|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-475 |
0e+00 |
|
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: 723.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 25 MEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRG 102
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKemKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 103 EVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAE 182
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 183 VTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLRKVSLELGNNSATVVH 262
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 263 KDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVK 342
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 343 EAVEEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMK 422
Cdd:cd07149 321 EAVEGGARLLTGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 654965072 423 AAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07149 401 AARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-477 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 601.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 1 MTSltqvKQYGLYVNGEW--ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAE 76
Cdd:COG1012 1 MTT----PEYPLFIGGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAwaATPPAERAAILLRAAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 77 LLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVesaqGSENRMAFTVKVPVGVVAAITPFN 156
Cdd:COG1012 77 LLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPS----DAPGTRAYVRREPLGVVGAITPWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 157 VPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRV 236
Cdd:COG1012 153 FPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 237 GELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLV 314
Cdd:COG1012 233 GRRIAAAAAenLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 315 VGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQ 390
Cdd:COG1012 313 VGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpdgeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 391 YDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEE 470
Cdd:COG1012 393 FDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTET 472
|
....*..
gi 654965072 471 RIIVLNL 477
Cdd:COG1012 473 KTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-473 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 586.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 19 ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKS 96
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPawRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 97 IRESRGEVERAATTLQISAEEAKRIHGEGVPVesaqgSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSV 176
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRLDGETLPS-----DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 177 VLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELG 254
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAqnLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 255 NNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEA 334
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 335 ERVEEWVKEAVEEGAKIELGGK---RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAG 411
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEaglDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654965072 412 LFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERII 473
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
26-475 |
0e+00 |
|
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: 580.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 26 EVLNKYTQQPAAEISVATKDDVNKAVASAKEALKNT--FSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGE 103
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMraLPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEV 183
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGEVLPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 184 TPICALKLAELMEEAGLPKGRLQVL--TGDGAEIgewLLENQDVNMFTFTGSPRVGELIRSKAGLRKVSLELGNNSATVV 261
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLpcSRDDADL---LVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWV 341
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 342 KEAVEEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAM 421
Cdd:cd07147 319 NEAVDAGAKLLTGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKAL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 654965072 422 KAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07147 399 RAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-475 |
0e+00 |
|
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: 550.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 25 MEVLNKYTQQPAAEISVATKDDVNKAVASAKEA--LKNTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRG 102
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGaeNRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 103 EVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAE 182
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 183 VTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLRKVSLELGNNSATVVH 262
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 263 KDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVK 342
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 343 EAVEEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMK 422
Cdd:cd07094 321 EAVEAGARLLCGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 654965072 423 AAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07094 401 AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-475 |
0e+00 |
|
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: 538.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 25 MEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRG 102
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDvmSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 103 EVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAE 182
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 183 VTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLR--KVSLELGNNSATV 260
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTgkKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 261 VHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEW 340
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 341 VKEAVEEGAKIELGGKRD-GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQF 419
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDeGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 654965072 420 AMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07145 401 ALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
48-475 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 518.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 48 NKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEg 125
Cdd:cd07078 1 DAAVAAARAAFKAwaALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 126 vpvESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRL 205
Cdd:cd07078 80 ---VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 206 QVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAG 283
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAenLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 284 QVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKRD----G 359
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeggkG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 360 AFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASA 439
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 654965072 440 YRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07078 397 GAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-469 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 514.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALK---NTfSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGE 103
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKtwrKT-TARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRIHGEGVPVESAqgseNRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEV 183
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGRTIPSPAP----GKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 184 TPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA--GLRKVSLELGNNSATVV 261
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAadTVKRVSLELGGNAPFIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWV 341
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 342 KEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQ 418
Cdd:cd07103 316 EDAVAKGAKVLTGGKRlglGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 654965072 419 FAMKAAREIEVGGLIVNDASAYrVDHMPYGGVKKSGNGKEGPKYAIEEMTE 469
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLIS-DAEAPFGGVKESGLGREGGKEGLEEYLE 445
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
26-475 |
3.86e-166 |
|
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: 476.47 E-value: 3.86e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 26 EVLNKYTQQPAAEISVATKDDVNKAVASAKeALKNTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVE 105
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAA-SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 106 RAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTP 185
Cdd:cd07146 81 RAADVLRFAAAEALRDDGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 186 ICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLRKVSLELGNNSATVVHKDA 265
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 266 DLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAV 345
Cdd:cd07146 241 DLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 346 EEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAR 425
Cdd:cd07146 321 AQGARVLLGNQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 654965072 426 EIEVGGLIVNDASAYRVDHMPYGGVKKSGNG-KEGPKYAIEEMTEERIIVL 475
Cdd:cd07146 401 RLDVGTVNVNEVPGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-473 |
3.25e-160 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 460.46 E-value: 3.25e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 46 DVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHG 123
Cdd:cd07104 1 DVDRAYAAAAAAQKAwaATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 124 EGVPvesaQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPIC-ALKLAELMEEAGLPK 202
Cdd:cd07104 81 EILP----SDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 203 GRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFN 280
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGrhLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 281 NAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKRDGA 360
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 361 FYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAY 440
Cdd:cd07104 317 FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN 396
|
410 420 430
....*....|....*....|....*....|...
gi 654965072 441 RVDHMPYGGVKKSGNGKEGPKYAIEEMTEERII 473
Cdd:cd07104 397 DEPHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
25-475 |
7.90e-156 |
|
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: 450.24 E-value: 7.90e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 25 MEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKnTFS---PYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESR 101
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP-AWAattPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 102 GEVERAATTLQISAEEAKRIHGEGVPvesaQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPA 181
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLP----SDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 182 EVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSAT 259
Cdd:cd07150 156 EETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGrhLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 260 VVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEE 339
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 340 WVKEAVEEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQF 419
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 654965072 420 AMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07150 396 AFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-475 |
3.65e-154 |
|
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: 445.84 E-value: 3.65e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKNT----FSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRG 102
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGawrkLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 103 EVERAATTLQISAEEAKRIHGEGVPVESAqgseNRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAE 182
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKG----DYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 183 VTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI--RSKAGLRKVSLELGNNSATV 260
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIarAAAENLAPVTLELGGKSPNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 261 VHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEW 340
Cdd:cd07114 237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 341 VKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLF 413
Cdd:cd07114 317 VARAREEGARVLTGGERpsgadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654965072 414 TNDLQFAMKAAREIEVGGLIVNDasaYRVDH--MPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07114 397 TRDLARAHRVARAIEAGTVWVNT---YRALSpsSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-475 |
9.02e-153 |
|
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: 442.86 E-value: 9.02e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEWE--TTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEI 88
Cdd:cd07088 1 YINGEFVpsSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKawERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 89 LATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESaqgsENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGP 168
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDR----PNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 169 AIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--L 246
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAenI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 247 RKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIG 326
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 327 PMIRLKEAERVEEWVKEAVEEGAKIELGGKRD----GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVN 402
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPegekGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 403 DSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDAS--AYRVDHmpyGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENfeAMQGFH---AGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
9-476 |
4.52e-150 |
|
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: 436.23 E-value: 4.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 9 QYGLYVNGEW-ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK---NTFSPYERYEVLMKAAELLLSRQEE 84
Cdd:cd07082 1 QFKYLINGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRgwwPTMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 85 FAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCH 164
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 165 KLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA 244
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 245 GLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTD 324
Cdd:cd07082 241 PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 325 IGPMIRLKEAERVEEWVKEAVEEGAKIELGGKRDGAFYL-PTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVND 403
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGNLIyPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654965072 404 SDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVLN 476
Cdd:cd07082 401 SNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
7-469 |
2.97e-144 |
|
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: 421.62 E-value: 2.97e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 7 VKQYGLYVNGEW--ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAELLLS 80
Cdd:cd07091 1 EQPTGLFINNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwwrKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 81 RQEEFAEILATEVGKSIRES-RGEVERAATTLQISAEEAKRIHGEGVPVesaqgSENRMAFTVKVPVGVVAAITPFNVPI 159
Cdd:cd07091 81 DRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPI-----DGNFLAYTRREPIGVCGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 160 NLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGEL 239
Cdd:cd07091 156 LMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 240 IR---SKAGLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVG 316
Cdd:cd07091 236 IMeaaAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 317 NPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDE 393
Cdd:cd07091 316 DPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERhgsKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654965072 394 IDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVdHMPYGGVKKSGNGKEGPKYAIEEMTE 469
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDA-AVPFGGFKQSGFGRELGEEGLEEYTQ 470
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-475 |
8.70e-144 |
|
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: 419.66 E-value: 8.70e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKNT--FSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESR-GE 103
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWsrMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRIHGEGVPVESaqgseNRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEV 183
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-----GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 184 TPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA--GLRKVSLELGNNSATVV 261
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAapNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWV 341
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 342 KEAVEEGAKIELGGKRD-------GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFT 414
Cdd:cd07093 316 ELARAEGATILTGGGRPelpdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654965072 415 NDLQFAMKAAREIEVGGLIVNDASAyRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVNCWLV-RDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-475 |
1.56e-143 |
|
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: 418.75 E-value: 1.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 25 MEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKNT---FSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESR 101
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRnnwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 102 GEVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPA 181
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 182 EVTPICALKLAELMEEAGLPKGRLQVLTGDgAEIGEWLLENQDVNMFTFTGSPRVGELIRSK--AGLRkVSLELGNNSAT 259
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWMLRSKlaPGTR-CALEHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 260 VVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEE 339
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 340 WVKEAVEEGAKIELGGKRDG-AFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQ 418
Cdd:cd07148 319 WVNEAVAAGARLLCGGKRLSdTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 654965072 419 FAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07148 399 VALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
13-465 |
2.67e-143 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 418.96 E-value: 2.67e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEWETTAEKMEVLNKY-TQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEIL 89
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAwrRTSPEARADILDKAGDELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 90 ATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPvesaQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPA 169
Cdd:cd07097 84 TREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLP----STRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 170 IAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLR-- 247
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARga 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 248 KVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGP 327
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 328 MIRLKEAERVEEWVKEAVEEGAKIELGGKR----DGAFYL-PTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVN 402
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERlkrpDEGYYLaPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654965072 403 DSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNG-KEGPKYAIE 465
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYGpREQGEAALE 463
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
4-476 |
3.85e-140 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 411.78 E-value: 3.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 4 LTQVKQYGLY-----VNGEWETT--AEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKA 74
Cdd:PLN02278 14 LVKLRNAGLLrtqglIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSwsKLTASERSKILRRW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 75 AELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAQGsenRMaFTVKVPVGVVAAITP 154
Cdd:PLN02278 94 YDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDR---RL-LVLKQPVGVVGAITP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 155 FNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSP 234
Cdd:PLN02278 170 WNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGST 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 235 RVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEK 312
Cdd:PLN02278 250 AVGKKLMAGAAatVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 313 LVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIA 389
Cdd:PLN02278 330 LVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRhslGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 390 QYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVND-----ASAyrvdhmPYGGVKKSGNGKEGPKYAI 464
Cdd:PLN02278 410 RFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEglistEVA------PFGGVKQSGLGREGSKYGI 483
|
490
....*....|..
gi 654965072 465 EEMTEERIIVLN 476
Cdd:PLN02278 484 DEYLEIKYVCLG 495
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-475 |
3.28e-139 |
|
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: 408.04 E-value: 3.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 12 LYVNGEWE--TTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKnTFS---PYERYEVLMKAAELLLSRQEEFA 86
Cdd:cd07138 1 FYIDGAWVapAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP-AWSatsVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 87 EILATEVGKSIRESRG-EVERAATTLQISAEEAKRIhgegvPVESAQGSenrmAFTVKVPVGVVAAITPFNVPINLVCHK 165
Cdd:cd07138 80 QAITLEMGAPITLARAaQVGLGIGHLRAAADALKDF-----EFEERRGN----SLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 166 LGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG 245
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 246 --LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQT 323
Cdd:cd07138 231 dtVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 324 DIGPMIRLKEAERVEEWVKEAVEEGAKIELGGK------RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEV 397
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgrpeglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654965072 398 ISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDAsayRVD-HMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGA---AFNpGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
13-476 |
3.12e-138 |
|
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: 406.35 E-value: 3.12e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEW--ETTAEKMEVLN-KYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAE 87
Cdd:cd07131 2 YIGGEWvdSASGETFDSRNpADLEEVVGTFPLSTASDVDAAVEAAREAFPEwrKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 88 ILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAqgseNRMAFTVKVPVGVVAAITPFNVPINLVCHKLG 167
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELP----NKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 168 PAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG-- 245
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCArp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 246 LRKVSLELGNNSATVVHKDADLEKA--ASLISqkSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQT 323
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLAleGALWS--AFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 324 DIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDE 396
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 397 VISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNG-KEGPKYAIEEMTEERIIVL 475
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
.
gi 654965072 476 N 476
Cdd:cd07131 476 D 476
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
34-475 |
2.72e-136 |
|
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: 400.56 E-value: 2.72e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 34 QPAAEISVATKDDVNKAVASAKEALKNTFSPY----ERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAAT 109
Cdd:cd07118 8 VVVARYAEGTVEDVDAAVAAARKAFDKGPWPRmsgaERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 110 TLQISAEEAKRIHGEGvpvESAQGsENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICAL 189
Cdd:cd07118 88 LWRYAASLARTLHGDS---YNNLG-DDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 190 KLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADL 267
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAArnLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 268 EKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEE 347
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 348 GAKIELGGKR----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKA 423
Cdd:cd07118 324 GATLLLGGERlasaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTV 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 424 AREIEVGGLIVN---DASAyrvdHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07118 404 ARRIRAGTVWVNtflDGSP----ELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-475 |
2.86e-136 |
|
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: 396.99 E-value: 2.86e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 52 ASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVE 129
Cdd:cd06534 1 AAARAAFKAwaALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 130 SAQGsenrMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLT 209
Cdd:cd06534 81 DPGG----EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 210 GDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCI 287
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAenLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 288 SVQRIYVHTNIYTAFVNKLKekteklvvgnpmdeqtdigpmirlkeaerveewvkeaveegakielggkrdgafylpTIL 367
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV---------------------------------------------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 368 TNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPY 447
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPF 339
|
410 420
....*....|....*....|....*...
gi 654965072 448 GGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
16-473 |
1.00e-135 |
|
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: 399.37 E-value: 1.00e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 16 GEWE--TTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILAT 91
Cdd:cd07151 1 GEWRdgTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEwaATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 92 EVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPvESAQGSENRMaftVKVPVGVVAAITPFNVPINLVCHKLGPAIA 171
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILP-SDVPGKENRV---YREPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 172 AGNSVVLKPAEVTPICA-LKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRK 248
Cdd:cd07151 157 LGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGrhLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 249 VSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPM 328
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 329 IRLKEAERVEEWVKEAVEEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGL 408
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 409 QAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERII 473
Cdd:cd07151 397 SGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-469 |
1.07e-132 |
|
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: 391.58 E-value: 1.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 23 EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIR 98
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvwsRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 99 ESR-GEVERAATTLQISAEEAKRIHGEGVPVEsaqgsENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVV 177
Cdd:cd07112 82 DALaVDVPSAANTFRWYAEAIDKVYGEVAPTG-----PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 178 LKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG---LRKVSLELG 254
Cdd:cd07112 157 LKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqsnLKRVWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 255 NNSATVVHKDA-DLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKE 333
Cdd:cd07112 237 GKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 334 AERVEEWVKEAVEEGAKIELGGKRD-----GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGL 408
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVltetgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654965072 409 QAGLFTNDLQFAMKAAREIEVGGLIVN-----DASayrvdhMPYGGVKKSGNGKEGPKYAIEEMTE 469
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNcfdegDIT------TPFGGFKQSGNGRDKSLHALDKYTE 456
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
37-471 |
8.37e-132 |
|
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: 388.58 E-value: 8.37e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 37 AEISVATKDDVNKAVASAKEALKNTF--SPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQIS 114
Cdd:cd07152 5 GEVGVADAADVDRAAARAAAAQRAWAatPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 115 AEEAKRIHGEGVPveSAQGsenRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICA-LKLAE 193
Cdd:cd07152 85 AGLPTQPQGEILP--SAPG---RLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 194 LMEEAGLPKGRLQVLTGdGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAA 271
Cdd:cd07152 160 LFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGrhLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 272 SLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKI 351
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 352 ELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGG 431
Cdd:cd07152 319 EAGGTYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGM 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 654965072 432 LIVNDASAYRVDHMPYGGVKKSGNGKE--GPKyAIEEMTEER 471
Cdd:cd07152 399 LHINDQTVNDEPHNPFGGMGASGNGSRfgGPA-NWEEFTQWQ 439
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-477 |
2.38e-131 |
|
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: 388.59 E-value: 2.38e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEWETTAEK--MEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK----NTFSPYERYEVLMKAAELLLSRQEEFA 86
Cdd:cd07119 1 YIDGEWVEAASGktRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsgewPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 87 EILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVesaqgSENRMAFTVKVPVGVVAAITPFNVPINLVCHKL 166
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV-----PPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 167 GPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI-RSKAG 245
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSImRAAAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 246 -LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTD 324
Cdd:cd07119 236 nVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 325 IGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEV 397
Cdd:cd07119 316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptgdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 398 ISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKEGPKYAIEEMTEERIIVLNL 477
Cdd:cd07119 396 IRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAE-APWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
27-469 |
3.42e-131 |
|
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: 387.49 E-value: 3.42e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIR-ESRGE 103
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEwaATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRIHGEGVPvesaqGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEV 183
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-----FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 184 TPICALKLAELMEEAgLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLR--KVSLELGNNSATVV 261
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRliPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDADLEKA-ASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEW 340
Cdd:cd07108 235 FPDADLDDAvDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 341 VKEAVEE-GAKIELGGK-------RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGL 412
Cdd:cd07108 315 IDLGLSTsGATVLRGGPlpgegplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 654965072 413 FTNDLQFAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKEgpkYAIEEMTE 469
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPG-QSYGGFKQSGLGRE---ASLEGMLE 447
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-475 |
5.15e-131 |
|
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: 387.32 E-value: 5.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 12 LYVNGEWET--TAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAELLLSRQEEF 85
Cdd:cd07139 1 LFIGGRWVApsGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpwpRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRESR-GEVERAATTLQISAEEAkrihgEGVPVESA-QGSENRMAFTVKVPVGVVAAITPFNVPINLVC 163
Cdd:cd07139 81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALA-----RDFPFEERrPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 164 HKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDgAEIGEWLLENQDVNMFTFTGSPRVGELIRSK 243
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 244 AG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDE 321
Cdd:cd07139 235 CGerLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 322 QTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDE 396
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpagldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 397 VISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNdasAYRVD-HMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN---GFRLDfGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
27-473 |
8.14e-130 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 383.42 E-value: 8.14e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEV 104
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGwsATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 105 ERAATTLQISAEEAkrihgegVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVT 184
Cdd:cd07106 81 GGAVAWLRYTASLD-------LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 185 PICALKLAELMEEAgLPKGRLQVLTGDGaEIGEWLLENQDVNMFTFTGSPRVGELI-RSKAG-LRKVSLELGNNSATVVH 262
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVmASAAKtLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 263 KDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVK 342
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 343 EAVEEGAKIELGGK---RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQF 419
Cdd:cd07106 312 DAKAKGAKVLAGGEpldGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 654965072 420 AMKAAREIEVGGLIVNDASAYRVdHMPYGGVKKSGNGKEGPKYAIEEMTEERII 473
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDP-DAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
27-477 |
2.67e-127 |
|
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: 377.55 E-value: 2.67e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRG-E 103
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAwsAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRIHGEGVPVESaqgseNRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEV 183
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRG-----PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 184 TPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGE-LIRSKAG-LRKVSLELGNNSATVV 261
Cdd:cd07115 156 TPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAGnLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWV 341
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 342 KEAVEEGAKIELGGKRDGA---FYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQ 418
Cdd:cd07115 316 DVGREEGARLLTGGKRPGArgfFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 654965072 419 FAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKEGPKYAIEEMTEERIIVLNL 477
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPG-SPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
47-466 |
2.80e-127 |
|
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: 376.42 E-value: 2.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 47 VNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEeakriHGE 124
Cdd:cd07100 1 IEAALDRAHAAFLAwrKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAE-----NAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 125 G----VPVESAQGSenrmAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGL 200
Cdd:cd07100 76 AfladEPIETDAGK----AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 201 PKGRLQVLTGDGAEIgEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKS 278
Cdd:cd07100 152 PEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGknLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 279 FNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR- 357
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 358 --DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN 435
Cdd:cd07100 311 dgPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430
....*....|....*....|....*....|.
gi 654965072 436 DASAYRVDhMPYGGVKKSGNGKEGPKYAIEE 466
Cdd:cd07100 391 GMVKSDPR-LPFGGVKRSGYGRELGRFGIRE 420
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-475 |
1.80e-126 |
|
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: 375.42 E-value: 1.80e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKNTF---SPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGE 103
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlrlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRIHGEGVPVEsaqgsENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEV 183
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLG-----PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 184 TPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVV 261
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAenVVPVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMdEQTDIGPMIRLKEAERVEEWV 341
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 342 KEAVEEGAKIELGGKR------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTN 415
Cdd:cd07109 315 ARARARGARIVAGGRIaegapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 416 DLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
27-469 |
7.34e-126 |
|
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: 373.95 E-value: 7.34e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEV 104
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKewSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 105 ERAATTLQISAEEAKRIHGEGVPVesaqgSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVT 184
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPL-----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 185 PICALKLAELMEEAGLPKGRLQVLTGDGaEIGEWLLENQDVNMFTFTGSPRVGELIRSKA--GLRKVSLELGNNSATVVH 262
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAakGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 263 KDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVK 342
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 343 EAVEEGAKIELGGKR-------DGAFYL-PTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFT 414
Cdd:cd07090 315 SAKQEGAKVLCGGERvvpedglENGFYVsPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 415 NDLQFAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKEGPKYAIEEMTE 469
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVE-VPFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
6-475 |
8.74e-125 |
|
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: 372.07 E-value: 8.74e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 6 QVKQYGLYVNGEW--ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKnTFSPY------ERYEVLMKAAEL 77
Cdd:cd07141 3 EIKYTKIFINNEWhdSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFK-LGSPWrtmdasERGRLLNKLADL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 78 LLSRQEEFAEILATEVGKSIRESR-GEVERAATTLQISAEEAKRIHGEGVPVESaqgseNRMAFTVKVPVGVVAAITPFN 156
Cdd:cd07141 82 IERDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDG-----DFFTYTRHEPVGVCGQIIPWN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 157 VPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRV 236
Cdd:cd07141 157 FPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 237 GELIRSKAG---LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKL 313
Cdd:cd07141 237 GKLIQQAAGksnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 314 VVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQ 390
Cdd:cd07141 317 VVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRhgdKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 391 YDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVdHMPYGGVKKSGNGKEGPKYAIEEMTEE 470
Cdd:cd07141 397 FKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSP-QAPFGGYKMSGNGRELGEYGLQEYTEV 475
|
....*
gi 654965072 471 RIIVL 475
Cdd:cd07141 476 KTVTI 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
27-475 |
1.28e-124 |
|
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: 370.81 E-value: 1.28e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKNT---FSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIR-ESRG 102
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdwsTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 103 EVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAE 182
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 183 VTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATV 260
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAatLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 261 VHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEW 340
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 341 VKEAVEEGAKIELGGKR-----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTN 415
Cdd:cd07089 321 IARGRDEGARLVTGGGRpagldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 416 DLQFAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPD-APFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-477 |
2.26e-124 |
|
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: 370.97 E-value: 2.26e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 11 GLYVNGEW--ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKNTFS---PYERYEVLMKAAELLLSRQEEF 85
Cdd:cd07144 9 GLFINNEFvkSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSkvtGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRE-SRGEVERAATTLQISAEEAKRIHGEGVPVESaqgseNRMAFTVKVPVGVVAAITPFNVPINLVCH 164
Cdd:cd07144 89 AAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSP-----NKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 165 KLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA 244
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 245 G--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKT-EKLVVGNPMDE 321
Cdd:cd07144 244 AqnLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 322 QTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKRD------GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEID 395
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKApeglgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 396 EVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVdHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV-GVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
..
gi 654965072 476 NL 477
Cdd:cd07144 483 NL 484
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
10-469 |
9.66e-123 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 366.90 E-value: 9.66e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 10 YGLYVNGEW--ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEF 85
Cdd:PRK13252 7 QSLYIDGAYveATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKiwAAMTAMERSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRESR-GEVERAATTLQISAEEAKRIHGEGVPVesaqgSENRMAFTVKVPVGVVAAITPFNVPINLVCH 164
Cdd:PRK13252 87 AALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPL-----RGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 165 KLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGaEIGEWLLENQDVNMFTFTGSPRVGELIRSKA 244
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 245 G--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQ 322
Cdd:PRK13252 241 AasLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 323 TDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEID 395
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERlteggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654965072 396 EVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKEGPKYAIEEMTE 469
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAE-MPVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
11-477 |
4.35e-122 |
|
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: 364.93 E-value: 4.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 11 GLYVNGEWETTAEK--MEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKNT----FSPYERYEVLMKAAELLLSRQEE 84
Cdd:cd07143 8 GLFINGEFVDSVHGgtVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDwglkVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 85 FAEILATEVGKSIRE-SRGEVERAATTLQISAEEAKRIHGEGVpvesaQGSENRMAFTVKVPVGVVAAITPFNVPINLVC 163
Cdd:cd07143 88 LASIEALDNGKTFGTaKRVDVQASADTFRYYGGWADKIHGQVI-----ETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 164 HKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI--- 240
Cdd:cd07143 163 WKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVmea 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 241 RSKAGLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMD 320
Cdd:cd07143 243 AAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 321 EQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEV 397
Cdd:cd07143 323 EDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRhgnEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 398 ISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAyrVDH-MPYGGVKKSGNGKEGPKYAIEEMTEERIIVLN 476
Cdd:cd07143 403 IKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNL--LHHqVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
.
gi 654965072 477 L 477
Cdd:cd07143 481 L 481
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
46-473 |
2.43e-119 |
|
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: 356.12 E-value: 2.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 46 DVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHG 123
Cdd:cd07105 1 DADQAVEAAAAAFPawSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 124 EGVPvesaQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKG 203
Cdd:cd07105 81 GSIP----SDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 204 RLQVLT---GDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKS 278
Cdd:cd07105 157 VLNVVThspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAkhLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 279 FNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNpmdeqTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR- 357
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAd 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 358 ---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIV 434
Cdd:cd07105 312 espSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 654965072 435 NDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERII 473
Cdd:cd07105 392 NGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-475 |
1.50e-118 |
|
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: 356.03 E-value: 1.50e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 7 VKQYGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAELLLS 80
Cdd:cd07142 1 VKHTKLFINGQFVDAAsgKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpwpRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 81 RQEEFAEILATEVGKSIRESR-GEVERAATTLQISAEEAKRIHGEGVPVESaqgseNRMAFTVKVPVGVVAAITPFNVPI 159
Cdd:cd07142 81 HADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADG-----PHHVYTLHEPIGVVGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 160 NLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGEL 239
Cdd:cd07142 156 LMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 240 I---RSKAGLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVG 316
Cdd:cd07142 236 ImqlAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 317 NPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDE 393
Cdd:cd07142 316 DPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRigsKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 394 IDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN-----DASAyrvdhmPYGGVKKSGNGKEGPKYAIEEMT 468
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvfDASI------PFGGYKMSGIGREKGIYALNNYL 469
|
....*..
gi 654965072 469 EERIIVL 475
Cdd:cd07142 470 QVKAVVM 476
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
13-458 |
7.94e-118 |
|
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: 354.18 E-value: 7.94e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEW-ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEIL 89
Cdd:cd07086 2 VIGGEWvGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEwrKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 90 ATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAqgseNRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPA 169
Cdd:cd07086 82 SLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERP----GHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 170 IAAGNSVVLKPAEVTPICALKLAELMEEA----GLPKGRLQVLTGdGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG 245
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 246 --LRKVSLELGNNSATVVHKDADLEKA--ASLISqkSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDE 321
Cdd:cd07086 237 rrFGRVLLELGGNNAIIVMDDADLDLAvrAVLFA--AVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 322 QTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDE 396
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidggePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654965072 397 VISKVNDSDYGLQAGLFTNDLQFAMKA--AREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKE 458
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRE 458
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
8-462 |
4.22e-117 |
|
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: 353.45 E-value: 4.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 8 KQYGLYVNGEWETTAEKMEVLNkytqqPA------AEISVATKDDVNKAVASAKEAL---KNTfSPYERYEVLMKAAELL 78
Cdd:cd07124 31 REYPLVIGGKEVRTEEKIESRN-----PAdpsevlGTVQKATKEEAEAAVQAARAAFptwRRT-PPEERARLLLRAAALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 79 LSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEgvPVESAQGSENRmafTVKVPVGVVAAITPFNVP 158
Cdd:cd07124 105 RRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNR---YVYRPLGVGAVISPWNFP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 159 INLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGE 238
Cdd:cd07124 180 LAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 239 LIRSKAG--------LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKT 310
Cdd:cd07124 260 RIYERAAkvqpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 311 EKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGaKIELGGKRD-----GAFYLPTILTNVNDEMKVCRQEVFGPV 385
Cdd:cd07124 340 KALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLelaaeGYFVQPTIFADVPPDHRLAQEEIFGPV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 386 VAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN-DASAYRVDHMPYGGVKKSG-NGKE-GPKY 462
Cdd:cd07124 419 LAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrKITGALVGRQPFGGFKMSGtGSKAgGPDY 498
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
9-468 |
4.68e-117 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 351.90 E-value: 4.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 9 QYGLYVNGEW-ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEF 85
Cdd:PRK13473 2 QTKLLINGELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPewSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRESRGEvERAATTLQIS--AEEAKRIHGegvpveSAQG--SENRMAFTVKVPVGVVAAITPFNVPINL 161
Cdd:PRK13473 82 ARLESLNCGKPLHLALND-EIPAIVDVFRffAGAARCLEG------KAAGeyLEGHTSMIRRDPVGVVASIAPWNYPLMM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 162 VCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIR 241
Cdd:PRK13473 155 AAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 242 SKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPM 319
Cdd:PRK13473 234 SAAAdsVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 320 DEQTDIGPMIRLKEAERVEEWVKEAVEEG-AKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEID 395
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEApdgKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654965072 396 EVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYrVDHMPYGGVKKSGNGKEGPKYAIEEMT 468
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFML-VSEMPHGGQKQSGYGKDMSLYGLEDYT 465
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
32-474 |
1.09e-115 |
|
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: 347.67 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 32 TQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAAT 109
Cdd:cd07099 5 TGEVLGEVPVTDPAEVAAAVARARAAQRawAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 110 TLQISAEEAKRIHGEGvPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICAL 189
Cdd:cd07099 85 AIDWAARNAPRVLAPR-KVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 190 KLAELMEEAGLPKGRLQVLTGDGaEIGEWLLENQdVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADL 267
Cdd:cd07099 164 LLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAG-VDKVAFTGSVATGRKVMAAAAerLIPVVLELGGKDPMIVLADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 268 EKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEE 347
Cdd:cd07099 242 ERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 348 GAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAA 424
Cdd:cd07099 322 GAKALTGGARsngGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 654965072 425 REIEVGGLIVNDASA-YRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIV 474
Cdd:cd07099 402 RRLEAGAVSINDVLLtAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
10-477 |
8.29e-115 |
|
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: 346.36 E-value: 8.29e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 10 YGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEF 85
Cdd:cd07117 1 YGLFINGEWVKGSsgETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTwrKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRESRG-EVERAATTLQ-----ISAEEAkrihgegvpvESAQGSENRMAFTVKVPVGVVAAITPFNVPI 159
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRyfagvIRAEEG----------SANMIDEDTLSIVLREPIGVVGQIIPWNFPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 160 NLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGEL 239
Cdd:cd07117 151 LMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 240 IRSKAGLRKV--SLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGN 317
Cdd:cd07117 230 VAIAAAKKLIpaTLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 318 PMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQ 390
Cdd:cd07117 310 PLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltengldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 391 YDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNdasAYRV--DHMPYGGVKKSGNGKEGPKYAIEEMT 468
Cdd:cd07117 390 FKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN---TYNQipAGAPFGGYKKSGIGRETHKSMLDAYT 466
|
....*....
gi 654965072 469 EERIIVLNL 477
Cdd:cd07117 467 QMKNIYIDL 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
10-477 |
1.75e-114 |
|
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: 345.48 E-value: 1.75e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 10 YGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEF 85
Cdd:cd07559 1 YDNFINGEWVAPSkgEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTwgKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRESRG-EVERAATTLQ-----ISAEEAkrihgegvpvESAQGSENRMAFTVKVPVGVVAAITPFNVPI 159
Cdd:cd07559 81 AVAETLDNGKPIRETLAaDIPLAIDHFRyfagvIRAQEG----------SLSEIDEDTLSYHFHEPLGVVGQIIPWNFPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 160 NLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGEL 239
Cdd:cd07559 151 LMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 240 IRSKAG--LRKVSLELGNNSATVVHKDA-----DLEKAAsLISQKSFN-NAGQVCISVQRIYVHTNIYTAFVNKLKEKTE 311
Cdd:cd07559 230 IMQYAAenLIPVTLELGGKSPNIFFDDAmdaddDFDDKA-EEGQLGFAfNQGEVCTCPSRALVQESIYDEFIERAVERFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 312 KLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGP 384
Cdd:cd07559 309 AIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERltlggldKGYFYEPTLIKGGNNDMRIFQEEIFGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 385 VVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVdHMPYGGVKKSGNGKEGPKYAI 464
Cdd:cd07559 389 VLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPA-HAPFGGYKKSGIGRETHKMML 467
|
490
....*....|...
gi 654965072 465 EEMTEERIIVLNL 477
Cdd:cd07559 468 DHYQQTKNILVSY 480
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
27-468 |
4.12e-114 |
|
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: 343.54 E-value: 4.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESR-GE 103
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSwrRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRIHGegvpveSAQGS--ENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPA 181
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEG------PAAGEylPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 182 EVTPICALKLAELMEEaGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA--GLRKVSLELGNNSAT 259
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAadTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 260 VVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEE 339
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 340 WVKEAvEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTND 416
Cdd:cd07092 314 FVERA-PAHARVLTGGRRaegPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 654965072 417 LQFAMKAAREIEVGGLIVNDASAYrVDHMPYGGVKKSGNGKEGPKYAIEEMT 468
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPL-AAEMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
26-474 |
3.59e-112 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 341.09 E-value: 3.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 26 EVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGE 103
Cdd:PRK09407 35 EVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAwaATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 VERAATTLQISAEEAKRI-----HGEGVPVESaQGSENRmaftvkVPVGVVAAITPFNVPINL-VCHKLgPAIAAGNSVV 177
Cdd:PRK09407 115 VLDVALTARYYARRAPKLlaprrRAGALPVLT-KTTELR------QPKGVVGVISPWNYPLTLaVSDAI-PALLAGNAVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 178 LKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTftGSPRVGELIRSKAGLRKV--SLELGN 255
Cdd:PRK09407 187 LKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNADYLMFT--GSTATGRVLAEQAGRRLIgfSLELGG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 256 NSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAE 335
Cdd:PRK09407 265 KNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 336 RVEEWVKEAVEEGAKIELGGKR--D-G-AFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAG 411
Cdd:PRK09407 345 TVSAHVDDAVAKGATVLAGGKArpDlGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNAS 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654965072 412 LFTNDLQFAMKAAREIEVGGLIVND--ASAYRVDHMPYGGVKKSG----NGKEGpkyaIEEMTEERIIV 474
Cdd:PRK09407 425 VWTGDTARGRAIAARIRAGTVNVNEgyAAAWGSVDAPMGGMKDSGlgrrHGAEG----LLKYTESQTIA 489
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
12-477 |
1.12e-111 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 338.79 E-value: 1.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 12 LYVNGEWETTAE--KMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAELLLSRQEEF 85
Cdd:PRK09847 22 LFINGEYTAAAEneTFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdwsLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRES-RGEVERAATTLQISAEEAKRIHGEGVPVESAQgsenrMAFTVKVPVGVVAAITPFNVPINLVCH 164
Cdd:PRK09847 102 ALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHE-----LAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 165 KLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA 244
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 245 G---LRKVSLELGNNSATVVHKDA-DLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMD 320
Cdd:PRK09847 257 GdsnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 321 EQTDIGPMIRLKEAERVEEWVKEAVEEGaKIELGGKRDG--AFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVI 398
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGlaAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 399 SKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDasaYRVDHM--PYGGVKKSGNGKEGPKYAIEEMTEERIIVLN 476
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN---YNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
|
.
gi 654965072 477 L 477
Cdd:PRK09847 493 L 493
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
31-459 |
9.15e-111 |
|
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: 335.05 E-value: 9.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 31 YTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAA 108
Cdd:cd07101 4 FTGEPLGELPQSTPADVEAAFARARAAQRAwaARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 109 TTLQISAEEAKRI-----HGEGVPVESaQGSENRmaftvkVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEV 183
Cdd:cd07101 84 IVARYYARRAERLlkprrRRGAIPVLT-RTTVNR------RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 184 TPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTftGSPRVGELIRSKAGLRKV--SLELGNNSATVV 261
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADYVMFT--GSTATGRVVAERAGRRLIgcSLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWV 341
Cdd:cd07101 235 LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 342 KEAVEEGAKIELGGKR----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDL 417
Cdd:cd07101 315 DDAVAKGATVLAGGRArpdlGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 654965072 418 QFAMKAAREIEVGGLIVND--ASAYRVDHMPYGGVKKSG----NGKEG 459
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNEgyAAAWASIDAPMGGMKDSGlgrrHGAEG 442
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-477 |
1.42e-110 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 335.72 E-value: 1.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEW--ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEI 88
Cdd:PRK11241 14 LINGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPawRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 89 LATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAqgseNRMAFTVKVPVGVVAAITPFNVPINLVCHKLGP 168
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQA----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 169 AIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--L 246
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAkdI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 247 RKVSLELGNNSATVVHKDADLEKA--ASLISQksFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTD 324
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDADLDKAveGALASK--FRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 325 IGPMIRLKEAERVEEWVKEAVEEGAKIELGGK---RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKV 401
Cdd:PRK11241 328 IGPLIDEKAVAKVEEHIADALEKGARVVCGGKaheLGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 402 NDSDYGLQAGLFTNDLQFAMKAAREIEVG------GLIVNDASayrvdhmPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGivgintGIISNEVA-------PFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
..
gi 654965072 476 NL 477
Cdd:PRK11241 481 GL 482
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
11-469 |
5.60e-110 |
|
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: 334.02 E-value: 5.60e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 11 GLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKNTF---SPYERYEVLMKAAELLLSRQEEF 85
Cdd:cd07113 1 GHFIDGRPVAGQseKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWaktTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRESRG-EVERAATTLQISAEEAKRIHGE--GVPVESAQGsENRMAFTVKVPVGVVAAITPFNVPINLV 162
Cdd:cd07113 81 AQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGEtlAPSIPSMQG-ERYTAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 163 CHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGaEIGEWLLENQDVNMFTFTGSPRVGELIRS 242
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 243 KA--GLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMD 320
Cdd:cd07113 239 QAasDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 321 EQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGK---RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEV 397
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEalaGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654965072 398 ISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN-----DASayrvdhMPYGGVKKSGNGKE-GPKYaIEEMTE 469
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtflDPA------VPFGGMKQSGIGREfGSAF-IDDYTE 469
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
27-477 |
1.06e-109 |
|
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: 332.42 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEV 104
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEwrATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 105 ERAATTLQISAEEAKRIHGEGVPVesaqgSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVT 184
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPV-----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 185 PICALKLAELMEEAgLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI-RSKA-GLRKVSLELGNNSATVVH 262
Cdd:cd07107 156 PLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAImRAAAeGIKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 263 KDADLEKAA-SLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWV 341
Cdd:cd07107 235 PDADPEAAAdAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 342 KEAVEEGAKIELGGKR------DGAFYL-PTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFT 414
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpalEGGFYVePTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654965072 415 NDLQFAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKEgpkYAIEEM---TEERIIVLNL 477
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLG-APFGGVKNSGIGRE---ECLEELlsyTQEKNVNVRL 456
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
27-460 |
4.01e-109 |
|
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: 330.85 E-value: 4.01e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 27 VLNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEV 104
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPrwKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 105 ERAATTLQISAEEAKRIHgEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVT 184
Cdd:cd07110 81 DDVAGCFEYYADLAEQLD-AKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 185 PICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA--GLRKVSLELGNNSATVVH 262
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAaqDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 263 KDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVK 342
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 343 EAVEEGAKIELGGKR-----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDL 417
Cdd:cd07110 320 RGKEEGARLLCGGRRpahleKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 654965072 418 QFAMKAAREIEVGGLIVNdASAYRVDHMPYGGVKKSGNGKE-GP 460
Cdd:cd07110 400 ERCDRVAEALEAGIVWIN-CSQPCFPQAPWGGYKRSGIGRElGE 442
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-456 |
4.16e-109 |
|
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: 330.75 E-value: 4.16e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 28 LNKYTQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEV- 104
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKgwRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 105 ---ERAATTLQISAEEAKRIhgegvPVESAQGSENRMaftVKVPVGVVAAITPFNVP----INLVChklgPAIAAGNSVV 177
Cdd:cd07102 81 gmlERARYMISIAEEALADI-----RVPEKDGFERYI---RREPLGVVLIIAPWNYPyltaVNAVI----PALLAGNAVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 178 LKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGaEIGEWLLENQDVNMFTFTGSPRVGELI-RSKAG-LRKVSLELGN 255
Cdd:cd07102 149 LKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAIqRAAAGrFIKVGLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 256 NSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAE 335
Cdd:cd07102 228 KDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 336 RVEEWVKEAVEEGAKIELGGKR------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQ 409
Cdd:cd07102 308 FVRAQIADAIAKGARALIDGALfpedkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLT 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 654965072 410 AGLFTNDLQFAMKAAREIEVGGLIVNdasayRVDH----MPYGGVKKSGNG 456
Cdd:cd07102 388 ASVWTKDIARAEALGEQLETGTVFMN-----RCDYldpaLAWTGVKDSGRG 433
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
10-466 |
1.58e-108 |
|
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: 330.61 E-value: 1.58e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 10 YGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAELLLSRQE 83
Cdd:cd07140 6 HQLFINGEFVDAEggKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgewgKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 84 EFAEI------------LATEVGKSIResrgeveraatTLQISAEEAKRIHGEGVPVESAQGSENrMAFTVKVPVGVVAA 151
Cdd:cd07140 86 ELATIesldsgavytlaLKTHVGMSIQ-----------TFRYFAGWCDKIQGKTIPINQARPNRN-LTLTKREPIGVCGI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 152 ITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFT 231
Cdd:cd07140 154 VIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 232 GSPRVGELIR---SKAGLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKE 308
Cdd:cd07140 234 GSTPIGKHIMkscAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 309 KTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGK---RDGAFYLPTILTNVNDEMKVCRQEVFGPV 385
Cdd:cd07140 314 EVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKqvdRPGFFFEPTVFTDVEDHMFIAKEESFGPI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 386 VAIAQYD--EIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVdHMPYGGVKKSGNGKEGPKYA 463
Cdd:cd07140 394 MIISKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEEA 472
|
...
gi 654965072 464 IEE 466
Cdd:cd07140 473 LNE 475
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
10-477 |
1.33e-107 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 328.25 E-value: 1.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 10 YGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN-TFSP-YERYEVLMKAAELLLSRQEEF 85
Cdd:PLN00412 16 YKYYADGEWRTSSsgKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAwAKTPlWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEG--VPVESAQGSE-NRMAFTVKVPVGVVAAITPFNVPINLV 162
Cdd:PLN00412 96 AECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGkfLVSDSFPGNErNKYCLTSKIPLGVVLAIPPFNYPVNLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 163 CHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSpRVGELIRS 242
Cdd:PLN00412 176 VSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 243 KAGLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEq 322
Cdd:PLN00412 255 KAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 323 TDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVN 402
Cdd:PLN00412 334 CDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 403 DSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVLNL 477
Cdd:PLN00412 414 ASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINL 488
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
8-462 |
3.82e-106 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 325.35 E-value: 3.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 8 KQYGLYVNGEWETTAEKMEVLN-KYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEE 84
Cdd:PRK03137 35 QDYPLIIGGERITTEDKIVSINpANKSEVVGRVSKATKELAEKAMQAALEAFETwkKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 85 FAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIhGEGVPVESAQGSENRMAFTvkvPVGVVAAITPFNVPINLVCH 164
Cdd:PRK03137 115 FSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKL-ADGKPVESRPGEHNRYFYI---PLGVGVVISPWNFPFAIMAG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 165 KLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKA 244
Cdd:PRK03137 191 MTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 245 G--------LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVG 316
Cdd:PRK03137 271 AkvqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 317 NPmDEQTDIGPMIRLKEAERVEEWVKEAVEEGaKIELGGKRD---GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDE 393
Cdd:PRK03137 351 NP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDdskGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654965072 394 IDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN-DASAYRVDHMPYGGVKKSG-NGKEG-PKY 462
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrGCTGAIVGYHPFGGFNMSGtDSKAGgPDY 500
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
12-456 |
1.30e-105 |
|
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: 322.54 E-value: 1.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 12 LYVNGEW--ETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK---NTfSPYERYEVLMKAAELLLSRQEEFA 86
Cdd:cd07085 3 LFINGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPawsAT-PVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 87 EILATEVGKSIRESRGEVERAattlqISAEEakriHGEGVPV----ESAQGSENRM-AFTVKVPVGVVAAITPFNVPINL 161
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRG-----LEVVE----FACSIPHllkgEYLENVARGIdTYSYRQPLGVVAGITPFNFPAMI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 162 VCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGaEIGEWLLENQDVNMFTFTGSPRVGELIR 241
Cdd:cd07085 153 PLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK-EAVNALLDHPDIKAVSFVGSTPVGEYIY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 242 SKA---GLRKVSLELGNNSAtVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNP 318
Cdd:cd07085 232 ERAaanGKRVQALGGAKNHA-VVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 319 MDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQY 391
Cdd:cd07085 311 DDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGvkvpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 392 DEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDHMPYGGVKKSGNG 456
Cdd:cd07085 391 DTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFG 455
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
6-477 |
1.27e-103 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 319.45 E-value: 1.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 6 QVKQYGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAELLL 79
Cdd:PLN02466 54 QVSYTQLLINGQFVDAAsgKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpwpKMTAYERSRILLRFADLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 80 SRQEEFAEILATEVGKSIRESRG-EVERAATTLQISAEEAKRIHGEGVPVESaqgseNRMAFTVKVPVGVVAAITPFNVP 158
Cdd:PLN02466 134 KHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADG-----PHHVQTLHEPIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 159 INLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGE 238
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 239 LI---RSKAGLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVV 315
Cdd:PLN02466 289 IVlelAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 316 GNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYD 392
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRfgsKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 393 EIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN-----DASayrvdhMPYGGVKKSGNGKEGPKYAIEEM 467
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfDAA------IPFGGYKMSGIGREKGIYSLNNY 522
|
490
....*....|
gi 654965072 468 TEERIIVLNL 477
Cdd:PLN02466 523 LQVKAVVTPL 532
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
4-458 |
1.79e-103 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 317.92 E-value: 1.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 4 LTQVKQYGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN----TFSPYERYEVLMKAAEL 77
Cdd:PLN02766 15 VPEIKFTKLFINGEFVDAAsgKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpwpRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 78 LLSRQEEFAEILATEVGKSIRESRG-EVERAATTLQISAEEAKRIHGEGVPVESA-QGsenrmaFTVKVPVGVVAAITPF 155
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQlQG------YTLKEPIGVVGHIIPW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 156 NVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPR 235
Cdd:PLN02766 169 NFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 236 VGELIRSKAG---LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEK 312
Cdd:PLN02766 249 VGRKIMQAAAtsnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 313 LVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGK---RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIA 389
Cdd:PLN02766 329 WVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKpcgDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLM 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654965072 390 QYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDhMPYGGVKKSGNGKE 458
Cdd:PLN02766 409 KFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPD-CPFGGYKMSGFGRD 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
71-475 |
4.28e-102 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 311.29 E-value: 4.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 71 LMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPveSAQGSENRMAFtvKVPVGVVA 150
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQ--SDRPGENILLF--KRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 151 AITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTF 230
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 231 TGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKE 308
Cdd:PRK10090 157 TGSVSAGEKIMAAAAknITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 309 KTEKLVVGNPMDEQT-DIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGP 384
Cdd:PRK10090 237 AMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAvegKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 385 VVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDAS--AYRVDHmpyGGVKKSGNGKEGPKY 462
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENfeAMQGFH---AGWRKSGIGGADGKH 393
|
410
....*....|...
gi 654965072 463 AIEEMTEERIIVL 475
Cdd:PRK10090 394 GLHEYLQTQVVYL 406
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
43-475 |
2.15e-101 |
|
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: 311.20 E-value: 2.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 43 TKDDVNKAVASAKEALKNT---FSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAK 119
Cdd:cd07120 17 GVAEAEAAIAAARRAFDETdwaHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 120 RIHGEgvpveSAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEA- 198
Cdd:cd07120 97 TEAGR-----MIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 199 GLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQ 276
Cdd:cd07120 172 SLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAptLKRLGLELGGKTPCIVFDDADLDAALPKLER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 277 KSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIEL-GG 355
Cdd:cd07120 252 ALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLrGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 356 KRD-----GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVG 430
Cdd:cd07120 332 PVTeglakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAG 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 654965072 431 GLIVNDASAYRvDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIVL 475
Cdd:cd07120 412 TVWINDWNKLF-AEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-466 |
1.34e-98 |
|
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: 304.70 E-value: 1.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 5 TQVKQYGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLS 80
Cdd:cd07111 17 AHDRSFGHFINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESwsALPGHVRARHLYRIARHIQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 81 RQEEFAEILATEVGKSIRESR-GEVERAATTLQISAEEAKRIHGEGvpvesaQGSEnrmaftvkvPVGVVAAITPFNVPI 159
Cdd:cd07111 97 HQRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLDTEL------AGWK---------PVGVVGQIVPWNFPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 160 NLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAeIGEWLLENQDVNMFTFTGSPRVGEL 239
Cdd:cd07111 162 LMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 240 IR-SKAGL-RKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGN 317
Cdd:cd07111 241 LRrATAGTgKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 318 PMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKI---ELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEI 394
Cdd:cd07111 321 PLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVfqpGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654965072 395 DEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN-----DASAyrvdhmPYGGVKKSGNGKEGPKYAIEE 466
Cdd:cd07111 401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlfDAAA------GFGGYRESGFGREGGKEGLYE 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
11-458 |
4.94e-96 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 298.95 E-value: 4.94e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 11 GLYVNGEWETTAEK--MEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKNTFSPY-------ERYEVLMKAAELLLSR 81
Cdd:PLN02467 9 QLFIGGEWREPVLGkrIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKGKDwarttgaVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 82 QEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHG-EGVPVEsaQGSENRMAFTVKVPVGVVAAITPFNVPIN 160
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkQKAPVS--LPMETFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 161 LVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI 240
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 241 RSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNP 318
Cdd:PLN02467 247 MTAAAqmVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 319 MDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-----DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDE 393
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpehlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFST 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 394 IDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNdASAYRVDHMPYGGVKKSGNGKE 458
Cdd:PLN02467 407 EDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN-CSQPCFCQAPWGGIKRSGFGRE 470
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
42-466 |
1.20e-88 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 278.16 E-value: 1.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 42 ATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAK 119
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDyrTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 120 RIHGEgVPVESAQGSENRmAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAG 199
Cdd:PRK09406 100 ALLAD-EPADAAAVGASR-AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 200 LPKGRLQ-VLTGDGAEigEWLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQ 276
Cdd:PRK09406 178 FPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGdeIKKTVLELGGSDPFIVMPSADLDRAAETAVT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 277 KSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGK 356
Cdd:PRK09406 256 ARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 357 R---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLI 433
Cdd:PRK09406 336 RpdgPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVF 415
|
410 420 430
....*....|....*....|....*....|...
gi 654965072 434 VNDASAyRVDHMPYGGVKKSGNGKEGPKYAIEE 466
Cdd:PRK09406 416 INGMTV-SYPELPFGGVKRSGYGRELSAHGIRE 447
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
29-459 |
1.00e-87 |
|
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: 276.10 E-value: 1.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 29 NKYTQQPAAEISVATKDDVNKAVASAKEAL----KNTFSpyERYEVLMKAAELLLSRQEEFAEILATEVGKSIRE-SRGE 103
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQrewaKTSFA--ERRKVLRSLLKYILENQEEICRVACRDTGKTMVDaSLGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 104 V----ERAATTLQisaeeakriHGEGV--PvESAQGSENRMAFTVKV---PVGVVAAITPFNVPI-NLvchkLGPAIAA- 172
Cdd:cd07098 80 IlvtcEKIRWTLK---------HGEKAlrP-ESRPGGLLMFYKRARVeyePLGVVGAIVSWNYPFhNL----LGPIIAAl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 173 --GNSVVLKPAEVT-----PICALkLAELMEEAGLPKGRLQVLTGDGaEIGEWLLENQDVNMFTFTGSPRVGELIRSKAG 245
Cdd:cd07098 146 faGNAIVVKVSEQVawssgFFLSI-IRECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 246 --LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQT 323
Cdd:cd07098 224 esLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 324 DIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDE 396
Cdd:cd07098 304 DVGAMISPARFDRLEELVADAVEKGARLLAGGKRyphpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654965072 397 VISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVND-ASAYRVDHMPYGGVKKSG----NGKEG 459
Cdd:cd07098 384 AVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDfGVNYYVQQLPFGGVKGSGfgrfAGEEG 451
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-464 |
1.93e-83 |
|
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: 264.13 E-value: 1.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 46 DVNKAVASAKEAlkntFSPY------ERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAK 119
Cdd:cd07095 1 QVDAAVAAARAA----FPGWaalsleERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 120 RIHGEGVpVESAQGSenrmAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAG 199
Cdd:cd07095 77 ERTGERA-TPMAQGR----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 200 LPKGRLQVLTGdGAEIGEWLLENQDVNMFTFTGSPRVGELIRSK-AGLRKVS--LELGNNSATVVHKDADLEKAASLISQ 276
Cdd:cd07095 152 LPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKIlaLEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 277 KSFNNAGQVCISVQRIYVHTNIYT-AFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGG 355
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 356 KR---DGAFYLPTILtNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGgl 432
Cdd:cd07095 311 ERlvaGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG-- 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 654965072 433 IVN-------DASAyrvdhMPYGGVKKSGNGKEGPKYAI 464
Cdd:cd07095 388 IVNwnrpttgASST-----APFGGVGLSGNHRPSAYYAA 421
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
14-474 |
6.20e-82 |
|
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: 262.52 E-value: 6.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 14 VNGEWETTAEKMEVLN-KYTQQPAAEISVATKDDVNKAVASAKEAL---KNTfSPYERYEVLMKAAELLLSRQEEFAEIL 89
Cdd:cd07125 37 INGEETETGEGAPVIDpADHERTIGEVSLADAEDVDAALAIAAAAFagwSAT-PVEERAEILEKAADLLEANRGELIALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 90 ATEVGKSIRESRGEVERAATTLQISAEEAKRiHGEGVPVESAQGSENRMAFTvkvPVGVVAAITPFNVPINLVCHKLGPA 169
Cdd:cd07125 116 AAEAGKTLADADAEVREAIDFCRYYAAQARE-LFSDPELPGPTGELNGLELH---GRGVFVCISPWNFPLAIFTGQIAAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 170 IAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLRKV 249
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 250 SL-----ELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTD 324
Cdd:cd07125 272 PIlpliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 325 IGPMIR---------LKEAERVEEWV--KEAVEEGakielggkrDGAFYLPTILTNVNDEmkVCRQEVFGPVVAIAQYD- 392
Cdd:cd07125 352 VGPLIDkpagkllraHTELMRGEAWLiaPAPLDDG---------NGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKa 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 393 -EIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNdasayR------VDHMPYGGVKKSGNGKE--GPKYA 463
Cdd:cd07125 421 eDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-----RnitgaiVGRQPFGGWGLSGTGPKagGPNYL 495
|
490
....*....|.
gi 654965072 464 IEEMTEERIIV 474
Cdd:cd07125 496 LRFGNEKTVSL 506
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
5-473 |
1.88e-81 |
|
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: 260.97 E-value: 1.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 5 TQVKQYGLYVNGEWETTAEKMEVLNKY-TQQPAAEISVATKDDVNKAVASAKEALKN-TFSPYE-RYEVLMKAAELLLSR 81
Cdd:cd07083 14 EFGRAYPLVIGGEWVDTKERMVSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTwKDWPQEdRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 82 QEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAQGSENRmafTVKVPVGVVAAITPFNVPINL 161
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNE---SFYVGLGAGVVISPWNFPVAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 162 VCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIR 241
Cdd:cd07083 171 FTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 242 SKAGLR--------KVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKL 313
Cdd:cd07083 251 EAAARLapgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 314 VVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGaKIELGGKRD---GAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQ 390
Cdd:cd07083 331 SVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLegeGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 391 Y--DEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDAS-AYRVDHMPYGGVKKSG-NGKEGPKYAIEE 466
Cdd:cd07083 410 YkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKItGALVGVQPFGGFKLSGtNAKTGGPHYLRR 489
|
....*..
gi 654965072 467 MTEERII 473
Cdd:cd07083 490 FLEMKAV 496
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
28-466 |
8.39e-81 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 258.25 E-value: 8.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 28 LNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVE 105
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDwrETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 106 RAATTLQISAEeakriHGEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTP 185
Cdd:PRK13968 92 KSANLCDWYAE-----HGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 186 ICALKLAELMEEAGLPKGRLQVLTGDGAEIGEwLLENQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHK 263
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 264 DADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKE 343
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 344 AVEEGAKIELGGKR---DGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFA 420
Cdd:PRK13968 326 TLAEGARLLLGGEKiagAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 654965072 421 MKAAREIEVGGLIVN--DASAYRVdhmPYGGVKKSGNGKEGPKYAIEE 466
Cdd:PRK13968 406 RQMAARLECGGVFINgyCASDARV---AFGGVKKSGFGRELSHFGLHE 450
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-461 |
1.54e-77 |
|
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: 250.06 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 10 YGLYVNGEWETTA--EKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAElllsRQEEF 85
Cdd:cd07116 1 YDNFIGGEWVAPVkgEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAwgKTSVAERANILNKIAD----RMEAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 86 AEILAT----EVGKSIRESRG-EVERAATTLQ-----ISAEEAKrihgegvpveSAQGSENRMAFTVKVPVGVVAAITPF 155
Cdd:cd07116 77 LEMLAVaetwDNGKPVRETLAaDIPLAIDHFRyfagcIRAQEGS----------ISEIDENTVAYHFHEPLGVVGQIIPW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 156 NVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPR 235
Cdd:cd07116 147 NFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 236 VGELIRSKA--GLRKVSLELGNNSATVV------HKDADLEKAASLISQKSFNNaGQVCISVQRIYVHTNIYTAFVNKLK 307
Cdd:cd07116 226 TGRLIMQYAseNIIPVTLELGGKSPNIFfadvmdADDAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 308 EKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR-------DGAFYLPTILTNVNDeMKVCRQE 380
Cdd:cd07116 305 ERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelggllGGGYYVPTTFKGGNK-MRIFQEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 381 VFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVdHMPYGGVKKSGNGKEGP 460
Cdd:cd07116 384 IFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPA-HAAFGGYKQSGIGRENH 462
|
.
gi 654965072 461 K 461
Cdd:cd07116 463 K 463
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
61-471 |
3.39e-73 |
|
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: 237.51 E-value: 3.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 61 TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSiresrgEVERAATTLQISAEEA----KRIHG--EGVPVESAQGS 134
Cdd:cd07134 16 ASTAAERIAKLKRLKKAILARREEIIAALAADFRKP------AAEVDLTEILPVLSEInhaiKHLKKwmKPKRVRTPLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 135 ENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGDgAE 214
Cdd:cd07134 90 FGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGD-AE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 215 IGEWLLEnQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRI 292
Cdd:cd07134 168 VAQALLE-LPFDHIFFTGSPAVGKIVMAAAAkhLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 293 YVHTNIYTAFVNKLKEKTEKLVVGNPMDEQT-DIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKRDGA--FYLPTILTN 369
Cdd:cd07134 247 FVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAqrYIAPTVLTN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 370 VNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVD-HMPYG 448
Cdd:cd07134 327 VTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNpNLPFG 406
|
410 420
....*....|....*....|...
gi 654965072 449 GVKKSGNGKEGPKYAIEEMTEER 471
Cdd:cd07134 407 GVNNSGIGSYHGVYGFKAFSHER 429
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
13-418 |
1.82e-71 |
|
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: 234.02 E-value: 1.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEWETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALK---NTFSPyERYEVLMKAAELLLSRQEEFAEIL 89
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKewrDVPAP-KRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 90 ATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAqgseNRMAFTVKVPVGVVAAITPFNVP---------IN 160
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERP----GHRMMEQWNPLGVVGVITAFNFPvavwgwnaaIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 161 LVChklgpaiaaGNSVVLKPAEVTPICALK----LAELMEEAGLPKGRLQVLTGdGAEIGEWLLENQDVNMFTFTGSPRV 236
Cdd:cd07130 157 LVC---------GNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 237 GELIRSKAGLR--KVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLV 314
Cdd:cd07130 227 GRQVGQAVAARfgRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 315 VGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTILTNVNDeMKVCRQEVFGPVVAIAQY 391
Cdd:cd07130 307 IGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVidgPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKF 385
|
410 420
....*....|....*....|....*..
gi 654965072 392 DEIDEVISKVNDSDYGLQAGLFTNDLQ 418
Cdd:cd07130 386 DTLEEAIAWNNEVPQGLSSSIFTTDLR 412
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
56-474 |
2.39e-70 |
|
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: 229.72 E-value: 2.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 56 EALKNTFS-----PYE-RYEVLMKAAELLLSRQEEFAEILATEVGKSIRES--------RGEVEraaTTLQISAEEAKRI 121
Cdd:cd07087 5 ARLRETFLtgktrSLEwRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEID---HALKHLKKWMKPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 122 HGEgVPVESAQGSenrmAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLP 201
Cdd:cd07087 82 RVS-VPLLLQPAK----AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 202 KGRLQVLTGDGAEIGEWLLENQDVnMFtFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSF 279
Cdd:cd07087 156 PEAVAVVEGGVEVATALLAEPFDH-IF-FTGSPAVGKIVMEAAAkhLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 280 NNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLvVGNPMDEQTDIGPMIRLKEAERVEEWVkeaveEGAKIELGGKRDG 359
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQVDK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 360 A--FYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDA 437
Cdd:cd07087 308 EerYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDV 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 654965072 438 SA-YRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIV 474
Cdd:cd07087 388 LLhAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
11-463 |
7.04e-70 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 230.23 E-value: 7.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 11 GLYVNGEWET-TAEKMEVLNKYTQQPAAEISVATKDDVNKAVASAKEALKNTFS-PYE-RYEVLMKAAELLLSRQEEFAE 87
Cdd:PRK09457 2 TLWINGDWIAgQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARlSFEeRQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 88 ILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEgvpvesaqgSENRMAFTVKV----PVGVVAAITPFNVPINLVC 163
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAISIQAYHERTGE---------KRSEMADGAAVlrhrPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 164 HKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGdGAEIGEWLLENQDVNMFTFTGSPRVGELI-RS 242
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 243 KAGL--RKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYT-AFVNKLKEKTEKLVVGNPM 319
Cdd:PRK09457 232 FAGQpeKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGRWD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 320 DE-QTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGKR---DGAFYLPTIL--TNVN---DEmkvcrqEVFGPVVAIAQ 390
Cdd:PRK09457 312 AEpQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQlqaGTGLLTPGIIdvTGVAelpDE------EYFGPLLQVVR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 391 YDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGglIVN-------DASAyrvdhMPYGGVKKSGNGKEGPKYA 463
Cdd:PRK09457 386 YDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAG--IVNwnkpltgASSA-----APFGGVGASGNHRPSAYYA 458
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-474 |
1.18e-69 |
|
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: 228.26 E-value: 1.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 45 DDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESR-GEV----ERAATTLQISAEE 117
Cdd:cd07135 5 DEIDSIHSRLRATFRSgkTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVsgvkNDILHMLKNLKKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 118 AKrihGEGVPVESAQGSENRmAFTVKVPVGVVAAITPFNVPINLVchkLGP---AIAAGNSVVLKPAEVTPICALKLAEL 194
Cdd:cd07135 85 AK---DEKVKDGPLAFMFGK-PRIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 195 MEEAgLPKGRLQVLTGDGAEIGEwLLEnQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAAS 272
Cdd:cd07135 158 VPKY-LDPDAFQVVQGGVPETTA-LLE-QKFDKIFYTGSGRVGRIIAEAAAkhLTPVTLELGGKSPVIVTKNADLELAAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 273 LISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPmDEQTDIGPMIRLKEAERVEEWVKEAveeGAKIE 352
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTT---KGKVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 353 LGGKRDGA--FYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVG 430
Cdd:cd07135 311 IGGEMDEAtrFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 654965072 431 GLIVND-ASAYRVDHMPYGGVKKSGNGKEGPKYAIEEMTEERIIV 474
Cdd:cd07135 391 GVVINDtLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
56-459 |
5.73e-62 |
|
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: 208.11 E-value: 5.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 56 EALKNTF--SPY----ERYEVLMKAAELLLSRQEEFAEILATEVG-KSIRESR-GEVeraATTLQiSAEEAKRiHGEG-- 125
Cdd:cd07133 5 ERQKAAFlaNPPpsleERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEI---LPSIA-GIKHARK-HLKKwm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 126 ----VPVE-SAQGSENRMAFTvkvPVGVVAAITPFNVPINLVchkLGP---AIAAGNSVVLKPAEVTPICALKLAELMEE 197
Cdd:cd07133 80 kpsrRHVGlLFLPAKAEVEYQ---PLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 198 AGLPKgRLQVLTGdGAEIGEwllenqdvnMFT--------FTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADL 267
Cdd:cd07133 154 YFDED-EVAVVTG-GADVAA---------AFSslpfdhllFTGSTAVGRHVMRAAAenLTPVTLELGGKSPAIIAPDADL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 268 EKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKL---VVGNPmdeqtDIGPMIRLKEAERVEEWVKEA 344
Cdd:cd07133 223 AKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 345 VEEGAK-IELGGKRDGAF----YLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQF 419
Cdd:cd07133 298 RAKGARvIELNPAGEDFAatrkLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAE 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 654965072 420 AMKAAREIEVGGLIVNDASA-YRVDHMPYGGVKKSG----NGKEG 459
Cdd:cd07133 378 QDRVLRRTHSGGVTINDTLLhVAQDDLPFGGVGASGmgayHGKEG 422
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
139-456 |
1.39e-61 |
|
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: 207.36 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 139 AFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGDGAEIGEW 218
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 219 LleNQDVNMFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHT 296
Cdd:cd07136 173 L--DQKFDYIFFTGSVRVGKIVMEAAAkhLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 297 NIYTAFVNKLKEKTEKLVVGNPMDEqTDIGPMIRLKEAERVEEWVKEaveegAKIELGGKRD-GAFYL-PTILTNVNDEM 374
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDPLES-PDYGRIINEKHFDRLAGLLDN-----GKIVFGGNTDrETLYIePTILDNVTWDD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 375 KVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRV-DHMPYGGVKKS 453
Cdd:cd07136 325 PVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLAnPYLPFGGVGNS 404
|
...
gi 654965072 454 GNG 456
Cdd:cd07136 405 GMG 407
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
58-465 |
5.79e-58 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 199.10 E-value: 5.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 58 LKNTFS-----PYE-RYEVLMKAAELLLSRQEEFAEILATEVGKSIRES--------RGEVERaatTLQISAEEAKRihg 123
Cdd:PTZ00381 16 LKESFLtgktrPLEfRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEH---LLKHLDEYLKP--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 124 EGVPVESAQGSENrmAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKG 203
Cdd:PTZ00381 90 EKVDTVGVFGPGK--SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 204 RLQVLTGDGAEIGEWLLENQDVnmFTFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNN 281
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDH--IFFTGSPRVGKLVMQAAAenLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 282 AGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMdEQTDIGPMIRLKEAERVEEWVKeavEEGAKIELGGKRDGA- 360
Cdd:PTZ00381 245 AGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPK-KSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGEVDIEn 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 361 -FYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASA 439
Cdd:PTZ00381 321 kYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVF 400
|
410 420
....*....|....*....|....*..
gi 654965072 440 YRV-DHMPYGGVKKSGNGKEGPKYAIE 465
Cdd:PTZ00381 401 HLLnPNLPFGGVGNSGMGAYHGKYGFD 427
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
25-435 |
1.05e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 198.05 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 25 MEVLNKYTQQPAAEISVATKDDVNKAVASAKEAL---KNTfSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESR 101
Cdd:PLN02419 131 IDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFplwRNT-PITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 102 GEVERAATTLQISAEEAKRIHGEGVPvESAQGSENrmaFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPA 181
Cdd:PLN02419 210 GDIFRGLEVVEHACGMATLQMGEYLP-NVSNGVDT---YSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 182 EVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEwLLENQDVNMFTFTGSPRVGELI--RSKAGLRKVSLELGNNSAT 259
Cdd:PLN02419 286 EKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIyaRAAAKGKRIQSNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 260 VVHKDADLEKAASLISQKSFNNAGQVCISVQRIyVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEE 339
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 340 WVKEAVEEGAKIELGGK-------RDGAFYLPTILTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGL 412
Cdd:PLN02419 444 LIQSGVDDGAKLLLDGRdivvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAI 523
|
410 420
....*....|....*....|...
gi 654965072 413 FTNDLQFAMKAAREIEVGGLIVN 435
Cdd:PLN02419 524 FTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
9-462 |
1.45e-56 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 202.35 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 9 QYGLYVNGewetTAEKMEVLNKY-TQQPAAEISVATKDDVNKAVASAKEALK---NTfSPYERYEVLMKAAELLLSRQEE 84
Cdd:PRK11904 552 QAGPIING----EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPawsRT-PVEERAAILERAADLLEANRAE 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 85 FAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKvpvGVVAAITPFNVPINLVCH 164
Cdd:PRK11904 627 LIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGR---GVFVCISPWNFPLAIFLG 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 165 KLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI-RSK 243
Cdd:PRK11904 704 QVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTL 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 244 AGlRK---VSL--ELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCiSVQRI-YVHTNIYTAFVNKLKEKTEKLVVGN 317
Cdd:PRK11904 784 AA-RDgpiVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRC-SALRVlFVQEDIADRVIEMLKGAMAELKVGD 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 318 PMDEQTDIGPMIRLKEAERVEEWVKEAVEEG---AKIELG-GKRDGAFYLPTI--LTNVNDemkvCRQEVFGPVVAIAQY 391
Cdd:PRK11904 862 PRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPaGTENGHFVAPTAfeIDSISQ----LEREVFGPILHVIRY 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 392 --DEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNdasayR------VDHMPYGGVKKSGNGKE--GPK 461
Cdd:PRK11904 938 kaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-----RnqigavVGVQPFGGQGLSGTGPKagGPH 1012
|
.
gi 654965072 462 Y 462
Cdd:PRK11904 1013 Y 1013
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
42-462 |
2.74e-52 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 190.46 E-value: 2.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 42 ATKDDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAK 119
Cdd:PRK11905 587 ASAEDVERALAAAQAAFPEwsATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQAR 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 120 RihgegvpveSAQGSENRmaftvkvPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAG 199
Cdd:PRK11905 667 R---------LLNGPGHK-------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 200 LPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIR---SKAGLRKVSL--ELGNNSATVVHKDADLEKAASLI 274
Cdd:PRK11905 731 VPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQrtlAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADV 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 275 SQKSFNNAGQVCiSVQRI-YVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIEL 353
Cdd:PRK11905 811 IASAFDSAGQRC-SALRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQ 889
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 354 GGKRD----GAFYLPTI--LTNVNDeMKvcrQEVFGPVVAIAQY--DEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAR 425
Cdd:PRK11905 890 LPLPAetekGTFVAPTLieIDSISD-LE---REVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSRIDETIAHVTS 965
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 654965072 426 EIEVGGLIVNdasayR------VDHMPYGGVKKSGNGKE--GPKY 462
Cdd:PRK11905 966 RIRAGNIYVN-----RniigavVGVQPFGGEGLSGTGPKagGPLY 1005
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
14-462 |
7.03e-52 |
|
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: 182.80 E-value: 7.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 14 VNGEWETTAEKMEVLNKYTQQP-AAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILA 90
Cdd:TIGR01238 42 IGHSYKADGEAQPVTNPADRRDiVGQVFHANLAHVQAAIDSAQQAFPtwNATPAKERAAKLDRLADLLELHMPELMALCV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 91 TEVGKSIRESRGEVERAATTLQISAEEAKRIHGEgvpvesaqgsenrmaFTVKvPVGVVAAITPFNVPINLVCHKLGPAI 170
Cdd:TIGR01238 122 REAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGE---------------FSVE-SRGVFVCISPWNFPLAIFTGQISAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 171 AAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIR---SKAGLR 247
Cdd:TIGR01238 186 AAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINqtlAQREDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 248 KVSL--ELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDI 325
Cdd:TIGR01238 266 PVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 326 GPMIRLKEAERVEEWVKEAVEEGAKI------ELGGKRDGAFYLPTILTnvNDEMKVCRQEVFGPVVAIAQY--DEIDEV 397
Cdd:TIGR01238 346 GPVIDAEAKQNLLAHIEHMSQTQKKIaqltldDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYkaRELDQI 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654965072 398 ISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVN-DASAYRVDHMPYGGVKKSGNGKE--GPKY 462
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrNQVGAVVGVQPFGGQGLSGTGPKagGPHY 491
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-414 |
5.33e-51 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 180.80 E-value: 5.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 11 GLYVNGEWETTAEKMEVLNKYTQQPAAEISVATKDDVN---KAVASAKEALKNTFSPyERYEVLMKAAELLLSRQEEFAE 87
Cdd:PLN02315 22 GCYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEeglRACEEAAKIWMQVPAP-KRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 88 ILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVESAqgseNRMAFTVKVPVGVVAAITPFNVPinlvCHKLG 167
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERP----NHMMMEVWNPLGIVGVITAFNFP----CAVLG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 168 ----PAIAAGNSVVLKPAEVTPICALKL----AELMEEAGLPKGRLQVLTGdGAEIGEWLLENQDVNMFTFTGSPRVGEL 239
Cdd:PLN02315 173 wnacIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 240 IRSKAGLR--KVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGN 317
Cdd:PLN02315 252 VQQTVNARfgKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 318 PMDEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIELGGK---RDGAFYLPTILtNVNDEMKVCRQEVFGPVVAIAQYDEI 394
Cdd:PLN02315 332 PLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSaieSEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTL 410
|
410 420
....*....|....*....|
gi 654965072 395 DEVISKVNDSDYGLQAGLFT 414
Cdd:PLN02315 411 EEAIEINNSVPQGLSSSIFT 430
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-459 |
8.30e-50 |
|
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: 177.78 E-value: 8.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 12 LYVNGEWETTAEKMEVLNKYT-QQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEefAEI 88
Cdd:cd07123 35 LVIGGKEVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKewARMPFEDRAAIFLKAADLLSGKYR--YEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 89 LA-TEVGKSIRESRGEVERAAT---TLQISAEEAKRIHGEGvPVESAQGSENRMAFTvkvPV-GVVAAITPFN---VPIN 160
Cdd:cd07123 113 NAaTMLGQGKNVWQAEIDAACElidFLRFNVKYAEELYAQQ-PLSSPAGVWNRLEYR---PLeGFVYAVSPFNftaIGGN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 161 LVChklGPAIAaGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGS------- 233
Cdd:cd07123 189 LAG---APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGStptfksl 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 234 -PRVGELIRSKAGLRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEK 312
Cdd:cd07123 265 wKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 313 LVVGNPMDEQTDIGPMIRLKEAERVEEWVKEAVEE-GAKIELGGKRD---GAFYLPTILTNVNDEMKVCRQEVFGPVVAI 388
Cdd:cd07123 345 IKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDdsvGYFVEPTVIETTDPKHKLMTEEIFGPVLTV 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654965072 389 AQYD--EIDEVISKVND-SDYGLQAGLFTNDLQFAMKAAREIE--VGGLIVNDAS-AYRVDHMPYGGVKKSG-NGKEG 459
Cdd:cd07123 425 YVYPdsDFEETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPtGAVVGQQPFGGARASGtNDKAG 502
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
14-461 |
5.46e-49 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 180.52 E-value: 5.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 14 VNGEwETTAEKMEVLNKY-TQQPAAEISVATKDDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILA 90
Cdd:COG4230 562 IAGE-AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPawSATPVEERAAILERAADLLEAHRAELMALLV 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 91 TEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVEsaqgsenrmaftvkvPVGVVAAITPFNVPINLVCHKLGPAI 170
Cdd:COG4230 641 REAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLR---------------GRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 171 AAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI-RSKAGlRK- 248
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInRTLAA-RDg 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 249 --VSL--ELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCiSVQRI-YVHTNIYTAFVNKLKEKTEKLVVGNPMDEQT 323
Cdd:COG4230 785 piVPLiaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRC-SALRVlCVQEDIADRVLEMLKGAMAELRVGDPADLST 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 324 DIGPMIRlKEA-ERVEEWVKEAVEEGAKI---ELG-GKRDGAFYLPTI--LTNVnDEMKvcrQEVFGPVVAIAQY--DEI 394
Cdd:COG4230 864 DVGPVID-AEArANLEAHIERMRAEGRLVhqlPLPeECANGTFVAPTLieIDSI-SDLE---REVFGPVLHVVRYkaDEL 938
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654965072 395 DEVISKVNDSDYGLQAGLFT-NDlQFAMKAAREIEVGGLIVNdasayRvdHM--------PYGGVKKSGNgkeGPK 461
Cdd:COG4230 939 DKVIDAINATGYGLTLGVHSrID-ETIDRVAARARVGNVYVN-----R--NIigavvgvqPFGGEGLSGT---GPK 1003
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
139-471 |
2.37e-48 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 172.02 E-value: 2.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 139 AFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELmeeagLPK----GRLQVLTGDGAE 214
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKyldkECYPVVLGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 215 IGEwLLENQDVNMFtFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRI 292
Cdd:cd07132 169 TTE-LLKQRFDYIF-YTGSTSVGKIVMQAAAkhLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 293 YVHTNIYTAFVNKLKeKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVkeaveEGAKIELGGKRDGA--FYLPTILTNV 370
Cdd:cd07132 247 LCTPEVQEKFVEALK-KTLKEFYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTDEKerYIAPTVLTDV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 371 NDEMKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDA-SAYRVDHMPYGG 449
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTiMHYTLDSLPFGG 400
|
330 340
....*....|....*....|..
gi 654965072 450 VKKSGNGKEGPKYAIEEMTEER 471
Cdd:cd07132 401 VGNSGMGAYHGKYSFDTFSHKR 422
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
64-473 |
3.47e-46 |
|
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: 166.05 E-value: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 64 PYE-RYEVLMKAAELLLSRQEEFAEILATEVGKSIRES-RGEVE--RAATTLQISaEEAKRIHGEGVPVESAQGSENrmA 139
Cdd:cd07137 19 SAEwRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSvlVSSCKLAIK-ELKKWMAPEKVKTPLTTFPAK--A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 140 FTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGdGAEIGEWL 219
Cdd:cd07137 96 EIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 220 LENQDVNMFtFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLEKAAS-LISQKSFNNAGQVCISVQRIYVHT 296
Cdd:cd07137 174 LEQKWDKIF-FTGSPRVGRIIMAAAAkhLTPVTLELGGKCPVIVDSTVDLKVAVRrIAGGKWGCNNGQACIAPDYVLVEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 297 NIYTAFVNKLKEKTEKLVVGNPMdEQTDIGPMIRLKEAERVEEWVKEAvEEGAKIELGGKRD--GAFYLPTILTNVNDEM 374
Cdd:cd07137 253 SFAPTLIDALKNTLEKFFGENPK-ESKDLSRIVNSHHFQRLSRLLDDP-SVADKIVHGGERDekNLYIEPTILLDPPLDS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 375 KVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASA-YRVDHMPYGGVKKS 453
Cdd:cd07137 331 SIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqYAIDTLPFGGVGES 410
|
410 420
....*....|....*....|
gi 654965072 454 GNGKEGPKYAIEEMTEERII 473
Cdd:cd07137 411 GFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
13-458 |
5.51e-41 |
|
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: 153.58 E-value: 5.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEWET-TAEKMEVLNKYTQQPAAEISVATKDdVNKAVASAKE----ALKN-TFspYERYEVLMKAAELLLSRQEEFA 86
Cdd:cd07128 4 YVAGQWHAgTGDGRTLHDAVTGEVVARVSSEGLD-FAAAVAYAREkggpALRAlTF--HERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 87 EIlATEVGKSIRESRGEVERAATTLQISAEEAKR------IHGEGvPVESAQGSENRMAFTVKVPVGVVAA-ITPFNVPI 159
Cdd:cd07128 81 AL-SAATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahFLVEG-DVEPLSKDGTFVGQHILTPRRGVAVhINAFNFPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 160 NLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAG-LPKGRLQVLTGDGAEIGEWLLEnQDVnmFTFTGSPRVGE 238
Cdd:cd07128 159 WGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGE-QDV--VAFTGSAATAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 239 LIRSKAGLRK----VSLELGNNSATVVHKDA-------DL---EKAASLISQksfnnAGQVCISVQRIYVHTNIYTAFVN 304
Cdd:cd07128 236 KLRAHPNIVArsirFNAEADSLNAAILGPDAtpgtpefDLfvkEVAREMTVK-----AGQKCTAIRRAFVPEARVDAVIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 305 KLKEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVkEAVEEGAKIELGGK----------RDGAFYLPTILTnVNDEM 374
Cdd:cd07128 311 ALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPdrfevvgadaEKGAFFPPTLLL-CDDPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 375 K---VCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIE--VGGLIVNDASAYR-------- 441
Cdd:cd07128 389 AataVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAApyHGRLLVLNRDSAKestghgsp 468
|
490
....*....|....*..
gi 654965072 442 VDHMPYGGVKKSGNGKE 458
Cdd:cd07128 469 LPQLVHGGPGRAGGGEE 485
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
42-462 |
6.75e-41 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 156.67 E-value: 6.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 42 ATKDDVNKAVASAKEALKNTFS--PYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAK 119
Cdd:PRK11809 679 ATPAEVEQALESAVNAAPIWFAtpPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 120 RihgegvpvesaqgsenrmAFTVKV--PVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEE 197
Cdd:PRK11809 759 D------------------DFDNDThrPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLE 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 198 AGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELI-RSKAGL-----RKVSL--ELGNNSATVVHKDADLEK 269
Cdd:PRK11809 821 AGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLAGRldpqgRPIPLiaETGGQNAMIVDSSALTEQ 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 270 AASLISQKSFNNAGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDEQTDIGPMIRlKEA----ERVEEWVKEA- 344
Cdd:PRK11809 901 VVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVID-AEAkaniERHIQAMRAKg 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 345 --VEEGAKIELGGKRDGAFYLPTI--LTNVnDEMKvcrQEVFGPVVAIAQY--DEIDEVISKVNDSDYGLQAGLFTNDLQ 418
Cdd:PRK11809 980 rpVFQAARENSEDWQSGTFVPPTLieLDSF-DELK---REVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRIDE 1055
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 654965072 419 FAMKAAREIEVGGLIVNdasayR------VDHMPYGGVKKSGNGKE--GPKY 462
Cdd:PRK11809 1056 TIAQVTGSAHVGNLYVN-----RnmvgavVGVQPFGGEGLSGTGPKagGPLY 1102
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
76-474 |
2.11e-38 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 145.64 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 76 ELLLSRQEEFAEILATEVGK----SIRESRGEVERAAT-TLQISAEEAKRIHGEgVPVESAQGSenrmAFTVKVPVGVVA 150
Cdd:PLN02203 39 RLLKDNEEAIFKALHQDLGKhrveAYRDEVGVLTKSANlALSNLKKWMAPKKAK-LPLVAFPAT----AEVVPEPLGVVL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 151 AITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMeEAGLPKGRLQVLTGdGAEIGEWLLENQDVNMFtF 230
Cdd:PLN02203 114 IFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEG-GPAVGEQLLQHKWDKIF-F 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 231 TGSPRVGELIRSKAG--LRKVSLELGNNSATVVH---KDADLEKAASLISQKSFNN-AGQVCISVQRIYVHTNIYTAFVN 304
Cdd:PLN02203 191 TGSPRVGRIIMTAAAkhLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 305 KLKEKTEKLVVGNPmDEQTDIGPMIRLKEAERVEEWVKE-AVEegAKIELGGKRD--GAFYLPTILTNVNDEMKVCRQEV 381
Cdd:PLN02203 271 LLKSTIKKFFGENP-RESKSMARILNKKHFQRLSNLLKDpRVA--ASIVHGGSIDekKLFIEPTILLNPPLDSDIMTEEI 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 382 FGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDAS-AYRVDHMPYGGVKKSGNGKEGP 460
Cdd:PLN02203 348 FGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIiQYACDSLPFGGVGESGFGRYHG 427
|
410
....*....|....
gi 654965072 461 KYAIEEMTEERIIV 474
Cdd:PLN02203 428 KYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
139-474 |
4.54e-34 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 133.63 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 139 AFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAgLPKGRLQVLTGDGAEIGEw 218
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTA- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 219 LLENQDVNMFtFTGSPRVGELIRSKAG--LRKVSLELGNNSATVVHKDADLE-KAASLISQKSFNNAGQVCISVQRIYVH 295
Cdd:PLN02174 184 LLEQKWDKIF-YTGSSKIGRVIMAAAAkhLTPVVLELGGKSPVVVDSDTDLKvTVRRIIAGKWGCNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 296 TNIYTAFVNKLKEKTEKLVVGNPMdEQTDIGPMIRLKEAERVEEWVKEAvEEGAKIELGGKRD--GAFYLPTILTNVNDE 373
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLDEK-EVSDKIVYGGEKDreNLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 374 MKVCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIVNDASAYRVDH-MPYGGVKK 452
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGVGE 420
|
330 340
....*....|....*....|..
gi 654965072 453 SGNGKEGPKYAIEEMTEERIIV 474
Cdd:PLN02174 421 SGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
13-419 |
2.22e-29 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 120.29 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEWETTAEKMEVLNKYTQQPAAEISVATKDDVNKAVASA----KEALKNTFSPYERY----EVLMKAAELLLSRQEE 84
Cdd:cd07126 2 LVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLrqcpKSGLHNPLKNPERYllygDVSHRVAHELRKPEVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 85 --FAEILATEVGKSIRESRGEVERAATTLQISAEEAKRIHGEGVPVE-SAQGSENRmafTVKVPVGVVAAITPFNVPINL 161
Cdd:cd07126 82 dfFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPgDHQGQQSS---GYRWPYGPVAIITPFNFPLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 162 VCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLEnQDVNMFTFTGSPRVGE-LI 240
Cdd:cd07126 159 PALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSSKVAErLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 241 RSKAGlrKVSLELGNNSATVVHKD-ADLEKAASLISQKSFNNAGQVCiSVQRI-YVHTN-IYTAFVNKLKEKTEKLVVgn 317
Cdd:cd07126 238 LELHG--KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKC-SAQSIlFAHENwVQAGILDKLKALAEQRKL-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 318 pmdEQTDIGPMIRLkEAERVEEWVKEAVE-EGAKIELGGK--------------RDGAFYLPTILTNVNDEMKVCRQEVF 382
Cdd:cd07126 313 ---EDLTIGPVLTW-TTERILDHVDKLLAiPGAKVLFGGKpltnhsipsiygayEPTAVFVPLEEIAIEENFELVTTEVF 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 654965072 383 GPVVAIAQY--DEIDEVISKVNDSDYGLQAGLFTNDLQF 419
Cdd:cd07126 389 GPFQVVTEYkdEQLPLVLEALERMHAHLTAAVVSNDIRF 427
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
67-434 |
2.24e-29 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 119.65 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 67 RYEVLMKAAELLLSRQEEFAEILATEVGKSiRESRGEVERAATTLQISAEEAKRIHGEGVPVESAQGSENRMAFTVKVPV 146
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQQSHGYRWPY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 147 GVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAG-LPKGRLQVLTGDGaEIGEWLLENQDV 225
Cdd:cd07084 102 GPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDG-KTMQALLLHPNP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 226 NMFTFTGSPRVGELIRSKAGLRKVSLELGNNSATVVHKDADLEKA-ASLISQKSFNNAGQVCISVQRIYVHTNIY-TAFV 303
Cdd:cd07084 181 KMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQAVDYvAWQCVQDMTACSGQKCTAQSMLFVPENWSkTPLV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 304 NKLKEKTEKLVvgnpmDEQTDIGPMIRLKEAERVEEwvkEAVEEGAKIELGGKRDGAFYLPTI--------LTNVNDEM- 374
Cdd:cd07084 261 EKLKALLARRK-----LEDLLLGPVQTFTTLAMIAH---MENLLGSVLLFSGKELKNHSIPSIygacvasaLFVPIDEIl 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654965072 375 ---KVCRQEVFGPVVAIAQY--DEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREIEVGGLIV 434
Cdd:cd07084 333 ktyELVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTY 397
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
13-458 |
4.44e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 119.81 E-value: 4.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 13 YVNGEWET-TAEKMEVLNKYTQQPAAEISvATKDDVNKAVASAKE----ALKN-TFSpyERYEVLMKAAELLLSRQEEFA 86
Cdd:PRK11903 8 YVAGRWQAgSGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFAREqggaALRAlTYA--QRAALLAAIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 87 EIlATEVGKSIR-ESRGEVERAATTLQISAEEAKRIHGEGVPVESAQGSENR-MAFTVK---VPV-GVVAAITPFNVPIN 160
Cdd:PRK11903 85 DI-ATANSGTTRnDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKdPAFQGQhvlVPTrGVALFINAFNFPAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 161 LVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEAG-LPKGRLQVLTGDGAEIGEwLLENQDVnmFTFTGSPRVGEL 239
Cdd:PRK11903 164 GLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLD-HLQPFDV--VSFTGSAETAAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 240 IRSKAGLR----KVSLELGNNSATVVHKDAD---------LEKAASLISQKSfnnaGQVCISVQRIYVHTNIYTAFVNKL 306
Cdd:PRK11903 241 LRSHPAVVqrsvRVNVEADSLNSALLGPDAApgseafdlfVKEVVREMTVKS----GQKCTAIRRIFVPEALYDAVAEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 307 KEKTEKLVVGNPMDEQTDIGPMIRLKEAERVEEWVkEAVEEGAKIELGGKRD---------GAFYLPTIL--TNVNDEMK 375
Cdd:PRK11903 317 AARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFalvdadpavAACVGPTLLgaSDPDAATA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 376 VCRQEVFGPVVAIAQYDEIDEVISKVNDSDYGLQAGLFTNDLQFAMKAAREI-EVGG---LIVNDASAYRVDH---MP-- 446
Cdd:PRK11903 396 VHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELaDSHGrvhVISPDVAALHTGHgnvMPqs 475
|
490
....*....|...
gi 654965072 447 -YGGVKKSGNGKE 458
Cdd:PRK11903 476 lHGGPGRAGGGEE 488
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
134-439 |
3.63e-15 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 77.15 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 134 SENRMAFTVKV--PVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELM----EEAGLPKGRLQV 207
Cdd:cd07122 82 EEDEEKGIVEIaePVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQW 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 208 LTGDGAEIGEWLLENQDVNMFTFTGSPrvgELIRSKAGLRKVSLELG-NNSATVVHKDADLEKAA-SLISQKSFNNaGQV 285
Cdd:cd07122 162 IEEPSIELTQELMKHPDVDLILATGGP---GMVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVkDIILSKTFDN-GTI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 286 CISVQRIYVHTNIYTAFVNKLKE-------KTEKLVVGNPM-DEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIeLGGKR 357
Cdd:cd07122 238 CASEQSVIVDDEIYDEVRAELKRrgayflnEEEKEKLEKALfDDGGTLNPDIVGKSAQKIAELAGIEVPEDTKV-LVAEE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 358 DGafylptiltnVNDEMKVCRqEVFGPVVAIAQYDEIDEVISKVND----SDYGLQAGLFTNDLQFAMKAAREIEVGGLI 433
Cdd:cd07122 317 TG----------VGPEEPLSR-EKLSPVLAFYRAEDFEEALEKARElleyGGAGHTAVIHSNDEEVIEEFALRMPVSRIL 385
|
....*.
gi 654965072 434 VNDASA 439
Cdd:cd07122 386 VNTPSS 391
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
47-425 |
1.04e-14 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 75.77 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 47 VNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKsiresrGEVERAATTLQISAEEAKRIHGE 124
Cdd:cd07081 1 LDDAVAAAKVAQQglSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGM------GRVEDKVIKNHFAAEYIYNVYKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 125 GVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKP----AEVTPICALKLAELMEEAGL 200
Cdd:cd07081 75 EKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 201 PKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSkAGLRKVSLELGnNSATVVHKDADLEKAA-SLISQKSF 279
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYS-SGKPAIGVGAG-NTPVVIDETADIKRAVqSIVKSKTF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 280 NNaGQVCISVQRIYVHTNIYTAFVNKLKEKTEKLVVGNPMDE-------QTDIGPMIRLKEAERVEEWVKEAVEEGAKIE 352
Cdd:cd07081 233 DN-GVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQvqpvilkNGDVNRDIVGQDAYKIAAAAGLKVPQETRIL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 353 LGGkrdgafylptilTNVNDEMKVCRQEVFGPVVAIAQYDEIDEVISK----VNDSDYGLQAGLFTNDL-------QF-- 419
Cdd:cd07081 312 IGE------------VTSLAEHEPFAHEKLSPVLAMYRAANFADADAKalalKLEGGCGHTSAMYSDNIkaienmnQFan 379
|
....*.
gi 654965072 420 AMKAAR 425
Cdd:cd07081 380 AMKTSR 385
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
61-353 |
1.09e-14 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 75.72 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 61 TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESR-------GEVERAATTLQISAEEAKRIHGEGVPVESAQG 133
Cdd:cd07077 12 VNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIanwiammGCSESKLYKNIDTERGITASVGHIQDVLLPDN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 134 SEnrmAFTVKVPVGVVAAITPFNVPInLVCHKLGPAIAAGNSVVLKPAEVTPICALKLAELMEEA---GLPKGRLQVLTG 210
Cdd:cd07077 92 GE---TYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 211 DGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLRKVSLELGNNSATVVHKDADLEKAASLISQ-KSFNNAgqVCISV 289
Cdd:cd07077 168 PSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDsKFFDQN--ACASE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654965072 290 QRIYVHTNIYTAfvnKLKEKTEKLVVgnpmdEQTDIGPMIRLKEAERVEEWVKEAVEEGAKIEL 353
Cdd:cd07077 246 QNLYVVDDVLDP---LYEEFKLKLVV-----EGLKVPQETKPLSKETTPSFDDEALESMTPLEC 301
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
47-435 |
4.63e-14 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 74.11 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 47 VNKAVASAKEA---LKNTfSPYERYEVLMKAAELLLSRQEEFAEILATEVGKSIRESRGEVERAATTLQISAEEAKRihG 123
Cdd:cd07129 1 VDAAAAAAAAAfesYRAL-SPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRE--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 124 E--GVPVESAQGSEN--------RMaftvKVPVGVVAAITPFNVPinLVCHKLG----PAIAAGNSVVLK--PA--EVTP 185
Cdd:cd07129 78 SwlDARIDPADPDRQplprpdlrRM----LVPLGPVAVFGASNFP--LAFSVAGgdtaSALAAGCPVVVKahPAhpGTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 186 ICALKLAELMEEAGLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLRK----VSLELGNNSATVV 261
Cdd:cd07129 152 LVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepipFYAELGSVNPVFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 262 HKDAdLEKAASLISQK---SFN-NAGQVCISVQRIYVHTNI-YTAFVNKLKEKTEKLVVGnPMdeqtdIGPMIRLKEAER 336
Cdd:cd07129 232 LPGA-LAERGEAIAQGfvgSLTlGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQ-TM-----LTPGIAEAYRQG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 337 VEEWVKEAVEEgAKIELGGKRDGAFYLPTIL-TNVNDEMK--VCRQEVFGPVVAIAQYDEIDE---VISKVNDSdygLQA 410
Cdd:cd07129 305 VEALAAAPGVR-VLAGGAAAEGGNQAAPTLFkVDAAAFLAdpALQEEVFGPASLVVRYDDAAEllaVAEALEGQ---LTA 380
|
410 420
....*....|....*....|....*....
gi 654965072 411 GLF--TNDLQFAMKAAREIE--VGGLIVN 435
Cdd:cd07129 381 TIHgeEDDLALARELLPVLErkAGRLLFN 409
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
45-308 |
2.13e-10 |
|
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: 62.64 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 45 DDVNKAVASAKEALK--NTFSPYERYEVLMKAAELLLSRQEEFAEILATEVGksiresRGEVERAATTLQISAEeakRIH 122
Cdd:cd07121 4 ATVDDAVAAAKAAQKqyRKCTLADREKIIEAIREALLSNAEELAEMAVEETG------MGRVEDKIAKNHLAAE---KTP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 123 GEGVPVESAQGSENRMAFTVKVPVGVVAAITPFNVPI-NLVCHKLGpAIAAGNSVVLKPAEVTPICALKLAELMEEA--- 198
Cdd:cd07121 75 GTEDLTTTAWSGDNGLTLVEYAPFGVIGAITPSTNPTeTIINNSIS-MLAAGNAVVFNPHPGAKKVSAYAVELINKAiae 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 199 -GLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRsKAGLRKVSLELGnNSATVVHKDADLEKAA-SLISQ 276
Cdd:cd07121 154 aGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAAL-SSGKKAIGAGAG-NPPVVVDETADIEKAArDIVQG 231
|
250 260 270
....*....|....*....|....*....|..
gi 654965072 277 KSFNNaGQVCISVQRIYVHTNIYTAFVNKLKE 308
Cdd:cd07121 232 ASFDN-NLPCIAEKEVIAVDSVADYLIAAMQR 262
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
25-308 |
4.06e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 55.29 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 25 MEVLNKYTQQPAAEISVATK-----DDVNKAVASAKEALKN--TFSPYERYEVLMKAAELLLSRQEEFAEILATEVGksi 97
Cdd:PRK15398 11 KAVLAEMLSSQTVSPPAAVGemgvfASVDDAVAAAKVAQQRyqQKSLAMRQRIIDAIREALLPHAEELAELAVEETG--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 98 resRGEVERAATTLQISAEeakrihgeGVP-VE----SAQGSENRMAFTVKVPVGVVAAITPFNVPI-NLVCHKLGpAIA 171
Cdd:PRK15398 88 ---MGRVEDKIAKNVAAAE--------KTPgVEdlttEALTGDNGLTLIEYAPFGVIGAVTPSTNPTeTIINNAIS-MLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 172 AGNSVVLKPAEVTPICALKLAELMEEA----GLPKGRLQVLTGDGAEIGEWLLENQDVNMFTFTGSPRVGELIRsKAGLR 247
Cdd:PRK15398 156 AGNSVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAM-KSGKK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654965072 248 KVSLELGNNSAtVVHKDADLEKAA-SLISQKSFNNaGQVCISVQRIYVHTNIYTAFVNKLKE 308
Cdd:PRK15398 235 AIGAGAGNPPV-VVDETADIEKAArDIVKGASFDN-NLPCIAEKEVIVVDSVADELMRLMEK 294
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
105-440 |
6.61e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 51.71 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 105 ERAATTLQISAEEAKRIHGEGVpVESAQGSENRMA----FTVkVPVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKP 180
Cdd:cd07127 151 DRGLEAVAYAWREMSRIPPTAE-WEKPQGKHDPLAmektFTV-VPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 181 AevtPICALKLA-------ELMEEAGL-PKgrLQVLTGD--GAEIGEWLLENQDVNMFTFTGSPRVGELIRSKAGLRKVS 250
Cdd:cd07127 229 H---PAAILPLAitvqvarEVLAEAGFdPN--LVTLAADtpEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 251 LELGNNSATVVHKDADLEKAASLISQKSFNNAGQVCISVQRIYVHTN---------IYTAFVNKLKEKTEKLvVGNPMDE 321
Cdd:cd07127 304 TEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 322 QTDIGPMIRLKEAERVEEWVK--EAVEEGAKIELGGKRDGAFYLPTILTNVNDEMKVCRQEVFGP---VVAIAQYDEIDE 396
Cdd:cd07127 383 AALLGAIQSPDTLARIAEARQlgEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPiafVVATDSTDHSIE 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 654965072 397 VISKVNDSDYGLQAGLFTNDLQF---AMKAAREIEV-------GGLIVNDASAY 440
Cdd:cd07127 463 LARESVREHGAMTVGVYSTDPEVverVQEAALDAGValsinltGGVFVNQSAAF 516
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
134-439 |
4.14e-06 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 49.41 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 134 SENRMAFTVKV--PVGVVAAITPFNVPINLVCHKLGPAIAAGNSVVLKP---AEVTPICALKLA-ELMEEAGLPKGRLQV 207
Cdd:PRK13805 95 EEDDEFGIIEIaePVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFhprAQKSSIAAAKIVlDAAVAAGAPKDIIQW 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 208 LTGDGAEIGEWLLENQDVNMFTFTGSPrvgelirskaGLRKVSLELGN--------NSATVVHKDADLEKA-ASLISQKS 278
Cdd:PRK13805 175 IEEPSVELTNALMNHPGIALILATGGP----------GMVKAAYSSGKpalgvgagNVPAYIDKTADIKRAvNDILLSKT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 279 FNNaGQVCISVQRIYVHTNIYTAFVNKL------------KEKTEKLVVGNpmdEQTDIGPMIRLKEAERVEEWVKEAVE 346
Cdd:PRK13805 245 FDN-GMICASEQAVIVDDEIYDEVKEEFashgayflnkkeLKKLEKFIFGK---ENGALNADIVGQSAYKIAEMAGFKVP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654965072 347 EGAKIELGGkrdgafylptiLTNVNDEMKVCRqEVFGPVVAIAQYDEIDEVISK----VNDSDYGLQAGLFTNDLQF--- 419
Cdd:PRK13805 321 EDTKILIAE-----------VKGVGESEPLSH-EKLSPVLAMYKAKDFEDAVEKaeklVEFGGLGHTAVIYTNDDELike 388
|
330 340
....*....|....*....|...
gi 654965072 420 ---AMKAAReievggLIVNDASA 439
Cdd:PRK13805 389 fglRMKACR------ILVNTPSS 405
|
|
| |
