|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
1-251 |
0e+00 |
|
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: 506.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENI 80
Cdd:cd07132 193 MQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFIN 160
Cdd:cd07132 273 KESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFIN 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 161 EREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKRE 240
Cdd:cd07132 353 SREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNME 432
|
250
....*....|.
gi 1595488129 241 GANKLRYPPNS 251
Cdd:cd07132 433 KLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
1-233 |
2.79e-151 |
|
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: 430.02 E-value: 2.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENI 80
Cdd:cd07087 193 MEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFIN 160
Cdd:cd07087 273 KESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFIN 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488129 161 EREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCL 233
Cdd:cd07087 353 SRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
1-265 |
7.45e-140 |
|
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: 401.88 E-value: 7.45e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENI 80
Cdd:cd07136 193 MEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFIN 160
Cdd:cd07136 273 LESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 161 EREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKRE 240
Cdd:cd07136 353 SRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD 432
|
250 260
....*....|....*....|....*
gi 1595488129 241 gaNKLRYPPNSqskvdwGKFFLLKR 265
Cdd:cd07136 433 --LPLRYPPYK------GKKKKLKK 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
1-254 |
3.46e-137 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 396.71 E-value: 3.46e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENI 80
Cdd:PTZ00381 202 MQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDP 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE--GQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINF 158
Cdd:PTZ00381 282 KKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEF 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 159 INEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLK 238
Cdd:PTZ00381 362 INSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTG 441
|
250
....*....|....*.
gi 1595488129 239 REGANKLRYPPNSQSK 254
Cdd:PTZ00381 442 NSFDLSLRYPPYTSFK 457
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
2-231 |
1.13e-123 |
|
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: 360.00 E-value: 1.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIK 81
Cdd:cd07135 202 EAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGAN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 82 ESPDYERIINLRHFKRILSLLE--GQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFI 159
Cdd:cd07135 282 ASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVI 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595488129 160 NEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRP 231
Cdd:cd07135 362 NSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
1-233 |
7.54e-121 |
|
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: 352.68 E-value: 7.54e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGEN- 79
Cdd:cd07134 193 MAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDa 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 -IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:cd07134 273 aRKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCL 233
Cdd:cd07134 353 EVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
1-231 |
1.12e-117 |
|
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: 344.85 E-value: 1.12e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGeNI 80
Cdd:cd07133 194 MRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKI---AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07133 273 ADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSL 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRP 231
Cdd:cd07133 353 DEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
1-233 |
1.11e-107 |
|
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: 319.36 E-value: 1.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNC-GQTCIAPDYILCEASLQNQIVWKIKETVKEFYGEN 79
Cdd:cd07137 194 MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGEN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEA 155
Cdd:cd07137 274 PKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEES 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 156 INFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCL 233
Cdd:cd07137 354 IEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-255 |
2.89e-92 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 281.62 E-value: 2.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYID---KDCDLDIVCRRITWGKYMNC-GQTCIAPDYILCEASLQNQIVWKIKETVKEFY 76
Cdd:PLN02203 201 MTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCaGQACIAIDYVLVEERFAPILIELLKSTIKKFF 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 77 GENIKESPDYERIINLRHFKRILSLLEGQKIA----FGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:PLN02203 281 GENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKI 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPC 232
Cdd:PLN02203 361 EDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
250 260
....*....|....*....|...
gi 1595488129 233 LLKSLKREgaNKLRYPPNSQSKV 255
Cdd:PLN02203 441 LRRSLLTE--FEFRYPPWNDFKL 461
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1-234 |
1.05e-85 |
|
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: 262.91 E-value: 1.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGEN- 79
Cdd:cd07078 192 MRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNp 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEAT--RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07078 272 LDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGKRLEGGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNsFPFGGVGSSGMGAYHGKHSFDTFSHQRPC 232
Cdd:cd07078 352 EEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
..
gi 1595488129 233 LL 234
Cdd:cd07078 431 TI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
1-264 |
8.47e-83 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 257.28 E-value: 8.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKY-MNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGEN 79
Cdd:PLN02174 205 MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEA 155
Cdd:PLN02174 285 PMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEES 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 156 INFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLK 235
Cdd:PLN02174 365 FDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYR 444
|
250 260
....*....|....*....|....*....
gi 1595488129 236 SLKreGANKLRYPPNSQskvdwGKFFLLK 264
Cdd:PLN02174 445 SLF--GDSAVRYPPYSR-----GKLRLLK 466
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-230 |
1.87e-69 |
|
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: 222.69 E-value: 1.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:COG1012 237 AAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIedavaEGAELLTGGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNsFPFGGVGSSGMGAYHGKHSFDTFSHQR 230
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
1-234 |
1.23e-61 |
|
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: 199.38 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKetvkefygeni 80
Cdd:cd06534 188 MKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 kespdyeriinlrhfkrilsllegqkiafggetdeatryiapTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFIN 160
Cdd:cd06534 257 ------------------------------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALAN 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595488129 161 EREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSfPFGGVGSSGMGAYHGKHSFDTFSHQRPCLL 234
Cdd:cd06534 295 DTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA-PFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-230 |
1.06e-58 |
|
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: 194.29 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:pfam00171 222 AEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEAT-RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:pfam00171 302 LDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMhFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQR 230
Cdd:pfam00171 382 EAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
1-230 |
4.99e-51 |
|
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: 173.95 E-value: 4.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07099 213 MAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGAD 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE-TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:cd07099 293 DIGDADIGPMTTARQLDIVRRHVDdavakGAKALTGGArSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADED 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQR 230
Cdd:cd07099 373 EAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1-226 |
6.50e-46 |
|
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: 160.89 E-value: 6.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07088 229 MEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVkVGDP 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATR--YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07088 309 FDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSL 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV----TGNDVIMHFtlnsfpFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07088 389 DEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETyinrENFEAMQGF------HAGWKKSGLGGADGKHGLEEY 460
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
1-220 |
1.28e-43 |
|
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: 154.38 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07098 219 MAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE-----TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:cd07098 299 LDGDVDVGAMISPARFDRLEELVadaveKGARLLAGGKryphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKA 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGK 220
Cdd:cd07098 379 SDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1-226 |
1.58e-42 |
|
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: 151.43 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07103 213 MAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNG 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEAT-RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:cd07103 293 LDEGTDMGPLINERAVEKVEALVEdavakGAKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTED 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMhfTLNSFPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07103 373 EVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI--SDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
1-230 |
1.35e-41 |
|
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: 148.87 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07093 213 MRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALkVGDP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR-----YIAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:cd07093 293 LDPDTEVGPLISKEHLEKVLGYVelaraEGATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPF 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimhfTLNSF-------PFGGVGSSGMGAYHGKHS 222
Cdd:cd07093 373 DDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTV---------WVNCWlvrdlrtPFGGVKASGIGREGGDYS 443
|
....*...
gi 1595488129 223 FDTFSHQR 230
Cdd:cd07093 444 LEFYTELK 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
2-230 |
1.13e-40 |
|
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: 146.14 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07104 196 ELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVGDPR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEA 155
Cdd:cd07104 276 DPDTVIGPLINERQVDRVHAIVEdavaaGARLLTGGTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEA 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 156 INFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVimhfTLNS---FPFGGVGSSGMGAYHGKHSFDTFSHQR 230
Cdd:cd07104 354 VELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ----TVNDephVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1-227 |
1.74e-39 |
|
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: 143.14 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF---YG 77
Cdd:cd07109 213 MRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALrvgPG 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 78 EnikESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATR----YIAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:cd07109 293 L---EDPDLGPLISAKQLDRVEGFVArararGARIVAGGRIAEGAPaggyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGND------VIMhftlnsfPFGGVGSSGMGAYHGKHS 222
Cdd:cd07109 370 FDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNygagggIEL-------PFGGVKKSGHGREKGLEA 442
|
....*
gi 1595488129 223 FDTFS 227
Cdd:cd07109 443 LYNYT 447
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1-215 |
3.88e-39 |
|
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: 142.73 E-value: 3.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GE 78
Cdd:cd07091 237 MEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGD 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 79 NIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07091 317 PFDPDTFQGPQVSKAQFDKILSYIesgkkEGATLLTGGERhGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTE 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLNSF----PFGGVGSSGMG 215
Cdd:cd07091 397 DEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN------TYNVFdaavPFGGFKQSGFG 457
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
1-226 |
7.76e-39 |
|
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: 142.16 E-value: 7.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY--GE 78
Cdd:cd07144 240 MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 79 NIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE----TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:cd07144 320 PFDDDTVVGPQVSKTQYDRVLSYIEkgkkeGAKLVYGGEkapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV---TGNDviMHFTLnsfPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSND--SDVGV---PFGGFKMSGIGRELGEYGLETY 474
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
1-220 |
1.68e-38 |
|
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: 140.36 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GEN 79
Cdd:cd07106 208 MASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:cd07106 288 LDPGTTLGPVQNKMQYDKVKELVEdakakGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDED 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHFTLN-SFPFGGVGSSGMGAYHGK 220
Cdd:cd07106 368 EVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGALDpDAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
2-230 |
2.13e-38 |
|
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: 140.16 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07150 216 EKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDeaTRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEA 155
Cdd:cd07150 296 DPDTVIGPLISPRQVERIKRQVEdavakGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEA 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488129 156 INFINEREKPLALYVFSHN-HKLIKrMIDETSSGGVTGNDVIMHFTLNSfPFGGVGSSGMGAYHGKHSFDTFSHQR 230
Cdd:cd07150 374 LELANDTEYGLSAAILTNDlQRAFK-LAERLESGMVHINDPTILDEAHV-PFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-215 |
2.91e-38 |
|
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: 140.04 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 8 LTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDY 86
Cdd:cd07149 224 LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 87 ERIINLRHFKRILSLLE-----GQKIAFGGETDEAtrYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINE 161
Cdd:cd07149 304 GPMISEAEAERIEEWVEeavegGARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAND 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1595488129 162 REKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvIMHFTLNSFPFGGVGSSGMG 215
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
1-227 |
1.54e-37 |
|
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: 137.71 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEfygenI 80
Cdd:cd07105 197 AETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEK-----L 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERI-INLRHFKRILSLLE-----GQKIAFGGETD--EATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07105 272 FAGPVVLGSlVSAAAADRVKELVDdalskGAKLVVGGLADesPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMH--FTLnsfPFGGVGSSGMGAYHGKHSFDTFS 227
Cdd:cd07105 352 EEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHdePTL---PHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
1-215 |
3.43e-37 |
|
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: 137.07 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07092 213 ARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIrVGDP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDE 154
Cdd:cd07092 293 DDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDE 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595488129 155 AINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTL-NSFPFGGVGSSGMG 215
Cdd:cd07092 373 AIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLaAEMPHGGFKQSGYG 431
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-230 |
8.60e-36 |
|
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: 133.23 E-value: 8.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKE-TVKEFYGEN 79
Cdd:cd07118 215 AAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVArSRKVRVGDP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDE--ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07118 295 LDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTV 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTFSHQR 230
Cdd:cd07118 375 DEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
1-226 |
9.32e-36 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 134.05 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDG 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATRYiAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVqdavsKGAKVLLGGKrhSLGGTFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:PLN02278 415 EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTE--VAPFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
1-227 |
1.46e-35 |
|
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: 132.73 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDC-DLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-G 77
Cdd:cd07112 220 LEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 78 ENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:cd07112 300 DPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITF 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN-----DVIMhftlnsfPFGGVGSSGMGAYHGKHSFD 224
Cdd:cd07112 380 DSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdegDITT-------PFGGFKQSGNGRDKSLHALD 452
|
...
gi 1595488129 225 TFS 227
Cdd:cd07112 453 KYT 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
2-230 |
2.02e-35 |
|
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: 132.29 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKefygeNIK 81
Cdd:cd07114 216 RAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARAR-----AIR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 82 -ESPDYER-----IINLRHFKRILSLL-----EGQKIAFGGET-----DEATRYIAPTVLTDVDPKTKVMQEEIFGPILP 145
Cdd:cd07114 291 vGDPLDPEtqmgpLATERQLEKVERYVarareEGARVLTGGERpsgadLGAGYFFEPTILADVTNDMRIAQEEVFGPVLS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 146 IVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimhFTLNSF--PFGGVGSSGMGAYHGKHSF 223
Cdd:cd07114 371 VIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT----YRALSPssPFGGFKDSGIGRENGIEAI 446
|
....*..
gi 1595488129 224 DTFSHQR 230
Cdd:cd07114 447 REYTQTK 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
4-215 |
8.74e-35 |
|
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: 130.55 E-value: 8.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 4 AAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKE 82
Cdd:cd07145 222 AGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLkVGDPLDE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 83 SPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATrYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAIN 157
Cdd:cd07145 302 STDLGPLISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 158 FINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMhFTLNSFPFGGVGSSGMG 215
Cdd:cd07145 381 IANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGGFKKSGIG 437
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
2-215 |
1.91e-34 |
|
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: 129.87 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GENI 80
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQvGSPM 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDE 154
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEAlAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595488129 155 AINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHFTLN-SFPFGGVGSSGMG 215
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQSGIG 456
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
2-230 |
2.54e-34 |
|
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: 129.34 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-----Y 76
Cdd:cd07152 207 EAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLpvgdpA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 77 GENIKESPdyerIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKN 151
Cdd:cd07152 287 TGQVALGP----LINARQLDRVHAIVDdsvaaGARLEAGGTYDG--LFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 152 VDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVimhfTLNS---FPFGGVGSSGMGAYHG-KHSFDTFS 227
Cdd:cd07152 361 DEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFGGMGASGNGSRFGgPANWEEFT 436
|
...
gi 1595488129 228 HQR 230
Cdd:cd07152 437 QWQ 439
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1-227 |
3.13e-34 |
|
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: 129.10 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07115 213 MQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLrPGDP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR-YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:cd07115 293 LDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEE 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLNSF----PFGGVGSSGMGAYHGKHSFDTFS 227
Cdd:cd07115 373 EALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN------TYNRFdpgsPFGGYKQSGFGREMGREALDEYT 444
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
1-226 |
3.50e-34 |
|
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: 129.16 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDivcRRITWG---KYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-Y 76
Cdd:cd07138 226 AEAAADTVKRVALELGGKSANIILDDADLE---KAVPRGvaaCFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 77 GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG----ETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIV 147
Cdd:cd07138 303 GDPRDPATTLGPLASAAQFDRVQGYIqkgieEGARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSII 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 148 PVKNVDEAINFINEREKPLALYVFSHN----HKLIKRMidetSSGGVTGNDVIMHFtlnSFPFGGVGSSGMGAYHGKHSF 223
Cdd:cd07138 383 PYDDEDEAIAIANDTPYGLAGYVWSADperaRAVARRL----RAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGL 455
|
...
gi 1595488129 224 DTF 226
Cdd:cd07138 456 EEF 458
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
1-227 |
8.96e-34 |
|
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: 128.20 E-value: 8.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07119 230 MRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIkLGNG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:cd07119 310 LDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKrpTGDELAkgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERF 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS 227
Cdd:cd07119 390 DTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-230 |
9.87e-34 |
|
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: 127.74 E-value: 9.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07089 219 MAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKN 151
Cdd:cd07089 299 ADPGTVMGPLISAAQRDRVEGYIargrdEGARLVTGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDD 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 152 VDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDViMHFTLNSfPFGGVGSSGMGAYHGKHSFDTFSHQR 230
Cdd:cd07089 379 DDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGG-GGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
2-215 |
9.87e-34 |
|
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: 127.75 E-value: 9.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHltpVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07147 220 RAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALkTGDPK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATryIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEA 155
Cdd:cd07147 297 DDATDVGPMISESEAERVEGWVNeavdaGAKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEA 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 156 INFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDViMHFTLNSFPFGGVGSSGMG 215
Cdd:cd07147 375 LAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV-PTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
1-215 |
2.33e-33 |
|
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: 126.71 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWG-KYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGE 78
Cdd:cd07108 212 YRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 79 NIKESPDYERIINLRHFKRILSLLE------GQKIAFGGETDEATR-----YIAPTVLTDVDPKTKVMQEEIFGPILPIV 147
Cdd:cd07108 292 PLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGGPLPGEGPladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAI 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 148 PVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSFPFGGVGSSGMG 215
Cdd:cd07108 372 PWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ--GGGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1-226 |
5.09e-33 |
|
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: 126.15 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07139 232 AAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDP 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATR--YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKN 151
Cdd:cd07139 312 LDPATQIGPLASARQRERVEGYIakgraEGARLVTGGGRpAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDD 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 152 VDEAINFINEREKPLALYVFSHNH----KLIKRMidetSSGGVTGNDVIMHFTLnsfPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07139 392 EDDAVRIANDSDYGLSGSVWTADVerglAVARRI----RTGTVGVNGFRLDFGA---PFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
1-227 |
2.66e-32 |
|
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: 124.18 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF---- 75
Cdd:cd07143 240 MEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLkvgd 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 76 -YGENIKESPDYERIinlrHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:cd07143 320 pFAEDTFQGPQVSQI----QYERIMSYIEsgkaeGATVETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIFGPVVAVIK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNhklIKRMIdETSSGGVTGNDVIMHFTLNSF--PFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07143 396 FKTEEEAIKRANDSTYGLAAAVFTNN---INNAI-RVANALKAGTVWVNCYNLLHHqvPFGGYKQSGIGRELGEYALENY 471
|
.
gi 1595488129 227 S 227
Cdd:cd07143 472 T 472
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
1-226 |
3.20e-32 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 122.92 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:PRK10090 167 MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVqFGNP 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKES-PDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATRYI-APTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:PRK10090 247 AERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTL 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN----DVIMHFtlnsfpFGGVGSSGMGAYHGKHSFDTF 226
Cdd:PRK10090 327 EEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINrenfEAMQGF------HAGWRKSGIGGADGKHGLHEY 398
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
12-219 |
3.82e-32 |
|
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: 123.24 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 12 TLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERII 90
Cdd:cd07146 225 LLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 91 N---LRHF-KRILSLLE-GQKIAFGGETDEAtrYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKP 165
Cdd:cd07146 305 DeeaAIQIeNRVEEAIAqGARVLLGNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1595488129 166 LALYVFSHNHKLIKRMIDETSSGGVTGNDViMHFTLNSFPFGGVGSSGMGAYHG 219
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
1-228 |
6.02e-32 |
|
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: 123.23 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07131 231 GETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE-----TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:cd07131 311 LDEETDMGPLINEAQLEKVLNYNeigkeEGATLLLGGErltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN------DVIMhftlnsfPFGGVGSSGMGayH---GK 220
Cdd:cd07131 391 SSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaptigaEVHL-------PFGGVKKSGNG--HreaGT 461
|
....*...
gi 1595488129 221 HSFDTFSH 228
Cdd:cd07131 462 TALDAFTE 469
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1-236 |
1.41e-31 |
|
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: 122.03 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:cd07090 211 MSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIrIGDP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE----TD--EATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:cd07090 291 LDEDTQMGALISEEHLEKVLGYIesakqEGAKVLCGGErvvpEDglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimhFTLNS--FPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07090 371 FDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNISPveVPFGGYKQSGFGRENGTAALEHY 446
|
250
....*....|
gi 1595488129 227 SHqrpclLKS 236
Cdd:cd07090 447 TQ-----LKT 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
2-228 |
8.42e-31 |
|
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: 119.66 E-value: 8.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07102 212 RAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKIAFGGET----DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKN 151
Cdd:cd07102 292 DPSTTLGPVVSARAADFVRAQIAdaiakGARALIDGALfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKS 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 152 VDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DvimhFTLNSFPFGGVGSSGMGAYHGKHSFDTFSH 228
Cdd:cd07102 372 DAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcD----YLDPALAWTGVKDSGRGVTLSRLGYDQLTR 446
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
1-213 |
1.14e-30 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 120.04 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK------HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKE 74
Cdd:PRK03137 267 YERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 75 FYGENIKESPDYERIINLRHFKRILSLLE-GQ---KIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:PRK03137 347 LTVGNPEDNAYMGPVINQASFDKIMSYIEiGKeegRLVLGGEGDDSKGYfIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSG------GVTGNDVIMHftlnsfPFGGVGSSG 213
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGnlyfnrGCTGAIVGYH------PFGGFNMSG 490
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
2-227 |
5.90e-30 |
|
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: 117.41 E-value: 5.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07151 228 ELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALpYGDPS 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEA 155
Cdd:cd07151 308 DPDTVVGPLINESQVDGLLDKIEqaveeGATLLVGGEAEG--NVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEA 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595488129 156 INFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSfPFGGVGSSGMGAYHGKHSFDTFS 227
Cdd:cd07151 386 LELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
2-226 |
7.17e-30 |
|
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: 116.79 E-value: 7.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07100 192 AEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDY---ERiinlrhfKRILSLLEGQ---------KIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIV 147
Cdd:cd07100 272 DEDTDLgplAR-------KDLRDELHEQveeavaagaTLLLGGKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVI 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 148 PVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSFPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07100 345 KVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING--MVKSDPRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
1-215 |
8.85e-30 |
|
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: 117.06 E-value: 8.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYI-----DKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVkef 75
Cdd:cd07559 231 MQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERF--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 76 ygENIKE-SP-DYERII----NLRHFKRILSLL-----EGQKIAFGGE-----TDEATRYIAPTVLTDVDPKTKVMQEEI 139
Cdd:cd07559 308 --EAIKVgNPlDPETMMgaqvSKDQLEKILSYVdigkeEGAEVLTGGErltlgGLDKGYFYEPTLIKGGNNDMRIFQEEI 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 140 FGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLNSFP----FGGVGSSGMG 215
Cdd:cd07559 386 FGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN------CYHQYPahapFGGYKKSGIG 459
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
1-219 |
1.03e-29 |
|
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: 116.71 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGkyMN---CGQTCIAPDYILCEASLQNQIVWKIKETVKEFY- 76
Cdd:cd07107 211 MRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNftwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKv 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 77 GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG--ETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPI 146
Cdd:cd07107 289 GDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrPEGPALEggfYVEPTVFADVTPGMRIAREEIFGPVLSV 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488129 147 VPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHG 219
Cdd:cd07107 369 LRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
1-226 |
1.23e-29 |
|
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: 116.82 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKE-----TVKE 74
Cdd:cd07142 237 MQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKAralkrVVGD 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 75 FYGENIKESPDyeriINLRHFKRILSLL-----EGQKIAFGGE-TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:cd07142 317 PFRKGVEQGPQ----VDKEQFEKILSYIehgkeEGATLITGGDrIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVimhFTLnSFPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07142 393 FKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA-SIPFGGYKMSGIGREKGIYALNNY 468
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
2-216 |
1.32e-29 |
|
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: 116.58 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07097 232 AAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALkVGDAL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATR--YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGERlKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVIMHFTLnsfPFGGVGSSGMGA 216
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVDYHV---PFGGRKGSSYGP 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
1-230 |
7.48e-29 |
|
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: 114.37 E-value: 7.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVkefygENI 80
Cdd:cd07110 216 MQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAA-----EAI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYER------IINLRHFKRILSLL-----EGQKIAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPI 146
Cdd:cd07110 291 RVGDPLEEgvrlgpLVSQAQYEKVLSFIargkeEGARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 147 VPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:cd07110 371 RSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNY 448
|
....
gi 1595488129 227 SHQR 230
Cdd:cd07110 449 LEVK 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
2-215 |
1.45e-28 |
|
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: 113.70 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKEtvkEFygENIK 81
Cdd:cd07117 232 IAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKE---KF--ENVK 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 82 ----ESPDYE--RIINLRHFKRILSLL-----EGQKIAFGGE-----TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILP 145
Cdd:cd07117 307 vgnpLDPDTQmgAQVNKDQLDKILSYVdiakeEGAKILTGGHrltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVAT 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595488129 146 IVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLNSFP----FGGVGSSGMG 215
Cdd:cd07117 387 VIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN------TYNQIPagapFGGYKKSGIG 454
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
1-216 |
6.15e-28 |
|
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: 112.32 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK------HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKE 74
Cdd:cd07124 262 YERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 75 F-YGENIKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDE-ATR--YIAPTVLTDVDPKTKVMQEEIFGPILPI 146
Cdd:cd07124 342 LkVGDPEDPEVYMGPVIDKGARDRIRRYIEigksEGRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAV 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488129 147 VPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSG------GVTGNDVIMHftlnsfPFGGVGSSGMGA 216
Cdd:cd07124 422 IKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGnlyanrKITGALVGRQ------PFGGFKMSGTGS 491
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
3-215 |
9.47e-28 |
|
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: 111.37 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 3 AAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIK 81
Cdd:cd07094 219 RANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 82 ESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRYiaPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAI 156
Cdd:cd07094 299 EDTDVGPLISEEAAERVERWVEeaveaGARLLCGGERDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAI 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 157 NFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDViMHFTLNSFPFGGVGSSGMG 215
Cdd:cd07094 377 RIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1-215 |
1.25e-27 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 111.15 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGEN 79
Cdd:PRK13473 233 LSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLkVGDP 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE------GQKIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVErakalgHIRVVTGGEApDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTLNS-FPFGGVGSSGMG 215
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMLVSeMPHGGQKQSGYG 453
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
1-227 |
1.52e-27 |
|
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: 110.90 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKI-----KETVKE 74
Cdd:cd07141 241 QQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSverakKRVVGN 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 75 FYGENIKESPDyeriINLRHFKRILSLL-----EGQKIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:cd07141 321 PFDPKTEQGPQ----IDEEQFKKILELIesgkkEGAKLECGGKRhGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNhklIKRMIdeTSSGGVTGNDVIMHfTLNSF----PFGGVGSSGMGAYHGKHSFD 224
Cdd:cd07141 397 FKTIDEVIERANNTTYGLAAAVFTKD---IDKAI--TFSNALRAGTVWVN-CYNVVspqaPFGGYKMSGNGRELGEYGLQ 470
|
...
gi 1595488129 225 TFS 227
Cdd:cd07141 471 EYT 473
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1-228 |
2.97e-27 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 110.30 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF---- 75
Cdd:PLN02766 254 MQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWvvgd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 76 -YGENIKESPDYERiinlRHFKRILSLL-----EGQKIAFGGE-TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:PLN02766 334 pFDPRARQGPQVDK----QQFEKILSYIehgkrEGATLLTGGKpCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHFTL-NSFPFGGVGSSGMGAYHGKHSFDTFS 227
Cdd:PLN02766 410 FKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFdPDCPFGGYKMSGFGRDQGMDALDKYL 486
|
.
gi 1595488129 228 H 228
Cdd:PLN02766 487 Q 487
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
10-215 |
8.41e-27 |
|
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: 108.81 E-value: 8.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 10 PVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVkefygENIK------ES 83
Cdd:cd07082 244 RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV-----AKLKvgmpwdNG 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 84 PDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATrYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINF 158
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDdavakGATVLNGGGREGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488129 159 INEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlNSFPFGGVGSSGMG 215
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DHFPFLGRKDSGIG 453
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
2-220 |
4.72e-25 |
|
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: 103.54 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07101 213 ERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALrLGAAL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKIAFGGET--DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:cd07101 293 DYGPDMGSLISQAQLDRVTAHVDdavakGATVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDD 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvIMHFTLNSF--PFGGVGSSGMGAYHGK 220
Cdd:cd07101 373 EAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE-GYAAAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
2-215 |
5.52e-25 |
|
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: 103.80 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07086 233 ETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVrIGDPL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLLE-----GQKIAFGGET---DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNV 152
Cdd:cd07086 313 DEGTLVGPLINQAAVEKYLNAIEiaksqGGTVLTGGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595488129 153 DEAINFINEREKPLALYVFSHNHKLIKRMIDETSS--------GGVTGNDVIMhftlnsfPFGGVGSSGMG 215
Cdd:cd07086 393 EEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcgivnvnIPTSGAEIGG-------AFGGEKETGGG 456
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
1-226 |
1.74e-24 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 102.58 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWK-----IKETVKE 74
Cdd:PLN02466 291 LELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKakaraLKRVVGD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 75 FYGENIKESPDyeriINLRHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:PLN02466 371 PFKKGVEQGPQ----IDSEQFEKILRYIKsgvesGATLECGGDRFGSKGYyIQPTVFSNVQDDMLIAQDEIFGPVQSILK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVIMhftlNSFPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:PLN02466 447 FKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD----AAIPFGGYKMSGIGREKGIYSLNNY 522
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
1-230 |
3.19e-24 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 101.73 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKefygeNI 80
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAK-----NI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYER------IINLRHFKRILSLL-----EGQKIAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPI 146
Cdd:PLN02467 322 KISDPLEEgcrlgpVVSEGQYEKVLKFIstaksEGATILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 147 VPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFC--QAPWGGIKRSGFGRELGEWGLENY 479
|
....
gi 1595488129 227 SHQR 230
Cdd:PLN02467 480 LSVK 483
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-215 |
9.95e-24 |
|
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: 100.26 E-value: 9.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGE 78
Cdd:cd07140 243 MKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMkIGD 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 79 NIKESPDYERIINLRHFKRIL-----SLLEGQKIAFGG-ETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKN- 151
Cdd:cd07140 323 PLDRSTDHGPQNHKAHLDKLVeycerGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDg 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 152 -VDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLN----SFPFGGVGSSGMG 215
Cdd:cd07140 403 dVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN------TYNktdvAAPFGGFKQSGFG 465
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-226 |
1.07e-22 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 97.28 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GEN 79
Cdd:PRK11241 242 MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRIL-----SLLEGQKIAFGGETDE-ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD 153
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488129 154 EAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNsfPFGGVGSSGMGAYHGKHSFDTF 226
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLGREGSKYGIEDY 472
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
4-223 |
1.87e-22 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 96.47 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 4 AAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKE 82
Cdd:PRK13968 224 AGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALkMGDPRDE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 83 SPDYERI--INLR---HFKRILSLLEGQKIAFGGETDE-ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAI 156
Cdd:PRK13968 304 ENALGPMarFDLRdelHHQVEATLAEGARLLLGGEKIAgAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHAL 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488129 157 NFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimhfTLNSF-------PFGGVGSSGMG---AYHGKHSF 223
Cdd:PRK13968 384 ELANDSEFGLSATIFTTDETQARQMAARLECGGV---------FINGYcasdarvAFGGVKKSGFGrelSHFGLHEF 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
1-227 |
3.09e-22 |
|
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: 95.87 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKEtvkefYGENI 80
Cdd:cd07120 214 MAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAA-----RLAAV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYER------IINLRHFKRILSLLE------GQKIAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILP 145
Cdd:cd07120 289 KVGPGLDPasdmgpLIDRANVDRVDRMVEraiaagAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLT 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 146 IVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTL-NSFPFGGVGSSGMGAYHGKHSFD 224
Cdd:cd07120 369 LETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLfAEAEEGGYRQSGLGRLHGVAALE 445
|
...
gi 1595488129 225 TFS 227
Cdd:cd07120 446 DFI 448
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
10-219 |
8.60e-22 |
|
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: 94.57 E-value: 8.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 10 PVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYER 88
Cdd:cd07083 265 RLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 89 IINLRHFKRILSLLEGQK----IAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD--EAINFINE 161
Cdd:cd07083 345 VIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANS 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 162 REKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHG 219
Cdd:cd07083 425 TPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
2-227 |
3.44e-21 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 93.04 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDC-DLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GEN 79
Cdd:PRK09847 255 DAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQpGHP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATrYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDE 154
Cdd:PRK09847 335 LDPATTMGTLIDCAHADSVHSFIRegeskGQLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488129 155 AINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV---TGNDVIMhftlnSFPFGGVGSSGMGAYHGKHSFDTFS 227
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFT 484
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-219 |
3.70e-21 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 93.02 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKefygeNIK 81
Cdd:PRK09407 249 EQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVR-----AMR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 82 ESPDYE------RIINLRHFKRILSLLE-----GQKIAFGGET--DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVP 148
Cdd:PRK09407 324 LGAGYDysadmgSLISEAQLETVSAHVDdavakGATVLAGGKArpDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYP 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595488129 149 VKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMH-FTLNSFPFGGVGSSGMGAYHG 219
Cdd:PRK09407 404 VADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAaWGSVDAPMGGMKDSGLGRRHG 475
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
2-226 |
6.99e-21 |
|
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: 91.81 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENI 80
Cdd:cd07085 232 ERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 81 KESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATRY-----IAPTVLTDVDPKTKVMQEEIFGPILPIVPVK 150
Cdd:cd07085 312 DPGADMGPVISPAAKERIEGLIesgveEGAKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVD 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 151 NVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtGNDVIMHFTLNSFPFGGVGSSGMGAYH--GKHSFDTF 226
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMV-GINVPIPVPLAFFSFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
11-221 |
2.17e-20 |
|
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: 90.53 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 11 VTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERI 89
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 90 INLRHFKRILSLLEGQKiAFGGETDEATR-------YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINER 162
Cdd:cd07111 332 VDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488129 163 EKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLNSF----PFGGVGSSGMGAYHGKH 221
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWIN------GHNLFdaaaGFGGYRESGFGREGGKE 467
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
9-215 |
5.46e-18 |
|
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: 83.62 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 9 TPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYE 87
Cdd:cd07148 226 TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVG 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 88 RIINLRHFKRILSLLE-----GQKIAFGGETDEATRYiAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINER 162
Cdd:cd07148 306 PLIRPREVDRVEEWVNeavaaGARLLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSL 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595488129 163 EKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimH--FTLNSFPFGGVGSSGMG 215
Cdd:cd07148 385 PVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFRVDWMPFAGRRQSGYG 436
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-215 |
9.41e-18 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 83.01 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GEN 79
Cdd:PRK13252 237 MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRiGDP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 IKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPV 149
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIekgkaEGARLLCGGErlTEGGFAngaFVAPTVFTDCTDDMTIVREEIFGPVMSVLTF 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488129 150 KNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimhfTLNSF-------PFGGVGSSGMG 215
Cdd:PRK13252 397 DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIC---------WINTWgespaemPVGGYKQSGIG 460
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-216 |
1.99e-17 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 82.11 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 8 LTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYE 87
Cdd:PLN00412 258 MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDIT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 88 RIINLRHFKRILSLLEG--QKIA-FGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREK 164
Cdd:PLN00412 338 PVVSESSANFIEGLVMDakEKGAtFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNF 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595488129 165 PLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlNSFPFGGVGSSGMGA 216
Cdd:PLN00412 418 GLQGCVFTRDINKAILISDAMETGTVQINSAPARGP-DHFPFQGLKDSGIGS 468
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
4-223 |
4.24e-16 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 77.86 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 4 AAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKE 82
Cdd:PRK09406 221 AGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDP 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 83 SPDYERIINLRHFKRILSLLE-----GQKIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAI 156
Cdd:PRK09406 301 DTDVGPLATEQGRDEVEKQVDdavaaGATILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAI 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 157 NFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSFPFGGVGSSGMG---AYHGKHSF 223
Cdd:PRK09406 381 EIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
1-236 |
1.23e-15 |
|
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: 76.72 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 1 MEAAAKHLTPVTLELGGKSP-----CYIDKDcdlDIVCRRITWGKYM---NCGQTCIAPDYILCEASLQNQIVWKIKETV 72
Cdd:cd07116 231 MQYASENIIPVTLELGGKSPniffaDVMDAD---DAFFDKALEGFVMfalNQGEVCTCPSRALIQESIYDRFMERALERV 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 73 KEFygenIKESP-DYERII----NLRHFKRILSLL-----EGQKIAFGGET-----DEATRYIAPTVLTDVDpKTKVMQE 137
Cdd:cd07116 308 KAI----KQGNPlDTETMIgaqaSLEQLEKILSYIdigkeEGAEVLTGGERnelggLLGGGYYVPTTFKGGN-KMRIFQE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 138 EIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvIMHFTLNSFPFGGVGSSGMGAY 217
Cdd:cd07116 383 EIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIGRE 460
|
250
....*....|....*....
gi 1595488129 218 HGKHSFDTFSHQRpCLLKS 236
Cdd:cd07116 461 NHKMMLDHYQQTK-NLLVS 478
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
14-213 |
7.89e-12 |
|
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: 65.30 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 14 ELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEfygenIKESPDYE------ 87
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKE-----IKMGDPDDfsnfmg 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 88 RIINLRHFKRILSLLE------GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPI--VPVKNVDEAINF 158
Cdd:cd07123 359 AVIDEKAFDRIKGYIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLEL 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 159 INEREkPLALY--VFSHNHKLIKRM------------IDETSSGGVTGNDvimhftlnsfPFGGVGSSG 213
Cdd:cd07123 439 VDTTS-PYALTgaIFAQDRKAIREAtdalrnaagnfyINDKPTGAVVGQQ----------PFGGARASG 496
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
13-213 |
3.46e-11 |
|
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: 63.06 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 13 LELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTC------IAPDYILCEASLQnQIVWKIKETV-------KEFYGEN 79
Cdd:cd07095 205 LEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCtcarrlIVPDGAVGDAFLE-RLVEAAKRLRigapdaePPFMGPL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 80 I--KESPDYERIINLRHFKRILSLLEGQKIafggetDEATRYIAPTVLtDVDPKTKVMQEEIFGPILPIVPVKNVDEAIN 157
Cdd:cd07095 284 IiaAAAARYLLAQQDLLALGGEPLLAMERL------VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIA 356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488129 158 FINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMhFTLNSFPFGGVGSSG 213
Cdd:cd07095 357 LANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT-GASSTAPFGGVGLSG 411
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
2-187 |
1.11e-10 |
|
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: 61.84 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 2 EAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILceasLQNQIVWKIKETVKEFY----- 76
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI----VHESIYDEVLERLKKAYkqvri 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 77 GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE-TDEATRYIAPTVLTdVDPKTKVMQEEIFGPILPIVPVK 150
Cdd:cd07130 308 GDPLDDGTLVGPLHTKAAVDNYLAAIEeaksqGGTVLFGGKvIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFD 386
|
170 180 190
....*....|....*....|....*....|....*..
gi 1595488129 151 NVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 187
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGS 423
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-232 |
2.83e-10 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 60.62 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 13 LELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKES----PDYE 87
Cdd:PLN02315 265 LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVkIGDPLEKGtllgPLHT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 88 RIiNLRHFKRILSLLEGQ--KIAFGGETDEAT-RYIAPTVLtDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREK 164
Cdd:PLN02315 345 PE-SKKNFEKGIEIIKSQggKILTGGSAIESEgNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQ 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488129 165 PLALYVFSHNHKLIKRMIDETSSG-GVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPC 232
Cdd:PLN02315 423 GLSSSIFTRNPETIFKWIGPLGSDcGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
101-228 |
1.17e-09 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 58.99 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 101 LLEGQKIAFGGEtdEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKR 180
Cdd:PLN02419 456 LLDGRDIVVPGY--EKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARK 533
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1595488129 181 MIDETSSGGVtGNDVIMHFTLNSFPFGGVGSSGMG--AYHGKHSFDTFSH 228
Cdd:PLN02419 534 FQMDIEAGQI-GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
7-191 |
7.36e-09 |
|
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: 56.09 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 7 HLTPVTLELGGKSPCYIDKDCD-LDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQivwKIKETVKEFYGENIKESPD 85
Cdd:cd07084 200 KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKT---PLVEKLKALLARRKLEDLL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 86 YERIINLRHFKRILSL--LEGQKIAFGGETDEATRY-------IAPTVLTDVDP---KTKVMQEEIFGPILPIVPVKNVD 153
Cdd:cd07084 277 LGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQ 356
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1595488129 154 EA-INFINEREK-PLALYVFSHNHKLIKRMIDETSSGGVT 191
Cdd:cd07084 357 LAlVLELLERMHgSLTAAIYSNDPIFLQELIGNLWVAGRT 396
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
118-216 |
9.14e-07 |
|
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: 49.89 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 118 RYIAPTVLTDVdpKTKVMQEEIFGPILPIV--PVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDV 195
Cdd:cd07125 389 YFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRN 466
|
90 100
....*....|....*....|.
gi 1595488129 196 IMHFTLNSFPFGGVGSSGMGA 216
Cdd:cd07125 467 ITGAIVGRQPFGGWGLSGTGP 487
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
13-213 |
1.55e-06 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 49.19 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 13 LELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ-IVWKIKETVK-----EFYGENikeSPDY 86
Cdd:PRK09457 242 LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKrltvgRWDAEP---QPFM 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 87 ERIINLRHFKRilsLLEGQK--IAFGGET-------DEATRYIAPTVLtDVDPKTKVMQEEIFGPILPIVPVKNVDEAIN 157
Cdd:PRK09457 319 GAVISEQAAQG---LVAAQAqlLALGGKSllemtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIR 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 158 FINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimhfTLN----SFPFGGVGSSG 213
Cdd:PRK09457 395 LANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNK-----PLTgassAAPFGGVGASG 449
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
10-219 |
1.79e-06 |
|
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: 48.75 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 10 PVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYER 88
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLLTTDVGP 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 89 IINLRHFKRILSLLEGQKiAFGGETDEATR----------YIAPTV--LTDVDPktkvMQEEIFGPILPIVPVK--NVDE 154
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMS-QTQKKIAQLTLddsracqhgtFVAPTLfeLDDIAE----LSEEVFGPVLHVVRYKarELDQ 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595488129 155 AINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHG 219
Cdd:TIGR01238 423 IVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
96-182 |
1.05e-05 |
|
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: 46.49 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 96 KRILSLLEGQKIAFGGETDEATR--------YIAPTVLT--DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKP 165
Cdd:cd07128 345 AAVATLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGS 424
|
90
....*....|....*..
gi 1595488129 166 LALYVFSHNHKLIKRMI 182
Cdd:cd07128 425 LVASVVTNDPAFARELV 441
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
108-156 |
1.35e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 39.89 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1595488129 108 AFGGETDEATRYIaptvLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAI 156
Cdd:PRK15398 334 AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAI 378
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
118-164 |
1.66e-03 |
|
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: 39.53 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488129 118 RYIAPTVLTDVDPKTKVM-----------QEEIFGPILPIVPVKNVDEAINFINEREK 164
Cdd:cd07121 299 SKILKAAGIEVPADIRLIivetdkdhpfvVEEQMMPILPVVRVKNFDEAIELAVELEH 356
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
106-215 |
5.11e-03 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 38.26 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488129 106 KIAFGGETDEATrYIAPTV--LTDVDpktkVMQEEIFGPILPIVPVK--NVDEAINFINEREKPLALYVFSHNHKLIKRM 181
Cdd:PRK11904 897 QLPLPAGTENGH-FVAPTAfeIDSIS----QLEREVFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRI 971
|
90 100 110
....*....|....*....|....*....|....
gi 1595488129 182 IDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMG 215
Cdd:PRK11904 972 ADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| |
