166 |
|
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: 477.61 E-value: 7.31e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 103 LATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIG 181
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKS 261
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 262 NlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGIN 341
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 417
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14424442 418 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI-LSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
20-497 |
3.78e-165 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 475.55 E-value: 3.78e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 20 HTKIFINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERD 99
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 100 RLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGqtiPSDG----DIFTFTRREPIGVCGQIIPWNFPLLM 175
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGeyleGHTSMIRRDPVGVVASIAPWNYPLMM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 176 FIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK 255
Cdd:PRK13473 155 AAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 256 EAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP 335
Cdd:PRK13473 234 SAAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 336 LTQGINQGPQIDKEQHDKILDLIESGKKEG-AKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSI 414
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 415 DDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
...
gi 14424442 495 KIS 497
Cdd:PRK13473 473 KHT 475
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-492 |
1.01e-164 |
|
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: 473.77 E-value: 1.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAY 119
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGV-FYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLI 358
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 359 ESGKKE-GAK-LECG---GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 433
Cdd:cd07108 316 DLGLSTsGATvLRGGplpGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14424442 434 TKDLDRAITVSSALQAGVVWVN-CYMILSAQcPFGGFKMSGNGRELGEHGLYE-YTELKTV 492
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNqGGGQQPGQ-SYGGFKQSGLGREASLEGMLEhFTQKKTV 455
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
24-486 |
9.95e-164 |
|
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: 472.27 E-value: 9.95e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKihgqtipSDGDiftFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 183
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTE---LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEA-AGKSn 262
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRAtAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 263 lKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 342
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 343 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRAN 422
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14424442 423 NTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEY 486
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
38-494 |
9.38e-162 |
|
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: 466.04 E-value: 9.38e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 117
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 118 AYLsDLGGSIKALKYCAGWADKIHGQTIPSDG-DIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 197 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPC 276
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 356
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 357 LIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 437 LDRAITVSSALQAGVVWVNCYMILS-AQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
2-494 |
3.01e-160 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 464.16 E-value: 3.01e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 2 SSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMD 81
Cdd:PLN02278 6 SSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 82 ASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLSDLGGSiKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPI 160
Cdd:PLN02278 83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGA-SFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 161 GVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVD 240
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 241 KVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFV 320
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 321 RKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEE 400
Cdd:PLN02278 321 EAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 401 IFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGE 480
Cdd:PLN02278 401 VFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSK 480
|
490
....*....|....
gi 14424442 481 HGLYEYTELKTVAM 494
Cdd:PLN02278 481 YGIDEYLEIKYVCL 494
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
59-494 |
7.54e-160 |
|
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: 460.46 E-value: 7.54e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 59 DVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLsDLGGSIKALKYCAGWAD 138
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 139 KIHGQTIPSDGD-IFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLT-ALHMASLIKEAGFPP 216
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 217 GVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVF 296
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 297 YHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG 376
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 377 NkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNC 456
Cdd:cd07104 316 L---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 14424442 457 YMIL-SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
24-495 |
3.54e-157 |
|
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: 455.36 E-value: 3.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQT----IPS-DGDIFT-FTRREPIGVCGQIIPWNFPLLMFI 177
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSmQGERYTaFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 178 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 258 AgKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLT 337
Cdd:cd07113 240 A-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 338 QGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDV 417
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 418 IKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
14-496 |
2.95e-156 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 453.58 E-value: 2.95e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 14 ANLKIQhTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLA 93
Cdd:PRK09847 14 LSLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 94 DLMERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPL 173
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 174 LMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKL 253
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 254 IKEAAGKSNLKRVTLELGGKSPCIVFADA-DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVL 332
Cdd:PRK09847 252 LLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 333 GNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL--DGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 413 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
....
gi 14424442 493 AMKI 496
Cdd:PRK09847 490 WISL 493
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
24-496 |
9.47e-156 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 452.34 E-value: 9.47e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYLSdlggSIKALKYCAGWADK----IHGQTIPSDgDIFTFTRREPIGVCGQIIPWNFPLLMFIWK 179
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQ----VIRAAENFRFFADKceeaMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 180 IGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKeAAG 259
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIM-RNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 260 KSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQG 339
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 340 INQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG-------NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 413 SIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
....
gi 14424442 493 AMKI 496
Cdd:TIGR02299 475 ALAL 478
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-492 |
1.66e-154 |
|
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: 447.98 E-value: 1.66e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAnAY 119
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 200 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPCIVF 279
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYH-QGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLI 358
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 359 ESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 435 KDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-494 |
1.35e-151 |
|
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: 440.11 E-value: 1.35e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 117
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 118 AyLSDLGGSIKALKYCAGWADKIHGQTIPSDG-----DIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVV 192
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGksnLKRVTLELGG 272
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 273 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHD 352
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 353 KILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGV 432
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 433 FTKDLDRAITVSSALQAGVVWVNcyMILSAQC---PFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMIN--DSSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
18-496 |
1.17e-146 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 428.76 E-value: 1.17e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 18 IQHtkiFINNEWHDSvsGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLME 97
Cdd:TIGR03216 1 IRN---FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALK--GPWGKMTVAERADLLYAVADEIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 98 R--DRLLLAtiEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQ----TIPSDGDIFTFTRREPIGVCGQIIPWNF 171
Cdd:TIGR03216 74 RrfDDFLAA--EVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTEcfemATPDGKGALNYAVRKPLGVVGVISPWNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 172 PLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGP-TAGAAISSHMDVDKVAFTGSTQV 250
Cdd:TIGR03216 152 PLLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 251 GKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKY 330
Cdd:TIGR03216 232 GSAIMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 331 VLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGG--RWGNK---GFFVQPTVFSNVTDEMRIAKEEIFGPV 405
Cdd:TIGR03216 311 KIGVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGvpDFGDAlagGAWVQPTIWTGLPDSARVVTEEIFGPC 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 406 QQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYE 485
Cdd:TIGR03216 391 CHIAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEF 470
|
490
....*....|.
gi 14424442 486 YTELKTVAMKI 496
Cdd:TIGR03216 471 YTELTNVCIKL 481
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
38-493 |
2.57e-145 |
|
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: 424.45 E-value: 2.57e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 117
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 118 AYLsDLGGSIKALKYCAGWADKIHGQTIPSDGDIFT-----FTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVV 192
Cdd:cd07145 78 SRV-EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNerriaFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGG 272
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 273 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHD 352
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 353 KILDLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGV 432
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14424442 433 FTKDLDRAITVSSALQAGVVWVNCYMILSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWdNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-496 |
6.46e-142 |
|
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: 417.78 E-value: 6.46e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 19 QHTKIFINNEWHDSvsGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07124 31 REYPLVIGGKEVRT--EEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 98 RDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFI 177
Cdd:cd07124 106 RRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 178 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 258 AGK-----SNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVL 332
Cdd:cd07124 265 AAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 333 GNPLTQGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGN--KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMK 410
Cdd:cd07124 345 GDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 411 FKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN--CYMILSAQCPFGGFKMSG-NGRELGEHGLYEYT 487
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFM 503
|
....*....
gi 14424442 488 ELKTVAMKI 496
Cdd:cd07124 504 QPKTVTENF 512
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-492 |
1.34e-140 |
|
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: 413.11 E-value: 1.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 182
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 183 ALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGYGPtAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 259 GKSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ 338
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 339 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 416
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 417 VIKRANNTTYGLAAGVFTKDLDRAITVSSA--LQAGVVWVNCYMI-LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
41-494 |
2.79e-139 |
|
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: 409.04 E-value: 2.79e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTmDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYL 120
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 121 sDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPL 200
Cdd:cd07120 80 -EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 201 TALHMASLIKEA-GFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP-TLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLECGGGRWG---NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTeglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 437 LDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
24-490 |
1.00e-138 |
|
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: 408.38 E-value: 1.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPA 183
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 184 LSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNL 263
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 264 KRVTLELGGKSPCIVFA------DADLDIAVE----FAhhgvfYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLG 333
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEgfvmFA-----LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 334 NPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNvTDEMRIAKEEIFGPVQQIM 409
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelggLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 410 KFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQT 472
|
.
gi 14424442 490 K 490
Cdd:cd07116 473 K 473
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-495 |
5.42e-134 |
|
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: 395.90 E-value: 5.42e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 27 NEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLME--RDRLLLA 104
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEerRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 105 TIEAINGGKVFANAylsDLGGSIKALKYCAGWADKIHGQTIPSDGD-----IFtftrREPIGVCGQIIPWNFPLLMFIWK 179
Cdd:cd07151 78 LIRESGSTRIKANI---EWGAAMAITREAATFPLRMEGRILPSDVPgkenrVY----REPLGVVGVISPWNFPLHLSMRS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 180 IGPALSCGNTVVVKPAEQTPLTA-LHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07151 151 VAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 259 GKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ 338
Cdd:cd07151 231 GR-HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 339 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVI 418
Cdd:cd07151 310 DTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 419 KRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMIL-SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
60-492 |
1.07e-128 |
|
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: 381.04 E-value: 1.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 60 VDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAylsdlGGSI-KALKYCAGWAD 138
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-----RAEVeKCAWICRYYAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 139 KIHG----QTIPSDGDIfTFTRREPIGVCGQIIPWNFPLlmfiWKI----GPALSCGNTVVVKPAEQTPLTALHMASLIK 210
Cdd:cd07100 73 NAEAfladEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 211 EAGFPPGVVNIVPGYGPTAGAAISSHMdVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEF 290
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQVEAIIADPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 291 AHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLEC 370
Cdd:cd07100 226 AVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 371 GGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAG 450
Cdd:cd07100 306 GGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 14424442 451 VVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07100 386 MVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-494 |
9.61e-128 |
|
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: 379.47 E-value: 9.61e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 119
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPSD-----GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 194
Cdd:cd07094 79 RVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsnlKRVTLELGGKS 274
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG---KRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 275 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKI 354
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 355 LDLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14424442 435 KDLDRAITVSSALQAGVVWVNCYMILSAQ-CPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
47-479 |
2.29e-127 |
|
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: 378.17 E-value: 2.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 47 EVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAyLSDLGGS 126
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA-GFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 127 IKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTA-LHM 205
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 206 ASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLD 285
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 286 IAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEG 365
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 366 AKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSS 445
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|....*
gi 14424442 446 ALQAGVVWVNCYMIL-SAQCPFGGFKMSGNGRELG 479
Cdd:cd07152 393 RLRTGMLHINDQTVNdEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
41-493 |
1.51e-125 |
|
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: 373.87 E-value: 1.51e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYL 120
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 121 sDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTR----REPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07099 78 -EVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKatveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 197 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISShmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPC 276
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 356
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 357 LIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 437 LDRAITVSSALQAGVVWVNCYMILSAQC--PFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPalPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-495 |
4.08e-123 |
|
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: 368.38 E-value: 4.08e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 21 TKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDR 100
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP---AWSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 101 LLLATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTIP-SDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWK 179
Cdd:cd07085 78 DELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 180 IGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAG 259
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 260 KSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQG 339
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 340 INQGPQIDKEQHDKILDLIESGKKEGAKLECgGGRwGNK------GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKS 413
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVL-DGR-GVKvpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 414 IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYM-ILSAQCPFGGFKMS--GNGRELGEHGLYEYTELK 490
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSffGDLHFYGKDGVRFYTQTK 472
|
....*
gi 14424442 491 TVAMK 495
Cdd:cd07085 473 TVTSR 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
22-477 |
1.12e-122 |
|
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: 367.28 E-value: 1.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 22 KIFINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 102 LLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFT-----FTRREPIGVCGQIIPWNFPLLMF 176
Cdd:cd07082 80 EVANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 177 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 256
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 257 AAGKsnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPL 336
Cdd:cd07082 239 QHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 337 TQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 416
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 417 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCymilsaQC-------PFGGFKMSGNGRE 477
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS------KCqrgpdhfPFLGRKDSGIGTQ 455
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
19-496 |
1.26e-122 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 368.49 E-value: 1.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 19 QHTKIFINNEWHDSvsGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:PRK03137 35 QDYPLIIGGERITT--EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 98 RDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKI-HGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMF 176
Cdd:PRK03137 110 RRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 177 IWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 256
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 257 AAGKSN-----LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYV 331
Cdd:PRK03137 269 RAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 332 LGNPlTQGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKF 411
Cdd:PRK03137 349 VGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 412 KSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN--CYMILSAQCPFGGFKMSG-NGRELGEHGLYEYTE 488
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGtDSKAGGPDYLLLFLQ 506
|
....*...
gi 14424442 489 LKTVAMKI 496
Cdd:PRK03137 507 AKTVSEMF 514
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
59-492 |
1.42e-121 |
|
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: 362.67 E-value: 1.42e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 59 DVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLLLATIEAINGGKVFANaylSDLGGSIKALKYCAGW 136
Cdd:cd07105 1 DADQAVEAAAAAFPA---WSKTPPSERRDILLKAADLLEsrRDEFIEAMMEETGATAAWAG---FNVDLAAGMLREAASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 137 ADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFP 215
Cdd:cd07105 75 ITQIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 216 PGVVNIV---PGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAH 292
Cdd:cd07105 155 KGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 293 HGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTqginqGPQIDKEQHDKILDLIESGKKEGAKLECGG 372
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 373 -GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGV 451
Cdd:cd07105 309 lADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 14424442 452 VWVN-CYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07105 389 VHINgMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-493 |
1.46e-118 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 358.42 E-value: 1.46e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 31 DSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLM-ERDRLLLATIEAI 109
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVlENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 110 NGgKVFANAYLSDLGGSIKALKYcAGWADKI-----HGQTIPsdgdIFTFTR--REPIGVCGQIIPWNFPLLMFIWKIGP 182
Cdd:PRK09407 104 TG-KARRHAFEEVLDVALTARYY-ARRAPKLlaprrRAGALP----VLTKTTelRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 183 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdVDKVAFTGSTQVGKLIKEAAGkSN 262
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG-RR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 263 LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 342
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 343 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRA 421
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 422 NNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN-CYMIL--SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAwgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
24-496 |
1.26e-117 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 354.60 E-value: 1.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 182
Cdd:PRK11241 91 ARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPGhQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 183 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsN 262
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-D 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 263 LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQ 342
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 343 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRAN 422
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14424442 423 NTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 496
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
38-494 |
4.85e-117 |
|
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: 351.93 E-value: 4.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 117
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 118 AYlSDLGGSIKALKYCAGWADKIHGQTIPSDGD-----IFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVV 192
Cdd:cd07147 78 AR-GEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGygPTAGAAI-SSHMDVDKVAFTGSTQVGKLIKEAAGKsnlKRVTLELG 271
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 272 GKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQH 351
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 352 DKILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAG 431
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 432 VFTKDLDRAITVSSALQAGVVWVN---CYMILSAqcPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdvpTFRVDHM--PYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
40-492 |
2.25e-114 |
|
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: 345.11 E-value: 2.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAArqafqiGSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 119
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIPSD-----GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 194
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGksnLKRVTLELGGKS 274
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 275 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKI 354
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 355 LDLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14424442 435 KDLDRAITVSSALQAGVVWVN---CYMilSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNevpGFR--SELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
43-493 |
2.45e-114 |
|
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: 345.06 E-value: 2.45e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 43 PATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLSD 122
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 123 LGGSIKALKYC----AGWADKIHGQTIPsdgdIFTFTR--REPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07101 80 LDVAIVARYYArraeRLLKPRRRRGAIP----VLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 197 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGKSPC 276
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 356
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 357 LIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14424442 436 DLDRAITVSSALQAGVVWVN-CYMIL--SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
41-492 |
1.16e-112 |
|
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: 340.76 E-value: 1.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAyl 120
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 121 sdlGGSIKALKYCAGW----ADKIHGQTIPSDGDIFT-FTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPA 195
Cdd:cd07102 76 ---GGEIRGMLERARYmisiAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 196 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 276 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 355
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 356 DLIESGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGV 432
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 433 FTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
89-492 |
1.22e-107 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 326.31 E-value: 1.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 89 LNKLADLM-ERDRLLLATIEAiNGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD---GDIFTFTRrePIGVCG 164
Cdd:PRK10090 1 LRKIAAGIrERASEISALIVE-EGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 165 QIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAF 244
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 245 TGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSV 324
Cdd:PRK10090 157 TGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 325 ERAKKYVLGNPLTQG-INQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFG 403
Cdd:PRK10090 236 EAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 404 PVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGL 483
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGL 395
|
....*....
gi 14424442 484 YEYTELKTV 492
Cdd:PRK10090 396 HEYLQTQVV 404
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
42-493 |
3.31e-104 |
|
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: 319.63 E-value: 3.31e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 42 NPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLS 121
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQ---REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 122 DLGGSIKALKYCAGWADKiHGQTIPSDGDIFTFTRR-----EPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07098 79 EILVTCEKIRWTLKHGEK-ALRPESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 197 QTPLTALHMASLIKEA----GFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGG 272
Cdd:cd07098 158 QVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 273 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHD 352
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 353 KILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL 428
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 429 AAGVFTKDLDRAITVSSALQAGVVWVN----CYMILsaQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQ--QLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
41-492 |
1.79e-92 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 288.94 E-value: 1.79e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYl 120
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 121 SDLGGSIKALKYCAGWADKIHGQTiPSD----GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADE-PADaaavGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 197 QTPLTALHMASLIKEAGFPPGVVNIVPgYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPC 276
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILD 356
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 357 LIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 437 LDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09406 399 EAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-496 |
6.97e-90 |
|
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: 283.70 E-value: 6.97e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 19 QHTKIFINNEWHDSvsGKKFPVLNP-ATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07083 17 RAYPLVIGGEWVDT--KERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 98 RDRLLLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTI------PSDGDIFTftrrEPIGVCGQIIPWNF 171
Cdd:cd07083 92 RRRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESFY----VGLGAGVVISPWNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 172 PLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVG 251
Cdd:cd07083 167 PVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 252 KLIKEAAGK-----SNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVER 326
Cdd:cd07083 247 KKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 327 AKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQ 406
Cdd:cd07083 327 AERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 407 QIMKFKSID--DVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI--LSAQCPFGGFKMSG-NGRELGEH 481
Cdd:cd07083 406 SVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGtNAKTGGPH 485
|
490
....*....|....*
gi 14424442 482 GLYEYTELKTVAMKI 496
Cdd:cd07083 486 YLRRFLEMKAVAERF 500
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
26-479 |
8.23e-87 |
|
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: 274.85 E-value: 8.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 26 NNEWhdSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLAT 105
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 106 IEAINGGKVFANAYlsdlgGSIKAL----KYCAGWADKIHGQTIPSDgdiftftrR---------EPIGVCGQIIPWNFP 172
Cdd:cd07130 79 LVSLEMGKILPEGL-----GEVQEMidicDFAVGLSRQLYGLTIPSE--------RpghrmmeqwNPLGVVGVITAFNFP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 173 LLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGST 248
Cdd:cd07130 146 VAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 249 QVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVE---FAHHGVfyhQGQCCVAASRIFVEESVYDEFVRKSVE 325
Cdd:cd07130 225 AVGRQVGQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAVRavlFAAVGT---AGQRCTTTRRLIVHESIYDEVLERLKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 326 RAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDeMRIAKEEIFGPV 405
Cdd:cd07130 301 AYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 406 QQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQA--GVVWVNCYM----ILSAqcpFGGFKMSGNGRELG 479
Cdd:cd07130 380 LYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIGTsgaeIGGA---FGGEKETGGGRESG 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
12-479 |
2.49e-85 |
|
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: 272.15 E-value: 2.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 12 PLANLKIQHTKiFINNEWHDS--VSGKKF------PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDA 82
Cdd:cd07125 15 PLEALADALKA-FDEKEWEAIpiINGEETetgegaPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 83 SERGRLLNKLADLMERDR---LLLATIEAingGKVFANAyLSDLGGSIKALKYCAGWADKI--HGQTIPSDG--DIFTFT 155
Cdd:cd07125 91 EERAEILEKAADLLEANRgelIALAAAEA---GKTLADA-DAEVREAIDFCRYYAAQARELfsDPELPGPTGelNGLELH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 156 RREpIGVCgqIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISS 235
Cdd:cd07125 167 GRG-VFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 236 HMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEE 313
Cdd:cd07125 244 HPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 314 SVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEgAKLECGGGRWGNKGFFVQPTVFSNVTDE 393
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 394 MRiaKEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYM---ILSAQcPFGG 468
Cdd:cd07125 403 DL--TTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNItgaIVGRQ-PFGG 479
|
490
....*....|.
gi 14424442 469 FKMSGNGRELG 479
Cdd:cd07125 480 WGLSGTGPKAG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
40-475 |
9.29e-83 |
|
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: 263.90 E-value: 9.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWrtMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAy 119
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIKALKYCAGWADKIHGQTIP------SDGDIfTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVK 193
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPmgltpaSAGRI-AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 194 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdvdKVA---FTGSTQVGKLI--KEAAGKsnlkRVTL 268
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDP----RVAffsFIGSARVGWMLrsKLAPGT----RCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 269 ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDK 348
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 349 EQHDKILDLIESGKKEGAKLECGGGRWGNKGFfvQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL 428
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 14424442 429 AAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQ-CPFGGFKMSGNG 475
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-492 |
3.75e-80 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 257.50 E-value: 3.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 22 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 102 LLATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPS-DGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKI 180
Cdd:TIGR01722 79 EIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGK 260
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 261 SNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVyDEFVRKSVERAKKYVLGNPLTQGI 340
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 341 NQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGF----FVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDD 416
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 417 VIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcyMILSAQCP---FGGFKMS--GNGRELGEHGLYEYTELKT 491
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN--VPIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYTRGKT 472
|
.
gi 14424442 492 V 492
Cdd:TIGR01722 473 V 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
59-476 |
6.11e-75 |
|
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: 242.56 E-value: 6.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 59 DVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVF------ANAYLSDLGGSIKALKY 132
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 133 CAGWADKihgqtipSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA 212
Cdd:cd07095 78 RTGERAT-------PMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 213 GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAH 292
Cdd:cd07095 151 GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 293 HGVFYHQGQCCVAASRIFVEES-VYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL----DLIESGKK---E 364
Cdd:cd07095 230 QSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLlaqqDLLALGGEpllA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 365 GAKLECGGGrwgnkgfFVQPTVFsNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD---LDRAI 441
Cdd:cd07095 310 MERLVAGTA-------FLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDealFERFL 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 14424442 442 TvssALQAGVV-WVNCYMILSAQCPFGGFKMSGNGR 476
Cdd:cd07095 382 A---RIRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
22-475 |
6.92e-74 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 241.97 E-value: 6.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 22 KIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRL 101
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 102 LLATIEAINGGKVFANAyLSDLGGSIKALKYCA-------GWADKIHGQTIPSDG-DIFTFTRREPIGVCGQIIPWNFPL 173
Cdd:PLN00412 94 PIAECLVKEIAKPAKDA-VTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNErNKYCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 174 LMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGStQVGKL 253
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 254 IKEAAGKSNLKrvtLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLG 333
Cdd:PLN00412 252 ISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 334 NPlTQGINQGPQIDKEQHDKILDLIESGKKEGAKLEcggGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKS 413
Cdd:PLN00412 329 PP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 414 IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcymilSAQC------PFGGFKMSGNG 475
Cdd:PLN00412 405 VEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN-----SAPArgpdhfPFQGLKDSGIG 467
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
10-475 |
2.00e-73 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 252.48 E-value: 2.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 10 PAPLANLKIQHTKiFINNEWH-------DSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMD 81
Cdd:PRK11905 535 EATLAALDEALNA-FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 82 ASERGRLLNKLADLMERDR---LLLATIEAingGKVFANAyLSDLGGSIKALKYCAGWADkihgqtipsdgDIFTFTRRE 158
Cdd:PRK11905 611 AAERAAILERAADLMEAHMpelFALAVREA---GKTLANA-IAEVREAVDFLRYYAAQAR-----------RLLNGPGHK 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 159 PIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 238
Cdd:PRK11905 676 PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPR 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 239 VDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCvAASRI-FVEESV 315
Cdd:PRK11905 756 IAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRC-SALRVlCLQEDV 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 316 YDEFVRKSVERAKKYVLGNP--LTQGInqGPQIDKEQHDKILDLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFSnvTD 392
Cdd:PRK11905 835 ADRVLTMLKGAMDELRIGDPwrLSTDV--GPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--ID 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 393 EMRIAKEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI---LSAQcPFG 467
Cdd:PRK11905 911 SISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIgavVGVQ-PFG 989
|
....*...
gi 14424442 468 GFKMSGNG 475
Cdd:PRK11905 990 GEGLSGTG 997
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
156-492 |
5.14e-72 |
|
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: 235.20 E-value: 5.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 156 RREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGygptaGAAISS 235
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DAEVAQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 236 H---MDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVE 312
Cdd:cd07134 171 AlleLPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 313 ESVYDEFV---RKSVER---AKKYVLGNP-LTQGINQGpqidkeQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVqPT 385
Cdd:cd07134 250 ESVKDAFVehlKAEIEKfygKDAARKASPdLARIVNDR------HFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIA-PT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 386 VFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDlDRAI-TVSSALQAGVVWVNCYMI--LSA 462
Cdd:cd07134 323 VLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD-KANVnKVLARTSSGGVVVNDVVLhfLNP 401
|
330 340 350
....*....|....*....|....*....|
gi 14424442 463 QCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
31-475 |
1.07e-71 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 247.16 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 31 DSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLL-LATI 106
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEahRAELMaLLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 107 EAingGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTipsdgdiftfTRREPIGVCGQIIPWNFPLLMFIWKIGPALSC 186
Cdd:COG4230 642 EA---GKTLPDA-IAEVREAVDFCRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 187 GNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA-AGKSNlKR 265
Cdd:COG4230 708 GNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTlAARDG-PI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 266 VTL--ELGGKSPCIVfaD---------ADldiAVEFAhhgvFYHQGQCCVAAsRI-FVEESVYDEFvrksVER----AKK 329
Cdd:COG4230 787 VPLiaETGGQNAMIV--DssalpeqvvDD---VLASA----FDSAGQRCSAL-RVlCVQEDIADRV----LEMlkgaMAE 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 330 YVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFsnvtdEM-RIA--KEEIFGPV 405
Cdd:COG4230 853 LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-----EIdSISdlEREVFGPV 927
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 406 QQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMIlSA----QcPFGGFKMSGNG 475
Cdd:COG4230 928 LHVVRYKAdeLDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNII-GAvvgvQ-PFGGEGLSGTG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
39-490 |
5.16e-71 |
|
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: 234.42 E-value: 5.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 39 PVLNPAT-EEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFAN 117
Cdd:TIGR01238 54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPT---WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 118 AyLSDLGGSIKALKYCAGWADkihgqtipsdgDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQ 197
Cdd:TIGR01238 131 A-IAEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 198 TPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSP 275
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 276 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKIL 355
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 356 DLIESGKKEG---AKLECGGGRWGNKGFFVQPTVFSnvTDEMRIAKEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAA 430
Cdd:TIGR01238 359 AHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTM 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14424442 431 GVFTKDLDRAITVSSALQAGVVWVNCYM---ILSAQcPFGGFKMSGNG-RELGEHGLYEYTELK 490
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQvgaVVGVQ-PFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
24-492 |
7.28e-71 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 243.95 E-value: 7.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWH----DSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMER 98
Cdd:PRK11904 546 FLEKQWQagpiINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 99 DR---LLLATIEAingGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSDGdiftFT------RREPIGV--CgqII 167
Cdd:PRK11904 623 NRaelIALCVREA---GKTLQDA-IAEVREAVDFCRYYAAQARRLFGAPEKLPG----PTgesnelRLHGRGVfvC--IS 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 168 PWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS 247
Cdd:PRK11904 693 PWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGS 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 248 TQVGKLIKEA-AGKSNlKRVTL--ELGGKSPCIVFADADL----DIAVEFAhhgvFYHQGQCCVAASRIFVEESVYDEFV 320
Cdd:PRK11904 773 TETARIINRTlAARDG-PIVPLiaETGGQNAMIVDSTALPeqvvDDVVTSA----FRSAGQRCSALRVLFVQEDIADRVI 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 321 RKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEG---AKLECGGGrwGNKGFFVQPTVFSnvTDEMRIA 397
Cdd:PRK11904 848 EMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPAG--TENGHFVAPTAFE--IDSISQL 923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 398 KEEIFGPVQQIMKFKS--IDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMI---LSAQcPFGGFKMS 472
Cdd:PRK11904 924 EREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIgavVGVQ-PFGGQGLS 1002
|
490 500
....*....|....*....|.
gi 14424442 473 GNG-RELGEHGLYEYTELKTV 492
Cdd:PRK11904 1003 GTGpKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
68-492 |
9.57e-71 |
|
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: 231.61 E-value: 9.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 68 RQAFQI-GSPwrtmDASERGRLLNKLADLM--ERDRLllatIEAIN---GGKVFANAYLSDLGGSIKALKYC----AGW- 136
Cdd:cd07133 8 KAAFLAnPPP----SLEERRDRLDRLKALLldNQDAL----AEAISadfGHRSRHETLLAEILPSIAGIKHArkhlKKWm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 137 -ADKIHG--QTIPSDGDIftftRREPIGVCGQIIPWNFPLLMfiwKIGP---ALSCGNTVVVKPAEQTPLTALHMASLIK 210
Cdd:cd07133 80 kPSRRHVglLFLPAKAEV----EYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 211 EAgFPPGVVNIVPGyGPTAGAAISShMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEF 290
Cdd:cd07133 153 EY-FDEDEVAVVTG-GADVAAAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 291 AHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKY---VLGNP-LTQGINQGpqidkeQHDKILDLIESGKKEGA 366
Cdd:cd07133 229 IAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPdYTSIINER------HYARLQGLLEDARAKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 367 KL-ECG-GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVS 444
Cdd:cd07133 303 RViELNpAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 14424442 445 SALQAGVVWVNCYMILSAQ--CPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07133 383 RRTHSGGVTINDTLLHVAQddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
24-476 |
2.05e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 229.84 E-value: 2.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVF------ANAYLSDLGGSIKALKycagwadKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFI 177
Cdd:PRK09457 80 AEVIARETGKPLweaateVTAMINKIAISIQAYH-------ERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 178 WKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLI-KE 256
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 257 AAGKSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVY-DEFVRKSVERAKKYVLGNP 335
Cdd:PRK09457 232 FAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 336 LTQgiNQ---GPQIDKEQHDKILD----LIESGKK---EGAKLECGGGrwgnkgfFVQPTVFsNVTDEMRIAKEEIFGPV 405
Cdd:PRK09457 311 DAE--PQpfmGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEEYFGPL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14424442 406 QQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVV-WVNCYMILSAQCPFGGFKMSGNGR 476
Cdd:PRK09457 381 LQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
41-492 |
4.39e-69 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 228.21 E-value: 4.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYl 120
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 121 sdlGGSIKALKYCAGWADkiHG-------QTIPSDGDIFTFTRrePIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVK 193
Cdd:PRK13968 88 ---AEVAKSANLCDWYAE--HGpamlkaePTLVENQQAVIEYR--PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 194 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMdVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGK 273
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 274 SPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDK 353
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 354 ILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 433
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 434 TKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
63-492 |
8.39e-69 |
|
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: 226.25 E-value: 8.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 63 AVKAARQAFQIGspwRTMDASERGRLLNKLadlmerDRLLLATIEAING------GKVFANAYLSDLG---GSIK-ALKY 132
Cdd:cd07087 3 LVARLRETFLTG---KTRSLEWRKAQLKAL------KRMLTENEEEIAAalyadlGKPPAEAYLTEIAvvlGEIDhALKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 133 CAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA 212
Cdd:cd07087 74 LKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 213 gFPPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAH 292
Cdd:cd07087 154 -FDPEAVAVVEG-GVEVATALLAE-PFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 293 HGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGiNQGPQIDKEQHDKILDLIESGKKEGaklecgG 372
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDGKVVI------G 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 373 GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVV 452
Cdd:cd07087 303 GQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 14424442 453 WVNCYMI--LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07087 383 CVNDVLLhaAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
2-495 |
9.91e-69 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 231.17 E-value: 9.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 2 SSP---AQPAVPAPLANLkiqhtkifINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWR 78
Cdd:PLN02419 100 TSPeqsTQPQMPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 79 TMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYlSDLGGSIKALKYCAGWADKIHGQTIP--SDGdIFTFTR 156
Cdd:PLN02419 169 NTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEYLPnvSNG-VDTYSI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 157 REPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGaAISSH 236
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 237 MDVDKVAFTGSTQVGKLI-KEAAGKSnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASR-IFVEES 314
Cdd:PLN02419 326 EDIRAVSFVGSNTAGMHIyARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 315 vyDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNV 390
Cdd:PLN02419 404 --KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpGYEKGNFIGPTILSGV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 391 TDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNcyMILSAQCPFggFK 470
Cdd:PLN02419 482 TPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--VPIPVPLPF--FS 557
|
490 500 510
....*....|....*....|....*....|..
gi 14424442 471 MSGNGREL-------GEHGLYEYTELKTVAMK 495
Cdd:PLN02419 558 FTGNKASFagdlnfyGKAGVDFFTQIKLVTQK 589
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
62-492 |
3.71e-67 |
|
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: 222.76 E-value: 3.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 62 KAVKAARQAFQIGspwRTMDASERGRLLNKLADLMER--DRLLlatiEAING--GKVFANAYLSDLG---GSIK-ALKYC 133
Cdd:cd07136 2 SLVEKQRAFFKTG---ATKDVEFRIEQLKKLKQAIKKyeNEIL----EALKKdlGKSEFEAYMTEIGfvlSEINyAIKHL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 134 AGWADKIHGQT----IPSDGdiftFTRREPIGVCGQIIPWNFPLLMfiwKIGP---ALSCGNTVVVKPAEQTPLTALHMA 206
Cdd:cd07136 75 KKWMKPKRVKTpllnFPSKS----YIYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 207 SLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDvdKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDI 286
Cdd:cd07136 148 KIIEET-FDEEYVAVVEGGVEENQELLDQKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 287 AVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGinQGPQIDKEQH-DKILDLIESGKkeg 365
Cdd:cd07136 224 AAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP--DYGRIINEKHfDRLAGLLDNGK--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 366 akLECGGGrwGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVS 444
Cdd:cd07136 299 --IVFGGN--TDREtLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 14424442 445 SALQAGVVWVN-CYM-ILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07136 375 ENLSFGGGCINdTIMhLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
58-493 |
1.17e-65 |
|
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: 218.63 E-value: 1.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 58 ADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLM-ERDRLLLATIEAINGGKVFaNAYLSDLGGS----IKALKY 132
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVkDNEEAIVEALKKDLGRPPF-ETLLTEVSGVkndiLHMLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 133 CAGWA-DKIhgqtiPSDGDIF-----TFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMA 206
Cdd:cd07135 81 LKKWAkDEK-----VKDGPLAfmfgkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 207 SLIKEAgFPPGVVNIVPGYGPTAGAAISSHMdvDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDI 286
Cdd:cd07135 156 ELVPKY-LDPDAFQVVQGGVPETTALLEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 287 AvefAHH---GVFYHQGQCCVAASRIFVEESVYDEFvrksVERAKKyVLGNPLTQGINQGPQ----IDKEQHDKILDLIE 359
Cdd:cd07135 232 A---AKRilwGKFGNAGQICVAPDYVLVDPSVYDEF----VEELKK-VLDEFYPGGANASPDytriVNPRHFNRLKSLLD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKkegAKLECGGGRwGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD--- 436
Cdd:cd07135 304 TTK---GKVVIGGEM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDkse 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 437 LDRAITvsSALQAGVVWVNCYM-ILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07135 380 IDHILT--RTRSGGVVINDTLIhVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-486 |
8.73e-60 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 213.30 E-value: 8.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 39 PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERD-RLLLATI--EAingGKV 114
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPI---WFATPPAERAAILERAADLMEAQmQTLMGLLvrEA---GKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 115 FANAyLSDLGGSIKALKYCAGWADkihgqtipsdgDIFTFTRREPIG--VCgqIIPWNFPLLMFIWKIGPALSCGNTVVV 192
Cdd:PRK11809 736 FSNA-IAEVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 193 KPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK-------EAAGKSnlkr 265
Cdd:PRK11809 802 KPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQrnlagrlDPQGRP---- 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 266 VTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP--LTQGIn 341
Cdd:PRK11809 878 IPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPdrLSTDI- 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 342 qGPQIDKEQHDKILDLIESGKKEGAK---LECGGGRWGNKGFFVQPTVFS-NVTDEMriaKEEIFGPVQQIMKFKS--ID 415
Cdd:PRK11809 957 -GPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNRnqLD 1032
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 416 DVIKRANNTTYGLAAGVFTKdLDRAIT-VSSALQAGVVWVNCYMI---LSAQcPFGGFKMSGNGRELGehG-LYEY 486
Cdd:PRK11809 1033 ELIEQINASGYGLTLGVHTR-IDETIAqVTGSAHVGNLYVNRNMVgavVGVQ-PFGGEGLSGTGPKAG--GpLYLY 1104
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
153-495 |
5.90e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.48 E-value: 5.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 153 TFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGAA 232
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 233 ISSHMDVdkVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVE 312
Cdd:PTZ00381 182 LKEPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 313 ESVYDEFVRKSVERAKKYVLGNPLTQgiNQGPQIDKEQH-DKILDLIESGKKEGAKlecgGGRWGNKGFFVQPTVFSNVT 391
Cdd:PTZ00381 259 RSIKDKFIEALKEAIKEFFGEDPKKS--EDYSRIVNEFHtKRLAELIKDHGGKVVY----GGEVDIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 392 DEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVN-CYMILSAQ-CPFGGF 469
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLLNPnLPFGGV 412
|
330 340
....*....|....*....|....*.
gi 14424442 470 KMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
24-491 |
5.97e-56 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 194.67 E-value: 5.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWhdSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAyLSDLGGSIKALKYCAGWADKIHGQTIPSD-GDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGP 182
Cdd:PLN02315 99 GRLVSLEMGKILAEG-IGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 183 ALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 259 gKSNLKRVTLELGGKSPCIVFADADLDIAVE---FAHHGVfyhQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNP 335
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRsvlFAAVGT---AGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 336 LTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSnVTDEMRIAKEEIFGPVQQIMKFKSID 415
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 416 DVIKRANNTTYGLAAGVFTKDLDRAITVSSALQA--GVVWVNCYM----ILSAqcpFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIPTngaeIGGA---FGGEKATGGGREAGSDSWKQYMRR 488
|
..
gi 14424442 490 KT 491
Cdd:PLN02315 489 ST 490
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
48-473 |
2.82e-54 |
|
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: 190.49 E-value: 2.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 48 VICHVEEGDKADVDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLME---RDRLLLATieAINGGKvfaNAYLSDLG 124
Cdd:cd07123 59 VLATYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAAT--MLGQGK---NVWQAEID 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 125 GS---IKALKYCAGWADKI-HGQTIPSDGDIFTFTRREPI-GVCGQIIPWNF----------PLLMfiwkigpalscGNT 189
Cdd:cd07123 131 AAcelIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFtaiggnlagaPALM-----------GNV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 190 VVVKPAEqtplTALHMASLI----KEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKS---- 261
Cdd:cd07123 200 VLWKPSD----TAVLSNYLVykilEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldry 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 262 -NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGI 340
Cdd:cd07123 276 rTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 341 NQGPQIDKEQHDKILDLIESGKKE-GAKLECGGGRWGNKGFFVQPTVFSnVTDEM-RIAKEEIFGPVQQIM-----KFKS 413
Cdd:cd07123 356 FMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIE-TTDPKhKLMTEEIFGPVLTVYvypdsDFEE 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14424442 414 IDDVIkraNNTT-YGLAAGVFTKDLDRAITVSSALQ--AGVVWVN--CYMILSAQCPFGGFKMSG 473
Cdd:cd07123 435 TLELV---DTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
62-495 |
1.60e-48 |
|
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: 173.18 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 62 KAVKAARQAFQIGspwRTMDASERGRLLNKLADLME--RDRLLLATIEAINggKVFANAYLSDLGGSIK----ALKYCAG 135
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEenEDEIVEALAKDLR--KPKFEAVLSEILLVKNeikyAISNLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 136 WAdkihgQTIPSDGDIFT-----FTRREPIGVCGQIIPWNFPL-LMFIWKIGpALSCGNTVVVKPAEQTPLTALHMASLI 209
Cdd:cd07132 77 WM-----KPEPVKKNLATllddvYIYKEPLGVVLIIGAWNYPLqLTLVPLVG-AIAAGNCVVIKPSEVSPATAKLLAELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 210 -----KEAgFPpgVVnivpgygpTAGAAISSHM---DVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFAD 281
Cdd:cd07132 151 pkyldKEC-YP--VV--------LGGVEETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 282 ADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYvLGNPLTQGINQGPQIDKEQHDKILDLIESG 361
Cdd:cd07132 219 CDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 362 KKegakleCGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT---KDLD 438
Cdd:cd07132 298 KV------AIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSnnkKVIN 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 14424442 439 RAITVSSalqAGVVWVNCYMILSA--QCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:cd07132 372 KILSNTS---SGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
64-486 |
1.08e-45 |
|
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: 165.28 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 64 VKAARQAFQIGspwRTMDASERGRLLNKLADLM-ERDRLLLATIEAiNGGKVFANAYLSDLG---GSIK-ALKYCAGWAD 138
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSvlvSSCKlAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 139 ----KIHGQTIPSDGDIFTftrrEPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgF 214
Cdd:cd07137 81 pekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 215 PPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHG 294
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 295 VF-YHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGinQGPQIDKEQHDKILDLIESGKKEGAKLECGGG 373
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK--DLSRIVNSHHFQRLSRLLDDPSVADKIVHGGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 374 RwGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVW 453
Cdd:cd07137 311 R-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVT 389
|
410 420 430
....*....|....*....|....*....|....*
gi 14424442 454 VNCYMI--LSAQCPFGGFKMSGNGRelgEHGLYEY 486
Cdd:cd07137 390 FNDTVVqyAIDTLPFGGVGESGFGA---YHGKFSF 421
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
24-479 |
5.21e-39 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 148.70 E-value: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSvSGKKFPVLNPATEEVICHVEeGDKADVDKAVKAARQafQIGSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 104 ATIEAINGGKVFANAYLsDLGGSIKALKYCAGWADKIHGQTIPSDGD--------------IFTFTRrepiGVCGQIIPW 169
Cdd:PRK11903 84 YDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpafqgqhVLVPTR----GVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 170 NFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG-FPPGVVNIVPGygptAGAAISSH---MDVdkVAFT 245
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHlqpFDV--VSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 246 GSTQVGKLIK-EAAGKSNLKRVTLELGGKSPCIVFADADLDIAvEFAhhgVFYHQ---------GQCCVAASRIFVEESV 315
Cdd:PRK11903 233 GSAETAAVLRsHPAVVQRSVRVNVEADSLNSALLGPDAAPGSE-AFD---LFVKEvvremtvksGQKCTAIRRIFVPEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 316 YDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIEsGKKEGAKLECGGGRWG------NKGFFVQPTVF-- 387
Cdd:PRK11903 309 YDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLga 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 388 SNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLD--------------RAITVSSALQA---- 449
Cdd:PRK11903 388 SDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAflaaaaleladshgRVHVISPDVAAlhtg 467
|
490 500 510
....*....|....*....|....*....|.
gi 14424442 450 -GVVwvncyMilsAQCPFGGFKMSGNGRELG 479
Cdd:PRK11903 468 hGNV-----M---PQSLHGGPGRAGGGEELG 490
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
53-486 |
5.27e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 136.78 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 53 EEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLM--ERDRLLLATIEAIngGKVFANAYLSDLGGSIKAL 130
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESG---RTRSLEWRKSQLKGLLRLLkdNEEAIFKALHQDL--GKHRVEAYRDEVGVLTKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 131 KY---CAG-WADKIHGQ----TIPSDGDIFTftrrEPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTA 202
Cdd:PLN02203 76 NLalsNLKkWMAPKKAKlplvAFPATAEVVP----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 203 LHMASLIKeAGFPPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIV---F 279
Cdd:PLN02203 152 AFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdslS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 280 ADADLDIAVEFAHHGVFYH-QGQCCVAASRIFVEE---SVYDEFVRKSVeraKKYVLGNPLTQGinQGPQIDKEQH-DKI 354
Cdd:PLN02203 228 SSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEErfaPILIELLKSTI---KKFFGENPRESK--SMARILNKKHfQRL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 355 LDLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFT 434
Cdd:PLN02203 303 SNLLKDPRVAASIVH--GGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFT 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 435 KD--LDRAITvsSALQAGVVWVNCYMILSA--QCPFGGFKMSGNGRelgEHGLYEY 486
Cdd:PLN02203 381 NNekLKRRIL--SETSSGSVTFNDAIIQYAcdSLPFGGVGESGFGR---YHGKYSF 431
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
24-436 |
1.57e-33 |
|
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: 132.78 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 24 FINNEWHDSvSGKKFPVLNPATEEVICHVEeGDKADVDKAVKAARQafqIGSP-WRTMDASERGRLLNKLAD-LMERDRL 101
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYARE---KGGPaLRALTFHERAAMLKALAKyLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 102 LLAtIEAINGGKVFANAYlsDLGGSIKALKYCAGWADK-IHGQTIPSDGDIFTFTRREPI----------GVCGQIIPWN 170
Cdd:cd07128 79 LYA-LSAATGATRRDSWI--DIDGGIGTLFAYASLGRReLPNAHFLVEGDVEPLSKDGTFvgqhiltprrGVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 171 FPllmfIW----KIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG-FPPGVVNIVPGygptAGAAISSHMDV-DKVAF 244
Cdd:cd07128 156 FP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGDLLDHLGEqDVVAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 245 TGSTQVGKLIKEAAG-KSNLKRVTLELGGKSPCIVFADADLDIAvEFAhhgVFYHQ---------GQCCVAASRIFVEES 314
Cdd:cd07128 228 TGSAATAAKLRAHPNiVARSIRFNAEADSLNAAILGPDATPGTP-EFD---LFVKEvaremtvkaGQKCTAIRRAFVPEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 315 VYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEgAKLECGG-------GRWGNKGFFVQPTVF 387
Cdd:cd07128 304 RVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfevvGADAEKGAFFPPTLL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 14424442 388 -SNVTDEMRIAKE-EIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07128 383 lCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
120-492 |
6.17e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 125.16 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 120 LSDLGGSIK-ALKYCAGW----ADKIHGQTIPSDGDIFTftrrEPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP 194
Cdd:PLN02174 72 VSLLRNSIKlALKQLKNWmapeKAKTSLTTFPASAEIVS----EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 195 AEQTPLTALHMASLIkEAGFPPGVVNIVPGYGPTAGAAISSHMdvDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKS 274
Cdd:PLN02174 148 SELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW--DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 275 PCIVFADADLDIAVEFAHHGVF-YHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLtQGINQGPQIDKEQHDK 353
Cdd:PLN02174 224 PVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 354 ILDLIEsgKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVF 433
Cdd:PLN02174 303 LSKLLD--EKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLF 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14424442 434 TKDLDRAITVSSALQAGVVWVNCYMILSA--QCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PLN02174 381 THNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
60-436 |
1.79e-29 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 120.42 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 60 VDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKvfANAYLSDLGGSIKALKYCA--GWA 137
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGK--GWMFAENICGDQVQLRARAfvIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 138 DKIHGQTIPSDGDIFTFTRRE---PIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAG- 213
Cdd:cd07084 76 YRIPHEPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 214 FPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVG-KLIKEAAgksnLKRVTLELGGKSPCIVFADADL--DIAVEF 290
Cdd:cd07084 156 LPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAeKLALDAK----QARIYLELAGFNWKVLGPDAQAvdYVAWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 291 AHHGVFYhQGQCCVAASRIFVEEsvyDEFVRKSVERAKKYvlgnpLTQGINQGPQIDKEQHDKILDLIES-GKKEGAKLE 369
Cdd:cd07084 231 VQDMTAC-SGQKCTAQSMLFVPE---NWSKTPLVEKLKAL-----LARRKLEDLLLGPVQTFTTLAMIAHmENLLGSVLL 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 370 CGG------GRWGNKGFFVQPTVFSNVTDEMRIAK---EEIFGPVQQIMKFK--SIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07084 302 FSGkelknhSIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdQLALVLELLERMHGSLTAAIYSND 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
60-357 |
5.10e-16 |
|
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: 79.96 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 60 VDKAVKAARQA-FQIGSPWRTMDASERGRLLNKLADLMERdRLLLATieainggkvfanaylSDLGGSIKALKYCAGWAD 138
Cdd:cd07077 18 RDLIINAIANAlYDTRQRLASEAVSERGAYIRSLIANWIA-MMGCSE---------------SKLYKNIDTERGITASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 139 KIHGQTIPSDGDifTFTRREPIGVCGQIIPWNFPLLMfIWKIGPALSCGNTVVVKPAEQTPLTAlHMASLIKEAGFPPGV 218
Cdd:cd07077 82 HIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 219 VNIVPGYGPTAGAAIS----SHMDVDKVAFTGSTQVgklIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHG 294
Cdd:cd07077 158 PKILVLYVPHPSDELAeellSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14424442 295 VFYHQGQCCVAASRIFVE---ESVYDEFVRKSVErAKKYVLGNPLTQGINQGPQIDKEQHDKILDL 357
Cdd:cd07077 235 KFFDQNACASEQNLYVVDdvlDPLYEEFKLKLVV-EGLKVPQETKPLSKETTPSFDDEALESMTPL 299
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
60-422 |
6.19e-15 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 76.81 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 60 VDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME--RDRLL-LATIEA------INGG--------KVFANAYLSd 122
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEalGDELVaRAHAETglpearLQGElgrttgqlRLFADLVRE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 123 lgGSikalkycagWADKI------HGQTIPSdGDIftftRRE-----PIGVCGqiiPWNFPLLMFIwkIG----PALSCG 187
Cdd:cd07129 77 --GS---------WLDARidpadpDRQPLPR-PDL----RRMlvplgPVAVFG---ASNFPLAFSV--AGgdtaSALAAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 188 NTVVVKPAEQTPLTALHMASLI----KEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAgksnL 263
Cdd:cd07129 136 CPVVVKAHPAHPGTSELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA----A 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 264 KR-----VTLELGGKSPCIVFADAdL-----DIAVEFAHH---GVfyhqGQCCVAASRIFVEESV-YDEFVRKSVERAKK 329
Cdd:cd07129 212 ARpepipFYAELGSVNPVFILPGA-LaergeAIAQGFVGSltlGA----GQFCTNPGLVLVPAGPaGDAFIAALAEALAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 330 YVLGNPLTQGINQGPQIDKEQ---HDKILDLIESGKKEGaklecgggrwgnkGFFVQPTVFsnVTDEMRIAK-----EEI 401
Cdd:cd07129 287 APAQTMLTPGIAEAYRQGVEAlaaAPGVRVLAGGAAAEG-------------GNQAAPTLF--KVDAAAFLAdpalqEEV 351
|
410 420
....*....|....*....|.
gi 14424442 402 FGPVQQIMKFKSIDDVIKRAN 422
Cdd:cd07129 352 FGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
157-436 |
1.38e-09 |
|
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: 60.20 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 157 REPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSh 236
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 237 MDVDKVAFTGSTQVG-KLIKEAAGKsnlkrVTLELGGKSPCIVFAD-ADLDIAVEFAHHGVFYHQGQCCVAASRIFVEES 314
Cdd:cd07126 219 ANPRMTLFTGSSKVAeRLALELHGK-----VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 315 -VYDEFVRKSVERAKKYVLGNpLTQG--INQGPQIDKEQHDKILDLiesgkkEGAKLECGGGRWGNKGF-----FVQPT- 385
Cdd:cd07126 294 wVQAGILDKLKALAEQRKLED-LTIGpvLTWTTERILDHVDKLLAI------PGAKVLFGGKPLTNHSIpsiygAYEPTa 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 386 VF-----SNVTDEMRIAKEEIFGPVQQIMKFK--SIDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07126 367 VFvpleeIAIEENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
58-439 |
4.52e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 55.32 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 58 ADVDKAVKAARQAFQIgspWRTMDASERGRLLN--KLADLMERDRLLLATIEAINGG----KVFANAYLSDLGGSIKALK 131
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ---YRKCTLADREKIIEaiREALLSNAEELAEMAVEETGMGrvedKIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 132 YCAGWADkiHGqtipsdgdiFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP---AEQTPLTALHMAS- 207
Cdd:cd07121 81 TTAWSGD--NG---------LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELINk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 208 LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKlikeAAGKSNlKRVTLELGGKSPCIVFADADLDIA 287
Cdd:cd07121 150 AIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVK----AALSSG-KKAIGAGAGNPPVVVDETADIEKA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 288 VEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKsVERAKKYVLGNPLTQGI-------NQGPQIDKE----QHDKILD 356
Cdd:cd07121 225 ARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAA-MQRNGAYVLNDEQAEQLlevvlltNKGATPNKKwvgkDASKILK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 357 LIesGKKEGAKLECgggrwgnkgffvqptVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGL--AAGVFT 434
Cdd:cd07121 304 AA--GIEVPADIRL---------------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHS 366
|
....*
gi 14424442 435 KDLDR 439
Cdd:cd07121 367 KNVEN 371
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
56-455 |
9.13e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 54.41 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 56 DKADVDKAVKAARQAFQigsPWRtmDASERGRL---LNKLADLMERDrLLLATIEAINGGKVFANAYLSdlGGS------ 126
Cdd:cd07127 82 PQCDPDALLAAARAAMP---GWR--DAGARARAgvcLEILQRLNARS-FEMAHAVMHTTGQAFMMAFQA--GGPhaqdrg 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 127 IKALKYCAGWADKIHGQTIPsdgdIFTFTRREPI-----------GV-----CGQIIPWN-FPLLMfiwkigPALSCGNT 189
Cdd:cd07127 154 LEAVAYAWREMSRIPPTAEW----EKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 190 VVVKPAeqtPLTALHMASLIK-------EAGFPPGVVNIV--PGYGPTAGaAISSHMDVDKVAFTGSTQVGKLIKEAAGK 260
Cdd:cd07127 224 VIVKPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadTPEEPIAQ-TLATRPEVRIIDFTGSNAFGDWLEANARQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 261 snlKRVTLELGGKSPCIVFADADL-----DIAVEFAhhgvfYHQGQCCVAASRIFV---------EESVYDEfVRKSVER 326
Cdd:cd07127 300 ---AQVYTEKAGVNTVVVDSTDDLkamlrNLAFSLS-----LYSGQMCTTPQNIYVprdgiqtddGRKSFDE-VAADLAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 327 AKKYVLGNP-----LTQGInqgpqidkeQHDKILDLIESGKKEGAKLECGGGRwGNKGF---FVQPTVFSNVTDEMRIA- 397
Cdd:cd07127 371 AIDGLLADParaaaLLGAI---------QSPDTLARIAEARQLGEVLLASEAV-AHPEFpdaRVRTPLLLKLDASDEAAy 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14424442 398 KEEIFGPVQQIMKFKSIDDVIKRANNT--TYG-LAAGVFTKD---LDRaiTVSSALQAGV---------VWVN 455
Cdd:cd07127 441 AEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDpevVER--VQEAALDAGValsinltggVFVN 511
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
58-357 |
5.08e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 52.21 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 58 ADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATIEAINGG------KVFANAYLSDLGGSIKALK 131
Cdd:PRK15398 36 ASVDDAVAAAKVAQQR---YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNVAAAEKTPGVEDLT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 132 YCAGWADkiHGqtipsdgdiFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKP---AEQTPLTALHMAS- 207
Cdd:PRK15398 113 TEALTGD--NG---------LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgAKKVSLRAIELLNe 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 208 LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGstqvGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLDIA 287
Cdd:PRK15398 182 AIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVVVDETADIEKA 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 288 VEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRkSVERAKKYvlgnpltqginqgpQIDKEQHDKILDL 357
Cdd:PRK15398 257 ARDIVKGASFDNNLPCIAEKEVIVVDSVADELMR-LMEKNGAV--------------LLTAEQAEKLQKV 311
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
131-476 |
9.88e-07 |
|
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: 51.11 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 131 KYCagwaDKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIK 210
Cdd:cd07081 71 VYK----DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 211 EA----GFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGstqvGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLDI 286
Cdd:cd07081 147 QAavaaGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 287 AVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQ-------GINQGPQIDKEQHDKILDLIE 359
Cdd:cd07081 222 AVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQvqpvilkNGDVNRDIVGQDAYKIAAAAG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 360 SGKKEGAKLecgggrwgnkgFFVQPTVFsnvtDEMRIAKEEIFGPVQQIMKFKSIDDVIKRA----NNTTYGLAAGVFT- 434
Cdd:cd07081 302 LKVPQETRI-----------LIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSd 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 14424442 435 --KDLDRAITVSSALQAGVVWVNcymilsAQCPFGGFKMSGNGR 476
Cdd:cd07081 367 niKAIENMNQFANAMKTSRFVKN------GPCSQGGLGDLYNFR 404
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
154-330 |
1.13e-05 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 47.82 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 154 FTRREPIGVCGQIIPWNFPLLMFiWKIGPALSCGNTVVVKPAEQTP-LTALHMASLIK--EAGFPPGVVNIVPGYGPTAG 230
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVPLLPV-MSILMGLLVKNVNLLKVSSSDPfTAAALLASFADldPTHPLADSLSVVYWDGGSTQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 231 AAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGV-FYHQgQCCVAASRI 309
Cdd:pfam05893 162 LEDLIVANADVVIAWGGEDAINAIRECLKPG--KQWIDFGAKISFAVVDREAALDKAAERAADDIcVFDQ-QACLSPQTV 238
|
170 180
....*....|....*....|....
gi 14424442 310 FVE---ESVYDEFVRKSVERAKKY 330
Cdd:pfam05893 239 FVEsddKITPDEFAERLAAALAKR 262
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
158-456 |
2.27e-05 |
|
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: 46.72 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 158 EPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEA----GFPPGVVNIVPGYGPTAGAAI 233
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 234 SSHMDVDKVAFTGStqvGKLIKEA--AGKSNlkrvtleLG---GKSPCIVFADADLDIAVE-------FAHhgvfyhqGQ 301
Cdd:cd07122 174 MKHPDVDLILATGG---PGMVKAAysSGKPA-------IGvgpGNVPAYIDETADIKRAVKdiilsktFDN-------GT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 302 CCVAASRIFVEESVYDEFVRKsVERAKKYVLgnpltqginqgpqiDKEQHDKILDLIesgkkegakLECGGGRwgNK--- 378
Cdd:cd07122 237 ICASEQSVIVDDEIYDEVRAE-LKRRGAYFL--------------NEEEKEKLEKAL---------FDDGGTL--NPdiv 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 379 -----------GFFVQPTV------FSNVTDEMRIAKEEIFgPVQQIMKFKSIDDVIKRAN-NTTYGLA---AGVFTKDL 437
Cdd:cd07122 291 gksaqkiaelaGIEVPEDTkvlvaeETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKAReLLEYGGAghtAVIHSNDE 369
|
330
....*....|....*....
gi 14424442 438 DRAITVSSALQAGVVWVNC 456
Cdd:cd07122 370 EVIEEFALRMPVSRILVNT 388
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
154-314 |
3.06e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 39.95 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 154 FTRREPIGVCGQIIPWNFPLLMFiWKIGPALSCGNTVVVKPAEQTPLTALHMA-SLIKEAGFPPGVVNI----VPGYGPT 228
Cdd:cd07080 107 YIRAQPRGLVVHIIAGNVPLLPV-WSIVRGLLVKNVNLLKMSSSDPLTATALLrSLADVDPNHPLTDSIsvvyWPGGDAE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14424442 229 AGAAISSHMDVdKVAFTGSTQVgKLIKEAAGKSnlKRvTLELGGK-SPCIV----FADADL-DIAVEFAHHGVFYHQgQC 302
Cdd:cd07080 186 LEERILASADA-VVAWGGEEAV-KAIRSLLPPG--CR-LIDFGPKySFAVIdreaLESEKLaEVADALAEDICRYDQ-QA 259
|
170
....*....|..
gi 14424442 303 CVAASRIFVEES 314
Cdd:cd07080 260 CSSPQVVFVEKD 271
|
|
| DUF1487 |
pfam07368 |
Protein of unknown function (DUF1487); This family consists of several uncharacterized ... |
273-335 |
5.55e-03 |
|
Protein of unknown function (DUF1487); This family consists of several uncharacterized proteins from Drosophila melanogaster. The function of this family is unknown.
Pssm-ID: 254173 Cd Length: 215 Bit Score: 38.50 E-value: 5.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14424442 273 KSPC--IVFADADLDIAVEFAHHGVfyHQGQCCVAASRIFVEESVYDEF---VRKSVERAKKYVLGNP 335
Cdd:pfam07368 3 NSPRlmVIFEDGDVNSALHALVESL--HNPFAPGAVATVLVQESIRDEFverVRSRLKPLSERVANHP 68
|
|
| |
