|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
115-590 |
0e+00 |
|
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: 861.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWTIKHGQRALQPSRRPGPtnfFMKWYKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSE 274
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGG---LLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QVVWSSEFFVELIRKCLEACDEDPDLVQLCYCLPPTenddsANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVE 354
Cdd:cd07098 158 QVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPET-----AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 355 LGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLRQGSDidhlENVDMGA 434
Cdd:cd07098 233 LGGKDPAIVLDDA-DLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLD----GDVDVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 435 MISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQL 514
Cdd:cd07098 308 MISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321828 515 ANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFA-TFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSVCFD 590
Cdd:cd07098 388 ANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTED 464
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
104-587 |
5.10e-163 |
|
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: 475.10 E-value: 5.10e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 104 WNPEEPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSG 183
Cdd:pfam00171 1 WVDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 184 KTMLDAsMGEILVTLEKIQWTIKHGQRaLQPSRRPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALF 263
Cdd:pfam00171 81 KPLAEA-RGEVDRAIDVLRYYAGLARR-LDGETLPSDPGRL------AYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 264 TGNAIVVKCSEQVVWSSEFFVELIRKCleacDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKC 343
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEA----GLPAGVLNVV----TGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 344 AAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSD 423
Cdd:pfam00171 225 AAQNLKRVTLELGGKNPLIVLEDA-DLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK--LKVGDP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 424 IDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGsrfkHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMM 503
Cdd:pfam00171 302 LD--PDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGG----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 504 KAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGEEGLLGLCN 583
Cdd:pfam00171 376 RFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTE 455
|
....
gi 6321828 584 AKSV 587
Cdd:pfam00171 456 VKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
112-591 |
4.84e-139 |
|
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: 414.52 E-value: 4.84e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsM 191
Cdd:COG1012 23 FDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA-R 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 192 GEILVTLEKIQWTIKHGQRAL---QPSRRPGPTNFfmkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAI 268
Cdd:COG1012 102 GEVDRAADFLRYYAGEARRLYgetIPSDAPGTRAY---------VRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 269 VVKCSEQVVWSSEFFVELIRkclEAcDEDPDLVQLCYCLPPtendDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSL 348
Cdd:COG1012 173 VLKPAEQTPLSALLLAELLE---EA-GLPAGVLNVVTGDGS----EVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 349 TPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlE 428
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDA-DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA--LKVGDPLD--P 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 429 NVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNT 508
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEG---GYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 509 DHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSVC 588
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
...
gi 6321828 589 FDT 591
Cdd:COG1012 477 IRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
135-589 |
3.51e-126 |
|
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: 379.63 E-value: 3.51e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 135 DEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTmLDASMGEILVTLEKIQWTIKHGQRALQP 214
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 215 SRRPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLEac 294
Cdd:cd07078 80 VIPSPDPGEL------AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 295 deDPDLVQLCYCLPPTEnddsANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALS 374
Cdd:cd07078 152 --PPGVLNVVTGDGDEV----GAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDA-DLDAAV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 375 SIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAK 454
Cdd:cd07078 225 KGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKA--LKVGNPLD--PDTDMGPLISAAQLDRVLAYIEDAKAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 455 GARLLQGGSRfkhPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKEC 534
Cdd:cd07078 301 GAKLLCGGKR---LEGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 6321828 535 NYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSVCF 589
Cdd:cd07078 378 LRVAERLEAGTVWINDYSVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
115-587 |
3.74e-120 |
|
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: 365.01 E-value: 3.74e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMlDASMGEI 194
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR-ADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWTIKHGQRALQPSRRPgpTNFFMKWyKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSE 274
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVP--TGLLMPN-KKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QvvwsSEFFVELIRKCLEACDEDPDLVQLCYCLPPTenddSANYFTShpGFKHITFIGSQPVAHYILKCAAKSLTPVVVE 354
Cdd:cd07099 157 V----TPLVGELLAEAWAAAGPPQGVLQVVTGDGAT----GAALIDA--GVDKVAFTGSVATGRKVMAAAAERLIPVVLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 355 LGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSDIDhlENVDMGA 434
Cdd:cd07099 227 LGGKDPMIVLADA-DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAK--ARALRPGADDI--GDADIGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 435 MISDNRFDELEALVKDAVAKGARLLQGGsrfkHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQL 514
Cdd:cd07099 302 MTTARQLDIVRRHVDDAVAKGAKALTGG----ARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIAL 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321828 515 ANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFY-VCQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07099 378 ANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAgIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
117-589 |
1.20e-99 |
|
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: 311.67 E-value: 1.20e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEILV 196
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQRA---LQPSRRPGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFHNL---LGPIIAAlftGNAIVV 270
Cdd:cd07103 83 AASFLEWFAEEARRIygrTIPSPAPGKRILVIK---------QPVGVVAAITPWNFPAAMItrkIAPALAA---GCTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 271 KCSEQVVWSSEFFVELirkCLEAcDEDPDLVQLCYCLPPtendDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTP 350
Cdd:cd07103 151 KPAEETPLSALALAEL---AEEA-GLPAGVLNVVTGSPA----EIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 VVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENV 430
Cdd:cd07103 223 VSLELGGNAPFIVFDDA-DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKK--LKVGNGLD--EGT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 431 DMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKhpkyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDH 510
Cdd:cd07103 298 DMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLG----LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDE 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321828 511 CVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFAtFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSVCF 589
Cdd:cd07103 374 VIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL-ISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
134-587 |
2.32e-95 |
|
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: 299.76 E-value: 2.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 134 IDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTmLDASMGEIlvtlEKIQWTI----KHGQ 209
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKP-IAEARAEV----EKCAWICryyaENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 210 RALQPSRRPGPTnffmkwyKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRK 289
Cdd:cd07100 76 AFLADEPIETDA-------GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 290 CleACDEDpdlvqlCYCLPPTENDDSANyFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkN 369
Cdd:cd07100 149 A--GFPEG------VFQNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDA-D 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 370 LDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENVDMGAMISDNRFDELEALVK 449
Cdd:cd07100 219 LDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAA--LKVGDPMD--EDTDLGPLARKDLRDELHEQVE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 450 DAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGA 529
Cdd:cd07100 295 EAVAAGATLLLGGKRPDGP----GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTT 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321828 530 DIKECNYVANSLQTGNVAINDFaTFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07100 371 DLERAERVARRLEAGMVFINGM-VKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
115-587 |
4.20e-92 |
|
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: 292.61 E-value: 4.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNS-DFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGE 193
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 194 ILVTLEKIQWTIKHGQRALQPSRRPGPTNFFMkwYKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCS 273
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLPVPALRGG--PGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 274 EQVVWSSEFFVELIrkclEACDedpdlvqlcycLPP------TENDDSA-NYFTSHPGFKHITFIGSQPVAHYILKCAAK 346
Cdd:cd07089 160 PDTPLSALLLGEII----AETD-----------LPAgvvnvvTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 SLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDh 426
Cdd:cd07089 225 TLKRVLLELGGKSANIVLDDA-DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEA--LPVGDPAD- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 427 lENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAK 506
Cdd:cd07089 301 -PGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 507 NTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINdFATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKS 586
Cdd:cd07089 378 DDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
.
gi 6321828 587 V 587
Cdd:cd07089 457 I 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
141-589 |
4.92e-92 |
|
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: 289.13 E-value: 4.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 141 AGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEILVTLEKIQWTIKHGQRALQPSRRPGP 220
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 221 TNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdEDPDL 300
Cdd:cd06534 82 PGGE------AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 301 VQLCYCLPPTEnddsANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRG 380
Cdd:cd06534 152 VNVVPGGGDEV----GAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDA-DLDAAVEGAVFG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 381 TFQSSGQNCIGIERVIVSKENYDDLVkilndrmtanplrqgsdidhlenvdmgamisdnrfdelEALVkdavakgarllq 460
Cdd:cd06534 227 AFFNAGQICTAASRLLVHESIYDEFV--------------------------------------EKLV------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 461 ggsrfkhpkypqghyfqpTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANS 540
Cdd:cd06534 257 ------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAER 318
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 6321828 541 LQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSVCF 589
Cdd:cd06534 319 LRAGTVYINDSSIGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
117-587 |
3.91e-91 |
|
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: 289.43 E-value: 3.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEILV 196
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TlekIQWTIKHGQRALQPSRRPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQV 276
Cdd:cd07106 83 A---VAWLRYTASLDLPDEVIEDDDTRR------VELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 277 VWSSEFFVELIRKCLEacdedPDLVQLCyclppTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELG 356
Cdd:cd07106 154 PLCTLKLGELAQEVLP-----PGVLNVV-----SGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 357 GKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLRQGSDidhlENVDMGAMI 436
Cdd:cd07106 224 GNDAAIVLPDV-DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLD----PGTTLGPVQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 437 SDNRFDELEALVKDAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLAN 516
Cdd:cd07106 299 NKMQYDKVKELVEDAKAKGAKVLAGGEPLDGP----GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARAN 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321828 517 SAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07106 375 DSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDP-DAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
117-587 |
3.53e-90 |
|
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: 287.21 E-value: 3.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA-QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEIL 195
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 196 V----------TLEKIqwtikHGQralqpSRRPGPTNFfmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTG 265
Cdd:cd07109 83 AaaryfeyyggAADKL-----HGE-----TIPLGPGYF-------VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSSEFFVELirkCLEAcdedpDLVQLCYCLPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAA 345
Cdd:cd07109 146 NAVVVKPAEDAPLTALRLAEL---AEEA-----GLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 346 KSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDid 425
Cdd:cd07109 218 ENVVPVTLELGGKSPQIVFADA-DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRA--LRVGPG-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 426 hLENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKA 505
Cdd:cd07109 293 -LEDPDLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 506 KNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAK 585
Cdd:cd07109 371 DDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTK 450
|
..
gi 6321828 586 SV 587
Cdd:cd07109 451 TV 452
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
117-587 |
5.16e-88 |
|
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: 281.75 E-value: 5.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQST--WGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLD--ASMG 192
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIREtrAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 193 EILVTL-------EKIQwtikhgqRALQPSRRPGPTNFfmkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTG 265
Cdd:cd07114 84 YLAEWYryyaglaDKIE-------GAVIPVDKGDYLNF---------TRREPLGVVAAITPWNSPLLLLAKKLAPALAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSSeffVELIRKCLEACdedpdlvqlcycLPPT-------ENDDSANYFTSHPGFKHITFIGSQPVAH 338
Cdd:cd07114 148 NTVVLKPSEHTPAST---LELAKLAEEAG------------FPPGvvnvvtgFGPETGEALVEHPLVAKIAFTGGTETGR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 339 YILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpL 418
Cdd:cd07114 213 HIARAAAENLAPVTLELGGKSPNIVFDDA-DLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARA--I 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 419 RQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGP 498
Cdd:cd07114 290 RVGDPLD--PETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 499 ILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCqLPFGGINGSGYGKFGGEEGL 578
Cdd:cd07114 368 VLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPS-SPFGGFKDSGIGRENGIEAI 446
|
....*....
gi 6321828 579 LGLCNAKSV 587
Cdd:cd07114 447 REYTQTKSV 455
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
115-579 |
1.76e-87 |
|
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: 280.35 E-value: 1.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEI 194
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHA-FEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWTIKHGQRALQPSRRPGPTNFFMKwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSE 274
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRGAIPVLTR----TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QVVWSSEFFVELIRKC-LEAcdedpDLVQLCyCLPPTEND----DSANYftshpgfkhITFIGSQPVAHYILKCAAKSLT 349
Cdd:cd07101 156 QTALTALWAVELLIEAgLPR-----DLWQVV-TGPGSEVGgaivDNADY---------VMFTGSTATGRVVAERAGRRLI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 350 PVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDHleN 429
Cdd:cd07101 221 GCSLELGGKNPMIVLEDA-DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRA--LRLGAALDY--G 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 430 VDMGAMISDNRFDELEALVKDAVAKGARLLQGGSrfKHPKYpqGHYF-QPTLLVDVTPEMKIAQNEVFGPILVMMKAKNT 508
Cdd:cd07101 296 PDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGR--ARPDL--GPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADD 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321828 509 DHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIND--FATFYVCQLPFGGINGSGYGKFGGEEGLL 579
Cdd:cd07101 372 DEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEgyAAAWASIDAPMGGMKDSGLGRRHGAEGLL 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
106-587 |
2.40e-85 |
|
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: 275.22 E-value: 2.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 106 PEEPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSG 183
Cdd:cd07139 10 PSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 184 KTMLDASMGEILVTLEKIQWTIKHGQRALQPSRRPGPTnffmkwYKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALF 263
Cdd:cd07139 90 MPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSG------GGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 264 TGNAIVVKCSEQVVWSSEFFVElirkCLEACDEDPDLVQLCyclpPTENDDSAnYFTSHPGFKHITFIGSQPVAHYILKC 343
Cdd:cd07139 164 AGCTVVLKPSPETPLDAYLLAE----AAEEAGLPPGVVNVV----PADREVGE-YLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 344 AAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSD 423
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDA-DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAA--LKVGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 424 IDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMM 503
Cdd:cd07139 312 LD--PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGL--DRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 504 KAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYvcQLPFGGINGSGYGKFGGEEGLLGLCN 583
Cdd:cd07139 388 PYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF--GAPFGGFKQSGIGREGGPEGLDAYLE 465
|
....
gi 6321828 584 AKSV 587
Cdd:cd07139 466 TKSI 469
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
143-587 |
1.11e-84 |
|
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: 272.18 E-value: 1.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 143 KAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQRALQPSRRPGPTN 222
Cdd:cd07134 9 AHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 223 FFmkwykG--AEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdeDPDL 300
Cdd:cd07134 89 LF-----GtkSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAF-----DEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 301 VQLCyclpptEND-DSANYFTSHPgFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMR 379
Cdd:cd07134 159 VAVF------EGDaEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETA-DLKKAAKKIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 380 GTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANplrQGSDIDHLENVDMGAMISDNRFDELEALVKDAVAKGARLL 459
Cdd:cd07134 231 GKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKF---YGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 460 QGGSRfkhpkYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVAN 539
Cdd:cd07134 308 FGGQF-----DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLA 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 6321828 540 SLQTGNVAINDFATFYV-CQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07134 383 RTSSGGVVVNDVVLHFLnPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
108-570 |
5.93e-83 |
|
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: 269.06 E-value: 5.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 108 EPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQ-STWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTm 186
Cdd:cd07082 14 SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 187 LDASMGEILVTLEKIQWTIKHGQRaLQPSRRPGPTNFFMKwYKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGN 266
Cdd:cd07082 93 LKDALKEVDRTIDYIRDTIEELKR-LDGDSLPGDWFPGTK-GKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 267 AIVVKCSEQVVWSSEFFVELIRkclEACdEDPDLVQLCYclppTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAak 346
Cdd:cd07082 171 TVVFKPATQGVLLGIPLAEAFH---DAG-FPKGVVNVVT----GRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 SLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDh 426
Cdd:cd07082 241 PMKRLVLELGGKDPAIVLPDA-DLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAK--LKVGMPWD- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 427 lENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGsrfkhpKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAK 506
Cdd:cd07082 317 -NGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321828 507 NTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFatfyvCQ-----LPFGGINGSGYG 570
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK-----CQrgpdhFPFLGRKDSGIG 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
117-585 |
1.65e-82 |
|
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: 267.29 E-value: 1.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDaSMGEILV 196
Cdd:cd07145 6 PANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ-SRVEVER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEkiqwTIKHgqrALQPSRRPGPTNFFMKWYKGAE-----IRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVK 271
Cdd:cd07145 85 TIR----LFKL---AAEEAKVLRGETIPVDAYEYNErriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 272 CSEQVVWSSEFFVELIrkcleacdEDPDLVQLCYCLPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPV 351
Cdd:cd07145 158 PSSNTPLTAIELAKIL--------EEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 352 VVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENVD 431
Cdd:cd07145 230 ALELGGSDPMIVLKDA-DLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKK--LKVGDPLD--ESTD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 432 MGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHC 511
Cdd:cd07145 305 LGPLISPEAVERMENLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321828 512 VQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAK 585
Cdd:cd07145 379 VEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
133-575 |
2.81e-82 |
|
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: 265.93 E-value: 2.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 133 DIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEILVTLEKIQ----WTIK-H 207
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILReaagLPRRpE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 208 GQraLQPSRRPGPTNFfmkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFfveLI 287
Cdd:cd07104 80 GE--ILPSDVPGKESM---------VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGL---LI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 288 RKCLEACDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSA 367
Cdd:cd07104 146 AEIFEEAGLPKGVLNVV----PGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 368 kNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTA----NPLRqgsdidhlENVDMGAMISDNRFDE 443
Cdd:cd07104 222 -DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKAlpvgDPRD--------PDTVIGPLINERQVDR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 444 LEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLG 523
Cdd:cd07104 293 VHAIVEDAVAAGARLLTGGTY-------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLS 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6321828 524 GSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGE 575
Cdd:cd07104 366 AAVFTRDLERAMAFAERLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGP 417
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
112-587 |
1.56e-81 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 266.74 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsM 191
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHA-F 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 192 GEILVTLEKIQWTIKHGQRALQPSRRPGPTNFFMKwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVK 271
Cdd:PRK09407 113 EEVLDVALTARYYARRAPKLLAPRRRAGALPVLTK----TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 272 CSEQVVWSSEFFVELirkcLEACDEDPDLVQLCYCLPPTEND---DSANYftshpgfkhITFIGSQPVAHYILKCAAKSL 348
Cdd:PRK09407 189 PDSQTPLTALAAVEL----LYEAGLPRDLWQVVTGPGPVVGTalvDNADY---------LMFTGSTATGRVLAEQAGRRL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 349 TPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDHle 428
Cdd:PRK09407 256 IGFSLELGGKNPMIVLDDA-DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRA--MRLGAGYDY-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 429 NVDMGAMISDNRFDELEALVKDAVAKGARLLQGGsrfkHPKYPQGHYF-QPTLLVDVTPEMKIAQNEVFGPILVMMKAKN 507
Cdd:PRK09407 331 SADMGSLISEAQLETVSAHVDDAVAKGATVLAGG----KARPDLGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVAD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 508 TDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIND--FATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAK 585
Cdd:PRK09407 407 VDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgyAAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQ 486
|
..
gi 6321828 586 SV 587
Cdd:PRK09407 487 TI 488
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
111-581 |
4.66e-81 |
|
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: 263.74 E-value: 4.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 111 FIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAS 190
Cdd:cd07088 14 TIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 191 MgEILVTLEKIQWTIKHGQRA---LQPSRRPGPTNFfmkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNA 267
Cdd:cd07088 94 V-EVEFTADYIDYMAEWARRIegeIIPSDRPNENIF---------IFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 268 IVVKCSEQVVWSSEFFVELIRKCleacDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS 347
Cdd:cd07088 164 IVIKPSEETPLNALEFAELVDEA----GLPAGVLNIV----TGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAEN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 348 LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhl 427
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDA-DLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKA--VKVGDPFD-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 428 ENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKN 507
Cdd:cd07088 311 AATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKR---PEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSS 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321828 508 TDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINdfatfyvcQLPFGGING--SGYGK--FGGEEGLLGL 581
Cdd:cd07088 388 LDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN--------RENFEAMQGfhAGWKKsgLGGADGKHGL 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
117-589 |
6.29e-81 |
|
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: 262.92 E-value: 6.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEILV 196
Cdd:cd07149 6 PYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR-KEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTikhgqrALQPSRRPGPTnFFMKWYKGAEIRY-----EPLGVISSIVSWNYPFhNL----LGPIIAAlftGNA 267
Cdd:cd07149 85 AIETLRLS------AEEAKRLAGET-IPFDASPGGEGRIgftirEPIGVVAAITPFNFPL-NLvahkVGPAIAA---GNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 268 IVVKCSEQVVWSSEFFVELIrkcLEACdedpdlvqlcycLPPT-------ENDDSANYFTSHPGFKHITFIGSQPVAHYI 340
Cdd:cd07149 154 VVLKPASQTPLSALKLAELL---LEAG------------LPKGalnvvtgSGETVGDALVTDPRVRMISFTGSPAVGEAI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 341 LKCAAksLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQ 420
Cdd:cd07149 219 ARKAG--LKKVTLELGSNAAVIVDADA-DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK--LVV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 421 GSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPIL 500
Cdd:cd07149 294 GDPLD--EDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 501 VMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYG----KFGGEE 576
Cdd:cd07149 365 SLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGregpRYAIEE 444
|
490
....*....|...
gi 6321828 577 gllgLCNAKSVCF 589
Cdd:cd07149 445 ----MTEIKLVCF 453
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
149-587 |
4.56e-79 |
|
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: 257.41 E-value: 4.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 149 GNSDFSRRLRVLASLHDYILNNQDLIARVACRD-SGKTMLDASMGEILVTLEKIQWTIKHGQRALQPSRRPGPtnffmKW 227
Cdd:cd07133 15 PPPSLEERRDRLDRLKALLLDNQDALAEAISADfGHRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHVG-----LL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 228 YKGA--EIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdeDPDLVQLCy 305
Cdd:cd07133 90 FLPAkaEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-----DEDEVAVV- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 306 clppTENDDSANYFTSHPgFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAKNLDALSSiIMRGTFQSS 385
Cdd:cd07133 164 ----TGGADVAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAER-IAFGKLLNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 386 GQNCIGIERVIVSKENYDDLVKILNDRMTanplRQGSDIdhLENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSrf 465
Cdd:cd07133 238 GQTCVAPDYVLVPEDKLEEFVAAAKAAVA----KMYPTL--ADNPDYTSIINERHYARLQGLLEDARAKGARVIELNP-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 466 KHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGN 545
Cdd:cd07133 310 AGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 6321828 546 VAINDfATFYVCQ--LPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07133 390 VTIND-TLLHVAQddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
117-587 |
6.75e-77 |
|
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: 252.55 E-value: 6.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTmLDASMGEILV 196
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP-IAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQRALQPSRRPGPTNFfmKWYkgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQV 276
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGF--ERY----IRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 277 VWSSEFFVELirkcLEACDEDPDLVQLCYClpptENDDSANyFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELG 356
Cdd:cd07102 156 PLCGERFAAA----FAEAGLPEGVFQVLHL----SHETSAA-LIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 357 GKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDD----LVKILNDRMTANPLRQGSDIdhlenvdm 432
Cdd:cd07102 227 GKDPAYVRPDA-DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAfveaFVAVVKGYKLGDPLDPSTTL-------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 433 GAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCV 512
Cdd:cd07102 298 GPVVSARAADFVRAQIADAIAKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321828 513 QLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN--DFATFYvcqLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07102 377 ALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcDYLDPA---LAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
115-588 |
1.37e-76 |
|
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: 251.72 E-value: 1.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LvtlekiqwtikhgqRALQPSRrpgptnFFMKWYKGAE-------------IRYEPLGVISSIVSWNYPFHNLLGPIIAA 261
Cdd:cd07093 82 P--------------RAAANFR------FFADYILQLDgesypqdggalnyVLRQPVGVAGLITPWNLPLMLLTWKIAPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 262 LFTGNAIVVKCSEqvvWSSEFFVELIRKCLEACdedpdlvqlcycLPPT-------ENDDSANYFTSHPGFKHITFIGSQ 334
Cdd:cd07093 142 LAFGNTVVLKPSE---WTPLTAWLLAELANEAG------------LPPGvvnvvhgFGPEAGAALVAHPDVDLISFTGET 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 335 PVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmt 414
Cdd:cd07093 207 ATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA-DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVER-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 415 ANPLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNE 494
Cdd:cd07093 284 AKALKVGDPLD--PDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 495 VFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINdfaTFYVCQL--PFGGINGSGYGKF 572
Cdd:cd07093 362 IFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN---CWLVRDLrtPFGGVKASGIGRE 438
|
490
....*....|....*.
gi 6321828 573 GGEEGLLGLCNAKSVC 588
Cdd:cd07093 439 GGDYSLEFYTELKNVC 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
117-578 |
3.47e-76 |
|
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: 250.71 E-value: 3.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEILV 196
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIK-----HGQraLQPSRRPGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVK 271
Cdd:cd07150 85 TPELLRAAAGecrrvRGE--TLPSDSPGTVSMSVR---------RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 272 CSEQVVWSSEFFVELIrkclEACDEDPDLVQLCYCLPPTENDDsanyFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPV 351
Cdd:cd07150 154 PSEETPVIGLKIAEIM----EEAGLPKGVFNVVTGGGAEVGDE----LVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 352 VVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENVD 431
Cdd:cd07150 226 TLELGGKNPLIVLADA-DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASK--LKVGDPRD--PDTV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 432 MGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHC 511
Cdd:cd07150 301 IGPLISPRQVERIKRQVEDAVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEA 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321828 512 VQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDfATFY-VCQLPFGGINGSGYGKFGGEEGL 578
Cdd:cd07150 374 LELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHIND-PTILdEAHVPFGGVKASGFGREGGEWSM 440
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
104-587 |
8.34e-76 |
|
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: 250.11 E-value: 8.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 104 W-NPEEPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDS 182
Cdd:cd07138 7 WvAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 183 GK----------TMLDASMGEILVTLEKIQWTIKHGqralqpsrrpgptnffmkwykGAEIRYEPLGVISSIVSWNYPFH 252
Cdd:cd07138 87 GApitlaraaqvGLGIGHLRAAADALKDFEFEERRG---------------------NSLVVREPIGVCGLITPWNWPLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 253 NLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVElirkCLEACDEDPDLVQLCYCLPPTenddSANYFTSHPGFKHITFIG 332
Cdd:cd07138 146 QIVLKVAPALAAGCTVVLKPSEVAPLSAIILAE----ILDEAGLPAGVFNLVNGDGPV----VGEALSAHPDVDMVSFTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 333 SQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILndR 412
Cdd:cd07138 218 STRAGKRVAEAAADTVKRVALELGGKSANIILDDA-DLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIA--A 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 413 MTANPLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSrfKHPK-YPQGHYFQPTLLVDVTPEMKIA 491
Cdd:cd07138 295 AAAEAYVVGDPRD--PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGP--GRPEgLERGYFVKPTVFADVTPDMTIA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 492 QNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDfaTFYVCQLPFGGINGSGYGK 571
Cdd:cd07138 371 REEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING--AAFNPGAPFGGYKQSGNGR 448
|
490
....*....|....*.
gi 6321828 572 FGGEEGLLGLCNAKSV 587
Cdd:cd07138 449 EWGRYGLEEFLEVKSI 464
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
117-570 |
2.96e-75 |
|
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: 248.70 E-value: 2.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PA-TGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEIL 195
Cdd:cd07097 21 PSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEA-RGEVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 196 VTLEKIQWTIKHGQR---ALQPSRRPGptnffmkwyKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKC 272
Cdd:cd07097 100 RAGQIFRYYAGEALRlsgETLPSTRPG---------VEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 273 SEQVVWSSEFFVELIRKCleacdedpdlvqlcyCLPP-TEN------DDSANYFTSHPGFKHITFIGSQPVAHYILKCAA 345
Cdd:cd07097 171 AELTPASAWALVEILEEA---------------GLPAgVFNlvmgsgSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 346 KSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDID 425
Cdd:cd07097 236 ARGARVQLEMGGKNPLVVLDDA-DLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKA--LKVGDALD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 426 hlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYpqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKA 505
Cdd:cd07097 313 --EGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDE--GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321828 506 KNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYG 570
Cdd:cd07097 389 RDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYG 453
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
117-587 |
2.88e-74 |
|
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: 245.75 E-value: 2.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMlDASMGEILV 196
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPV-SAMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQW-----------TIKHGQRALQPSRRpgptnffmkwykgaeiryEPLGVISSIVSWNYPFHNLLGPIIAALFTG 265
Cdd:cd07107 83 AAALLDYfaglvtelkgeTIPVGGRNLHYTLR------------------EPYGVVARIVAFNHPLMFAAAKIAAPLAAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSSEFFVELIRKCLEacdedPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAA 345
Cdd:cd07107 145 NTVVVKPPEQAPLSALRLAELAREVLP-----PGVFNIL----PGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 346 KSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRG-TFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDI 424
Cdd:cd07107 216 EGIKHVTLELGGKNALIVFPDA-DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAA--IKVGDPT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 425 DhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMK 504
Cdd:cd07107 293 D--PATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 505 AKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNA 584
Cdd:cd07107 371 WRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL-GAPFGGVKNSGIGREECLEELLSYTQE 449
|
...
gi 6321828 585 KSV 587
Cdd:cd07107 450 KNV 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
113-571 |
5.49e-74 |
|
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: 245.20 E-value: 5.49e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 113 QCHCPATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAS 190
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 191 MGEILVTLEKIQWTIK-----HGQRAlqpsrrPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNL---LGPIIAAl 262
Cdd:cd07112 85 AVDVPSAANTFRWYAEaidkvYGEVA------PTGPDAL------ALITREPLGVVGAVVPWNFPLLMAawkIAPALAA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 263 ftGNAIVVKCSEQVVWSSEFFVELirkCLEACdedpdlvqlcycLPPtenddsaNYFTSHPGFKH--------------I 328
Cdd:cd07112 152 --GNSVVLKPAEQSPLTALRLAEL---ALEAG------------LPA-------GVLNVVPGFGHtagealglhmdvdaL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 329 TFIGSQPVAHYILKCAAKS-LTPVVVELGGKDAFIVLDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVK 407
Cdd:cd07112 208 AFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 408 ILNDRMTAnpLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkHPKYPQGHYFQPTLLVDVTPE 487
Cdd:cd07112 288 KVVAAARE--WKPGDPLD--PATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKR--VLTETGGFFVEPTVFDGVTPD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 488 MKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINdfaTFYVC--QLPFGGIN 565
Cdd:cd07112 362 MRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN---CFDEGdiTTPFGGFK 438
|
....*.
gi 6321828 566 GSGYGK 571
Cdd:cd07112 439 QSGNGR 444
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
117-587 |
9.22e-74 |
|
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: 244.81 E-value: 9.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQST--WGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:cd07091 26 PATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKGDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQ----WTIK-HGQRAlqpsrrPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIV 269
Cdd:cd07091 106 ALSIKCLRyyagWADKiQGKTI------PIDGNFL------AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 270 VKCSEQVVWSSEFFVELIrkcLEAcDEDPDLVQLCYCLPPTENDDsanyFTSHPGFKHITFIGSQPVAHYILKCAAKS-L 348
Cdd:cd07091 174 LKPAEQTPLSALYLAELI---KEA-GFPPGVVNIVPGFGPTAGAA----ISSHMDVDKIAFTGSTAVGRTIMEAAAKSnL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 349 TPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTA----NPLrqgsdi 424
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDA-DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKrvvgDPF------ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 425 dhLENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMK 504
Cdd:cd07091 319 --DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGS----KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 505 AKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNA 584
Cdd:cd07091 393 FKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDA-AVPFGGFKQSGFGRELGEEGLEEYTQV 471
|
...
gi 6321828 585 KSV 587
Cdd:cd07091 472 KAV 474
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
117-575 |
1.18e-73 |
|
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: 244.14 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEI-- 194
Cdd:cd07151 17 PYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKA-NIEWga 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 --LVTLEKIQWTIKHGQRALqPSRRPGPTNffmkwykgaEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKC 272
Cdd:cd07151 96 amAITREAATFPLRMEGRIL-PSDVPGKEN---------RVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 273 SEQVVWSSEFfveLIRKCLEACDedpdlvqlcycLPP-------TENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAA 345
Cdd:cd07151 166 ASDTPITGGL---LLAKIFEEAG-----------LPKgvlnvvvGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 346 KSLTPVVVELGGKDAFIVLDSAKNLDALSSIIMrGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLRQGSDID 425
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVF-GKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 426 HLenvdMGAMISDNRFDELEALVKDAVAKGARLLQGGSrfkhpkyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKA 505
Cdd:cd07151 311 TV----VGPLINESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 506 KNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGE 575
Cdd:cd07151 380 DDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGE 449
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
115-570 |
7.79e-73 |
|
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: 242.42 E-value: 7.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEI 194
Cdd:cd07085 21 YNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADA-RGDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWTIkhgqralqpsrrpGPTNFFMKWY-----KG--AEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNA 267
Cdd:cd07085 100 LRGLEVVEFAC-------------SIPHLLKGEYlenvaRGidTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 268 IVVKCSEQVVWSSEFFVELirkCLEAcdEDPD-LVQLCYClppteNDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAK 346
Cdd:cd07085 167 FVLKPSERVPGAAMRLAEL---LQEA--GLPDgVLNVVHG-----GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 SLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLRQGSDidh 426
Cdd:cd07085 237 NGKRVQALGGAKNHAVVMPDA-DLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 427 lENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAK 506
Cdd:cd07085 313 -PGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVD 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321828 507 NTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN-----DFATFyvcqlPFGGINGSGYG 570
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipvPLAFF-----SFGGWKGSFFG 455
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
117-587 |
9.62e-73 |
|
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: 241.46 E-value: 9.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILV 196
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWtIKHGQRALQPSRR----PGPTNFfmkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKC 272
Cdd:cd07092 84 AVDNFRF-FAGAARTLEGPAAgeylPGHTSM---------IRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 273 SEQVVWSSEFFVELIRKCLeacdedPDLVQLCYClppTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVV 352
Cdd:cd07092 154 SETTPLTTLLLAELAAEVL------PPGVVNVVC---GGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 353 VELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENVDM 432
Cdd:cd07092 225 LELGGKAPVIVFDDA-DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSA--IRVGDPDD--EDTEM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 433 GAMISDNRFDELEALVkDAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCV 512
Cdd:cd07092 300 GPLNSAAQRERVAGFV-ERAPAHARVLTGGRRAEGP----GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAI 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321828 513 QLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATfYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07092 375 ELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP-LAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
133-578 |
1.23e-72 |
|
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: 240.56 E-value: 1.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 133 DIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMgEILVTLEKIQWTIKHGQRA- 211
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLITQIi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 212 --LQPSRRPGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFhnLLG--PIIAALFTGNAIVVKCSEQVVWSSEFFVEli 287
Cdd:cd07105 80 ggSIPSDKPGTLAMVVK---------EPVGVVLGIAPWNAPV--ILGtrAIAYPLAAGNTVVLKASELSPRTHWLIGR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 288 rkCLEACDEDPDLVQLCYCLPptenDDSA---NYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVL 364
Cdd:cd07105 147 --VFHEAGLPKGVLNVVTHSP----EDAPevvEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 365 DSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSdidhlenVDMGAMISDNRFDEL 444
Cdd:cd07105 221 EDA-DLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAA--AEKLFAGP-------VVLGSLVSAAAADRV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 445 EALVKDAVAKGARLLQGGSRFKHPKypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGG 524
Cdd:cd07105 291 KELVDDALSKGAKLVVGGLADESPS---GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321828 525 SVFGADIKECNYVANSLQTGNVAIN-----DFAtfyvcQLPFGGINGSGYGKFGGEEGL 578
Cdd:cd07105 368 AVFTRDLARALAVAKRIESGAVHINgmtvhDEP-----TLPHGGVKSSGYGRFNGKWGI 421
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
117-591 |
1.48e-72 |
|
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: 241.05 E-value: 1.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMgEILV 196
Cdd:cd07090 4 PATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV-DIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQrALQPSRRPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQV 276
Cdd:cd07090 83 SADCLEYYAGLAP-TLSGEHVPLPGGSF------AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 277 VWSSEFFVELIRkclEACdedpdlvqlcycLPP------TENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTP 350
Cdd:cd07090 156 PLTALLLAEILT---EAG------------LPDgvfnvvQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 VVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMtaNPLRQGSDidHLENV 430
Cdd:cd07090 221 VTLELGGKSPLIIFDDA-DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERT--KKIRIGDP--LDEDT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 431 DMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFK-HPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTD 509
Cdd:cd07090 296 QMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 510 HCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNAKSVCF 589
Cdd:cd07090 376 EVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPV-EVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
..
gi 6321828 590 DT 591
Cdd:cd07090 455 EM 456
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
152-588 |
2.22e-72 |
|
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: 239.74 E-value: 2.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 152 DFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQRALQPSRRPGPtnfFMKWYKGA 231
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRVSVP---LLLQPAKA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 232 EIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdeDPDLVQLCyclpptE 311
Cdd:cd07087 95 YVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYF-----DPEAVAVV------E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 312 ND-DSANYFTSHPgFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCI 390
Cdd:cd07087 164 GGvEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDA-NLEVAARRIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 391 GIERVIVSKENYDDLVKILNDRMTA----NPLRQGsdidhlenvDMGAMISDNRFDELEALVKDAvakgaRLLQGGSRfk 466
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKAIKEfygeDPKESP---------DYGRIINERHFDRLASLLDDG-----KVVIGGQV-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 467 hpkYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNV 546
Cdd:cd07087 306 ---DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 6321828 547 AINDFATFYVCQ-LPFGGINGSGYGKFGGEEGLLGLCNAKSVC 588
Cdd:cd07087 383 CVNDVLLHAAIPnLPFGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
117-587 |
2.22e-72 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 240.80 E-value: 2.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTmLDASMGEILV 196
Cdd:PRK09406 8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQRALQPSrrpgPTNFFMKWYKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQV 276
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADE----PADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 277 VWSSEFFVELIRK------CLEACdedpdLVqlcyclppteNDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTP 350
Cdd:PRK09406 163 PQTALYLADLFRRagfpdgCFQTL-----LV----------GSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 VVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENV 430
Cdd:PRK09406 228 TVLELGGSDPFIVMPSA-DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAA--LRVGDPTD--PDT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 431 DMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDH 510
Cdd:PRK09406 303 DVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGP----GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDE 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321828 511 CVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:PRK09406 379 AIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYP-ELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
117-578 |
6.70e-72 |
|
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: 239.18 E-value: 6.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAS--MGEI 194
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQwTIKHGQRALQPSRRPGPTNFFmkwykGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSE 274
Cdd:cd07110 84 AGCFEYYA-DLAEQLDAKAERAVPLPSEDF-----KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QvvwSSEFFVELIRKCLEACdedpdlvqlcycLPPT-------ENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS 347
Cdd:cd07110 158 L---TSLTELELAEIAAEAG------------LPPGvlnvvtgTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 348 LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTA----NPLRqgsd 423
Cdd:cd07110 223 IKPVSLELGGKSPIIVFDDA-DLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAirvgDPLE---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 424 idhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMM 503
Cdd:cd07110 298 ----EGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRRPAHLE--KGYFIAPTVFADVPTDSRIWREEIFGPVLCVR 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321828 504 KAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN-DFATFyvCQLPFGGINGSGYGKFGGEEGL 578
Cdd:cd07110 372 SFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINcSQPCF--PQAPWGGYKRSGIGRELGEWGL 445
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
117-588 |
9.04e-72 |
|
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: 238.88 E-value: 9.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILV 196
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQ----WTIKHGQRALqPSRRPgptnfFMKWykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKC 272
Cdd:cd07115 84 AADTFRyyagWADKIEGEVI-PVRGP-----FLNY-----TVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 273 SEQVVWSSEFFVELirkCLEAcdEDPDLVqlcYCLPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVV 352
Cdd:cd07115 153 AELTPLSALRIAEL---MAEA--GFPAGV---LNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 353 VELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSDIDhlENVDM 432
Cdd:cd07115 225 LELGGKSANIVFADA-DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSL--ARSLRPGDPLD--PKTQM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 433 GAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCV 512
Cdd:cd07115 300 GPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGAR----GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEAL 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321828 513 QLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNAKSVC 588
Cdd:cd07115 376 RIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDP-GSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
115-587 |
4.00e-71 |
|
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: 237.24 E-value: 4.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTmLDASMG 192
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKP-ISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 193 EILVTLEkiQWTIKHGQ-RAL--QPSRRPGPTNFFMkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIV 269
Cdd:cd07118 81 EIEGAAD--LWRYAASLaRTLhgDSYNNLGDDMLGL-------VLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 270 VKCSEqvvWSSEFFVELIRKCLEAcdEDPDLVqlcYCLPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLT 349
Cdd:cd07118 152 VKPSE---FTSGTTLMLAELLIEA--GLPAGV---VNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 350 PVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMtaNPLRQGSDIDhlEN 429
Cdd:cd07118 224 KVSLELGGKNPQIVFADA-DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARS--RKVRVGDPLD--PE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 430 VDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTD 509
Cdd:cd07118 299 TKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAA---GLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVD 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321828 510 HCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07118 376 EAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP-ELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
117-587 |
6.26e-70 |
|
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: 234.93 E-value: 6.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA---QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGE 193
Cdd:cd07141 29 PATGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 194 ILVTLEKIQ----WTIK-HGQRAlqpsrrPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAI 268
Cdd:cd07141 109 LPGAIKVLRyyagWADKiHGKTI------PMDGDFF------TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 269 VVKCSEQVVWSSEFFVELIRkclEAcDEDPDLVQLCYCLPPTenddSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS- 347
Cdd:cd07141 177 VLKPAEQTPLTALYLASLIK---EA-GFPPGVVNVVPGYGPT----AGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSn 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 348 LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVK----ILNDRMTANPLRQGsd 423
Cdd:cd07141 249 LKRVTLELGGKSPNIVFADA-DLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKrsveRAKKRVVGNPFDPK-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 424 idhlenVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMM 503
Cdd:cd07141 326 ------TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDK----GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 504 KAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYvCQLPFGGINGSGYGKFGGEEGLLGLCN 583
Cdd:cd07141 396 KFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTE 474
|
....
gi 6321828 584 AKSV 587
Cdd:cd07141 475 VKTV 478
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
117-578 |
7.70e-70 |
|
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: 234.51 E-value: 7.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAS--MG 192
Cdd:cd07119 20 PANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEidID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 193 EILVTLEKiqwtikHGQRALQPSRR--PGPTNFFMKwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVV 270
Cdd:cd07119 100 DVANCFRY------YAGLATKETGEvyDVPPHVISR------TVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 271 KCSEQVVWSSEFFVELIrkclEACDEDPDLVQLCYCLPPTENDDsanyFTSHPGFKHITFIGSQPVAHYILKCAAKSLTP 350
Cdd:cd07119 168 KPSEVTPLTTIALFELI----EEAGLPAGVVNLVTGSGATVGAE----LAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 VVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSDIDhlENV 430
Cdd:cd07119 240 VALELGGKNPNIVFADA-DFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAER--AKKIKLGNGLD--ADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 431 DMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDH 510
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321828 511 CVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGL 578
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFA-EAPWGGYKQSGIGRELGPTGL 461
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
117-579 |
1.45e-69 |
|
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: 233.02 E-value: 1.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILV 196
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQW-----------TIKHGQRALQPSRRpgptnffmkwykgaeiryEPLGVISSIVSWNYPFHNLLGPIIAALFTG 265
Cdd:cd07108 84 LADLFRYfgglagelkgeTLPFGPDVLTYTVR------------------EPLGVVGAILPWNAPLMLAALKIAPALVAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSseffvelIRKCLEACDED-PDLVQLCYClppTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCA 344
Cdd:cd07108 146 NTVVLKAAEDAPLA-------VLLLAEILAQVlPAGVLNVIT---GYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 345 AKSLTPVVVELGGKDAFIVLDSAKNLDALSSII--MRGTFQssGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGS 422
Cdd:cd07108 216 ADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIagMRFTRQ--GQSCTAGSRLFVHEDIYDAFLEKLVAKLSK--LKIGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 423 DIDhlENVDMGAMISDNRFDELEALVKDAVA-KGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILV 501
Cdd:cd07108 292 PLD--EATDIGAIISEKQFAKVCGYIDLGLStSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 502 MMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATfyvcQLP---FGGINGSGYGKFGGEEGL 578
Cdd:cd07108 370 AIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGG----QQPgqsYGGFKQSGLGREASLEGM 445
|
.
gi 6321828 579 L 579
Cdd:cd07108 446 L 446
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
112-589 |
2.37e-69 |
|
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: 232.71 E-value: 2.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsM 191
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 192 GEILVTLEKIQwtikhgqRALQPSRRPGPTNFFMKWYKGAEIRY-----EPLGVISSIVSWNYPFhNL----LGPIIAal 262
Cdd:cd07094 80 VEVDRAIDTLR-------LAAEEAERIRGEEIPLDATQGSDNRLawtirEPVGVVLAITPFNFPL-NLvahkLAPAIA-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 263 fTGNAIVVKCSEQVVWSSEFFVELIRkcleacdeDPDLVQLCYCLPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILK 342
Cdd:cd07094 150 -TGCPVVLKPASKTPLSALELAKILV--------EAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 343 CAAKslTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGS 422
Cdd:cd07094 221 NAGG--KRIALELGGNAPVIVDRDA-DLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAA--VKKLKVGD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 423 DIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVM 502
Cdd:cd07094 296 PLD--EDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 503 MKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFGGEEGLLGLC 582
Cdd:cd07094 367 IRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMT 446
|
....*..
gi 6321828 583 NAKSVCF 589
Cdd:cd07094 447 EEKTVVI 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
115-573 |
2.86e-69 |
|
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: 232.14 E-value: 2.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 115 HCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEI 194
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWtikhgqrALQPSRRPGPTNFFMKWYKGAE-----IRYEPLGVISSIVSWNYPFhNL----LGPIIAAlftG 265
Cdd:cd07147 83 ARAIDTFRI-------AAEEATRIYGEVLPLDISARGEgrqglVRRFPIGPVSAITPFNFPL-NLvahkVAPAIAA---G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSSEFFVELIRKCleacdedpDLVQLCYCLPPTENDDsANYFTSHPGFKHITFIGSQPVAHYILKCAA 345
Cdd:cd07147 152 CPFVLKPASRTPLSALILGEVLAET--------GLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 346 KSltPVVVELGGKDAFIVlDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSDID 425
Cdd:cd07147 223 KK--KVVLELGGNAAVIV-DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVAR--VKALKTGDPKD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 426 hlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKA 505
Cdd:cd07147 298 --DATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPY 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321828 506 KNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFG 573
Cdd:cd07147 369 DDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREG 436
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
108-587 |
4.38e-69 |
|
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: 232.80 E-value: 4.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 108 EPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKA-QSTWG-NSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKT 185
Cdd:cd07143 20 HGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 186 MLDASMGEILVTLEKIQ----WTIK-HGQRALQPSRRPGPTnffmkwykgaeiRYEPLGVISSIVSWNYPFHNLLGPIIA 260
Cdd:cd07143 100 FGTAKRVDVQASADTFRyyggWADKiHGQVIETDIKKLTYT------------RHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 261 ALFTGNAIVVKCSEQVVWSSEFFVELIRKCleacdedpdlvqlcyCLPPT-------ENDDSANYFTSHPGFKHITFIGS 333
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEA---------------GFPPGvinvvsgYGRTCGNAISSHMDIDKVAFTGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 334 QPVAHYILKCAAKS-LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDR 412
Cdd:cd07143 233 TLVGRKVMEAAAKSnLKKVTLELGGKSPNIVFDDA-DLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 413 mtANPLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHpkypQGHYFQPTLLVDVTPEMKIAQ 492
Cdd:cd07143 312 --AKKLKVGDPFA--EDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGN----EGYFIEPTIFTDVTEDMKIVK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 493 NEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKF 572
Cdd:cd07143 384 EEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHH-QVPFGGYKQSGIGRE 462
|
490
....*....|....*
gi 6321828 573 GGEEGLLGLCNAKSV 587
Cdd:cd07143 463 LGEYALENYTQIKAV 477
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
117-571 |
6.48e-69 |
|
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: 231.96 E-value: 6.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILV 196
Cdd:cd07117 23 PANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQW---TIKHGQralqpsrrpGPTNFFMKWYKGAeIRYEPLGVISSIVSWNYPFhnLLG-----PIIAAlftGNAI 268
Cdd:cd07117 103 AADHFRYfagVIRAEE---------GSANMIDEDTLSI-VLREPIGVVGQIIPWNFPF--LMAawklaPALAA---GNTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 269 VVKCSEQVVWSSEFFVELIRKCLEAcdedpDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSL 348
Cdd:cd07117 168 VIKPSSTTSLSLLELAKIIQDVLPK-----GVVNIV----TGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 349 TPVVVELGGKDAFIVLDSAkNLD-ALSSIIMrGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhl 427
Cdd:cd07117 239 IPATLELGGKSANIIFDDA-NWDkALEGAQL-GILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFEN--VKVGNPLD-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 428 ENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKN 507
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321828 508 TDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFyVCQLPFGGINGSGYGK 571
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQI-PAGAPFGGYKKSGIGR 455
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
84-579 |
2.35e-68 |
|
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: 230.75 E-value: 2.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 84 PAPEAAQ--NNW--KGKRSVSTNI---W-NPEEPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSR 155
Cdd:cd07111 3 PAPESAAcaLAWldAHDRSFGHFIngkWvKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 156 RLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI-LVtlekIQWTIKH-GQRALQPSRRPGptnffmkwykgaei 233
Cdd:cd07111 83 RARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIpLV----ARHFYHHaGWAQLLDTELAG-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 234 rYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELirkCLEACdedpdlvqlcycLPP---- 309
Cdd:cd07111 145 -WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEI---CAEAG------------LPPgvln 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 310 --TENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQ 387
Cdd:cd07111 209 ivTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDA-DLDSAVEGIVDAIWFNQGQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 388 NCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSrfkh 467
Cdd:cd07111 288 VCCAGSRLLVQESVAEELIRKLKERMSH--LRVGDPLD--KAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGA---- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 468 PKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVA 547
Cdd:cd07111 360 DLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVW 439
|
490 500 510
....*....|....*....|....*....|..
gi 6321828 548 INDFATFYVCqLPFGGINGSGYGKFGGEEGLL 579
Cdd:cd07111 440 INGHNLFDAA-AGFGGYRESGFGREGGKEGLY 470
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
112-589 |
5.18e-67 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 227.65 E-value: 5.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsM 191
Cdd:PLN02278 42 FPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA-I 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 192 GEILVTLEKIQWTIKHGQRA---LQPSRRPGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAI 268
Cdd:PLN02278 121 GEVAYGASFLEYFAEEAKRVygdIIPSPFPDRRLLVLK---------QPVGVVGAITPWNFPLAMITRKVGPALAAGCTV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 269 VVKCSEQVVWSSEFFVELirkCLEAcDEDPDLVQLCYCLPPTENDDsanyFTSHPGFKHITFIGSQPVAHYILKCAAKSL 348
Cdd:PLN02278 192 VVKPSELTPLTALAAAEL---ALQA-GIPPGVLNVVMGDAPEIGDA----LLASPKVRKITFTGSTAVGKKLMAGAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 349 TPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlE 428
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDA-DLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQK--LVVGDGFE--E 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 429 NVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKhpkyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNT 508
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 509 DHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDfATFYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSVC 588
Cdd:PLN02278 415 EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNE-GLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVC 493
|
.
gi 6321828 589 F 589
Cdd:PLN02278 494 L 494
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
117-587 |
5.11e-66 |
|
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: 224.59 E-value: 5.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA-QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEIL 195
Cdd:cd07144 30 PSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSNALGDLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 196 VTLEKIQ----WTIK-HGQRAlqpsrrpgPTNFfmkwYKGAEIRYEPLGVISSIVSWNYPFHNL---LGPIIAAlftGNA 267
Cdd:cd07144 110 EIIAVIRyyagWADKiQGKTI--------PTSP----NKLAYTLHEPYGVCGQIIPWNYPLAMAawkLAPALAA---GNT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 268 IVVKCSEQVVWSSEFFVELIRkclEAcDEDPDLVQLCYCLPPTenddSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS 347
Cdd:cd07144 175 VVIKPAENTPLSLLYFANLVK---EA-GFPPGVVNIIPGYGAV----AGSALAEHPDVDKIAFTGSTATGRLVMKAAAQN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 348 LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANpLRQGSDIDhl 427
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDA-DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQN-YKVGSPFD-- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 428 ENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSrFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKN 507
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGE-KAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 508 TDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN-----DFatfyvcQLPFGGINGSGYGKFGGEEGLLGLC 582
Cdd:cd07144 402 YEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINssndsDV------GVPFGGFKMSGIGRELGEYGLETYT 475
|
....*
gi 6321828 583 NAKSV 587
Cdd:cd07144 476 QTKAV 480
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
130-577 |
8.00e-66 |
|
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: 222.48 E-value: 8.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 130 TEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQ 209
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 210 RALQPSRRPGPTNFFMKWykGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRK 289
Cdd:cd07135 83 KWAKDEKVKDGPLAFMFG--KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 290 CLeacdeDPDLVQLCYCLPPtenddSANYFTSHpGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkN 369
Cdd:cd07135 161 YL-----DPDAFQVVQGGVP-----ETTALLEQ-KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNA-D 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 370 LDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILN---DRMTANplrqgsdiDHLENVDMGAMISDNRFDELEA 446
Cdd:cd07135 229 LELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKkvlDEFYPG--------GANASPDYTRIVNPRHFNRLKS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 447 LVKDavAKGaRLLQGGSRFKHPKypqghYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSV 526
Cdd:cd07135 301 LLDT--TKG-KVVIGGEMDEATR-----FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYI 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6321828 527 FGADIKECNYVANSLQTGNVAIND-FATFYVCQLPFGGINGSGYGKFGGEEG 577
Cdd:cd07135 373 FTDDKSEIDHILTRTRSGGVVINDtLIHVGVDNAPFGGVGDSGYGAYHGKYG 424
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
117-571 |
2.29e-65 |
|
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: 222.60 E-value: 2.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsmgeilv 196
Cdd:cd07559 23 PVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRET------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQ------RALQPSRRPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFhnL-----LGPIIAAlftG 265
Cdd:cd07559 96 LAADIPLAIDHFRyfagviRAQEGSLSEIDEDTL------SYHFHEPLGVVGQIIPWNFPL--LmaawkLAPALAA---G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSSEFFVELIRKCLEacdedPDLVQLCYCLPPTenddSANYFTSHPGFKHITFIGSQPVAHYILKCAA 345
Cdd:cd07559 165 NTVVLKPASQTPLSILVLMELIGDLLP-----KGVVNVVTGFGSE----AGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 346 KSLTPVVVELGGKDAFIVLDSAKN-----LDALSSIIMRGTFqSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQ 420
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAMDadddfDDKAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEA--IKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 421 GSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPIL 500
Cdd:cd07559 313 GNPLD--PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321828 501 VMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATfYVCQLPFGGINGSGYGK 571
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQ-YPAHAPFGGYKKSGIGR 460
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
117-570 |
6.14e-65 |
|
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: 221.45 E-value: 6.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATG-QYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTmLDASMGEIL 195
Cdd:cd07131 21 PADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKP-LAEGRGDVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 196 VTLEKIQWTIKHGQR---ALQPSRRPGptnffmkwyKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKC 272
Cdd:cd07131 100 EAIDMAQYAAGEGRRlfgETVPSELPN---------KDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 273 SEQVVWSSEFFVElirkCLEACDEDPDLVQLC--YClpptenDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTP 350
Cdd:cd07131 171 AEDTPACALKLVE----LFAEAGLPPGVVNVVhgRG------EEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 VVVELGGKDAFIVLDSAkNLD-ALSSIIMrGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSDIDhlEN 429
Cdd:cd07131 241 VALEMGGKNPIIVMDDA-DLDlALEGALW-SAFGTTGQRCTATSRLIVHESVYDEFLKRFVER--AKRLRVGDGLD--EE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 430 VDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTD 509
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321828 510 HCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYG 570
Cdd:cd07131 395 EAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNG 455
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
132-640 |
3.46e-64 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 219.90 E-value: 3.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 132 ADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQRA 211
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 212 LQPsrRPGPTNFFMKWYKGaEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCL 291
Cdd:PTZ00381 87 LKP--EKVDTVGVFGPGKS-YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 292 eacdeDPDLVQLCyclpptENDDS-ANYFTSHPgFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVlDSAKNL 370
Cdd:PTZ00381 164 -----DPSYVRVI------EGGVEvTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIV-DKSCNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 371 DALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTA----NPLRQGsdidhlenvDMGAMISDNRFDELEA 446
Cdd:PTZ00381 231 KVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEffgeDPKKSE---------DYSRIVNEFHTKRLAE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 447 LVKDavaKGARLLQGGSRFKHPKYpqghyFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSV 526
Cdd:PTZ00381 302 LIKD---HGGKVVYGGEVDIENKY-----VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 527 FGADIKECNYVANSLQTGNVAINDfATFYVC--QLPFGGINGSGYGKFGGEEGLLGLCNAKSVCFDTLPFVStqiPKPLD 604
Cdd:PTZ00381 374 FGEDKRHKELVLENTSSGAVVIND-CVFHLLnpNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSF---DLSLR 449
|
490 500 510
....*....|....*....|....*....|....*.
gi 6321828 605 YPIRNNAKAWNFVKSFIVGAYTNSTWQRiKSLFSLA 640
Cdd:PTZ00381 450 YPPYTSFKSWVLSFLLKLSIPVQSEVLK-SRLFVSA 484
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
117-588 |
5.69e-64 |
|
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: 219.79 E-value: 5.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PA-TGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDyILNNQ--DLIARVAcRDSGKTMLDASmGE 193
Cdd:cd07124 53 PAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAA-LLRRRrfELAAWMV-LEVGKNWAEAD-AD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 194 ILVTLEKIQWTIKHgQRALQPSR---RPGPTNffmkwykgaEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVV 270
Cdd:cd07124 130 VAEAIDFLEYYARE-MLRLRGFPvemVPGEDN---------RYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 271 KCSEQVVWSSEFFVELIRkclEAcDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS--- 347
Cdd:cd07124 200 KPAEDTPVIAAKLVEILE---EA-GLPPGVVNFL----PGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 348 ---LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGsDI 424
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDA-DLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVER--TKALKVG-DP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 425 DHLEnVDMGAMISDNRFDELEALVKDAVaKGARLLQGGSRFKHPKypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMK 504
Cdd:cd07124 348 EDPE-VYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELAA--EGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 505 AKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQL-PFGGINGSGYG-KFGGEEGLLGLC 582
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMSGTGsKAGGPDYLLQFM 503
|
....*.
gi 6321828 583 NAKSVC 588
Cdd:cd07124 504 QPKTVT 509
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
117-571 |
1.62e-63 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 217.47 E-value: 1.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILV 196
Cdd:PRK13473 24 PATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEIPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQW-----TIKHGQRALQPSrrPGPTNFfmkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVK 271
Cdd:PRK13473 104 IVDVFRFfagaaRCLEGKAAGEYL--EGHTSM---------IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 272 CSEQVVWSSEFFVELIRKCLeacdedPDLVQLCYClppTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPV 351
Cdd:PRK13473 173 PSEITPLTALKLAELAADIL------PPGVLNVVT---GRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 352 VVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENVD 431
Cdd:PRK13473 244 HLELGGKAPVIVFDDA-DLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT--LKVGDPDD--EDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 432 MGAMISDNRFDELEALVKDAVAKG-ARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDH 510
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGK----GYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321828 511 CVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATfYVCQLPFGGINGSGYGK 571
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM-LVSEMPHGGQKQSGYGK 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
117-588 |
1.19e-62 |
|
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: 214.51 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWgNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTmLDASMGEI 194
Cdd:cd07120 4 PATGEVIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKI-LGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQW---TIKH--GqRALQPsrRPGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIV 269
Cdd:cd07120 82 SGAISELRYyagLARTeaG-RMIEP--EPGSFSLVLR---------EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 270 VKCSEQvvwSSEFFVELIRkCLEACDEDPD-LVQLCyclppTEN-DDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS 347
Cdd:cd07120 150 VKPAGQ---TAQINAAIIR-ILAEIPSLPAgVVNLF-----TESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 348 LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLRQGSDidhl 427
Cdd:cd07120 221 LKRLGLELGGKTPCIVFDDA-DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLD---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 428 ENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHpKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKN 507
Cdd:cd07120 296 PASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTE-GLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 508 TDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07120 375 EAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFA-EAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
.
gi 6321828 588 C 588
Cdd:cd07120 454 Y 454
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-587 |
9.76e-62 |
|
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: 211.98 E-value: 9.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 152 DFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQRALQPSRRPGP-TNFFMKWYkg 230
Cdd:cd07136 18 DVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRVKTPlLNFPSKSY-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 231 aeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdeDPDLVqlcYCLppt 310
Cdd:cd07136 96 --IYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETF-----DEEYV---AVV--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 311 END-DSANYFTSHPgFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNC 389
Cdd:cd07136 163 EGGvEENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDA-NLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 390 IGIERVIVSKENYDDLVKILNDRMTAnplRQGSDIdhLENVDMGAMISDNRFDELEALVKDAvakgaRLLQGGsrfkhpK 469
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKK---FYGEDP--LESPDYGRIINEKHFDRLAGLLDNG-----KIVFGG------N 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 470 Y-PQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAI 548
Cdd:cd07136 305 TdRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 6321828 549 ND----FATFYvcqLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:cd07136 385 NDtimhLANPY---LPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
120-574 |
2.49e-60 |
|
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: 207.92 E-value: 2.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 120 GQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEILVTLE 199
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAG-FEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 200 KIQW-----TIKHGQraLQPSRrPGPTNFfmkwykgaeIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSE 274
Cdd:cd07152 80 ELHEaaglpTQPQGE--ILPSA-PGRLSL---------ARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QVVWSSEFfveLIRKCLEACDEDPDLVQLcycLPPTENDDSAnyFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVE 354
Cdd:cd07152 148 RTPVSGGV---VIARLFEEAGLPAGVLHV---LPGGADAGEA--LVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 355 LGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSDIDhlENVDMGA 434
Cdd:cd07152 220 LGGKNALIVLDDA-DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAK--AKHLPVGDPAT--GQVALGP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 435 MISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQL 514
Cdd:cd07152 295 LINARQLDRVHAIVDDSVAAGARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVAL 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321828 515 ANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYG-KFGG 574
Cdd:cd07152 368 ANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGGMGASGNGsRFGG 428
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
117-588 |
6.30e-60 |
|
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: 208.06 E-value: 6.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA-QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEIL 195
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 196 VTLEKIQ----WTIKHGQRALQPSRrPGPtnffmkwykgAEIRY------EPLGVISSIVSWNYPFHNLLGPIIAALFTG 265
Cdd:cd07113 102 QSANFLRyfagWATKINGETLAPSI-PSM----------QGERYtaftrrEPVGVVAGIVPWNFSVMIAVWKIGAALATG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSSEFFVELIRkclEACdedpdlvqlcycLPP------TENDDSANYFTSHPGFKHITFIGSQPVAHY 339
Cdd:cd07113 171 CTIVIKPSEFTPLTLLRVAELAK---EAG------------IPDgvlnvvNGKGAVGAQLISHPDVAKVSFTGSVATGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 340 ILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLR 419
Cdd:cd07113 236 IGRQAASDLTRVTLELGGKNAAAFLKDA-DIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSS--FQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 420 QGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPI 499
Cdd:cd07113 313 VGSPMD--ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE----GYFVQPTLVLARSADSRLMREETFGPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 500 LVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINdFATFYVCQLPFGGINGSGYGKFGGEEGLL 579
Cdd:cd07113 387 VSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN-MHTFLDPAVPFGGMKQSGIGREFGSAFID 465
|
....*....
gi 6321828 580 GLCNAKSVC 588
Cdd:cd07113 466 DYTELKSVM 474
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
112-587 |
1.12e-59 |
|
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: 206.44 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDfsrRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsM 191
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAASYRSTLTRYQ---RSAILNKAAALLEARREEFARLITLESGLCLKDT-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 192 GEILVTLEKIQWTIKHGQRaLQPSRRPGPTNFFMKWYKGAEIRyEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVK 271
Cdd:cd07146 77 YEVGRAADVLRFAAAEALR-DDGESFSCDLTANGKARKIFTLR-EPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 272 CSEQVVWSSEFFVELIRKCLEAcdedPDLVQLCYCLPptenDDSANYFTSHPGFKHITFIGSQPVAHYILKCAA-KSLtp 350
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLP----PDMLSVVTGEP----GEIGDELITHPDVDLVTFTGGVAVGKAIAATAGyKRQ-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 vVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhlENV 430
Cdd:cd07146 225 -LLELGGNDPLIVMDDA-DLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAA--LVVGDPMD--PAT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 431 DMGAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDH 510
Cdd:cd07146 299 DMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDE 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321828 511 CVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYG-KFGGEEGLLGLCNAKSV 587
Cdd:cd07146 372 AIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
117-587 |
1.14e-57 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 201.63 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEILV 196
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQRALQPSrrpgPTnffMKWYKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQV 276
Cdd:PRK13968 93 SANLCDWYAEHGPAMLKAE----PT---LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 277 VWSSEFFVELIrkcleacdEDPDLVQLCYCLPPTENDdSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELG 356
Cdd:PRK13968 166 MGCAQLIAQVF--------KDAGIPQGVYGWLNADND-GVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 357 GKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSkenyDDLVKILNDRMTA--NPLRQGSDIDhlENVDMGA 434
Cdd:PRK13968 237 GSDPFIVLNDA-DLELAVKAAVAGRYQNTGQVCAAAKRFIIE----EGIASAFTERFVAaaAALKMGDPRD--EENALGP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 435 MISDNRFDELEALVKDAVAKGARLLQGGSRFKHpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQL 514
Cdd:PRK13968 310 MARFDLRDELHHQVEATLAEGARLLLGGEKIAG----AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALEL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321828 515 ANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATfYVCQLPFGGINGSGYGKFGGEEGLLGLCNAKSV 587
Cdd:PRK13968 386 ANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCA-SDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
117-578 |
5.90e-56 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 198.03 E-value: 5.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSR-----RLRVLASLHDYILNNQDLIARVACRDSGKTMLDAS- 190
Cdd:PLN02467 30 PATEETIGDIPAATAEDVDAAVEAARKAFKRNKGKDWARttgavRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAw 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 191 -MGEILVTLEKIQwtikhGQRALQPSRRPGPTNFFMKWYKGaEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIV 269
Cdd:PLN02467 110 dMDDVAGCFEYYA-----DLAEALDAKQKAPVSLPMETFKG-YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 270 VKCSEqvvWSSEFFVELIRKCLEACdedpdlvqlcycLPPT-------ENDDSANYFTSHPGFKHITFIGSQPVAHYILK 342
Cdd:PLN02467 184 LKPSE---LASVTCLELADICREVG------------LPPGvlnvvtgLGTEAGAPLASHPGVDKIAFTGSTATGRKIMT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 343 CAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIV----SKENYDDLVKILNDRMTANPL 418
Cdd:PLN02467 249 AAAQMVKPVSLELGGKSPIIVFDDV-DLDKAVEWAMFGCFWTNGQICSATSRLLVheriASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 419 RQGsdidhlenVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKypQGHYFQPTLLVDVTPEMKIAQNEVFGP 498
Cdd:PLN02467 328 EEG--------CRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLK--KGFFIEPTIITDVTTSMQIWREEVFGP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 499 ILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN-DFATFyvCQLPFGGINGSGYGKFGGEEG 577
Cdd:PLN02467 398 VLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINcSQPCF--CQAPWGGIKRSGFGRELGEWG 475
|
.
gi 6321828 578 L 578
Cdd:PLN02467 476 L 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
117-587 |
7.18e-56 |
|
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: 196.95 E-value: 7.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:cd07142 26 PRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARYAEV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQ----WTIK-HGQRAlqpsrrPGPTNFFmkwykgAEIRYEPLGVISSIVSWNYPFHNL---LGPIIAAlftGN 266
Cdd:cd07142 106 PLAARLFRyyagWADKiHGMTL------PADGPHH------VYTLHEPIGVVGQIIPWNFPLLMFawkVGPALAC---GN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 267 AIVVKCSEQVVWSSEFFVELIrkcLEAcDEDPDLVQLCYCLPPTenddSANYFTSHPGFKHITFIGSQPVAHYILKCAAK 346
Cdd:cd07142 171 TIVLKPAEQTPLSALLAAKLA---AEA-GLPDGVLNIVTGFGPT----AGAAIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 S-LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILN----DRMTANPLRQG 421
Cdd:cd07142 243 SnLKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKaralKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 422 sdidhlenVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILV 501
Cdd:cd07142 322 --------VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGS----KGYYIQPTIFSDVKDDMKIARDEIFGPVQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 502 MMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGL 581
Cdd:cd07142 390 ILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDA-SIPFGGYKMSGIGREKGIYALNNY 468
|
....*.
gi 6321828 582 CNAKSV 587
Cdd:cd07142 469 LQVKAV 474
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
112-587 |
2.34e-55 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 196.31 E-value: 2.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPA-TGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAS 190
Cdd:PRK03137 52 IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 191 mGEilvTLEKIQWTIKHGQRALQ------PSRRPGPTNFFMkwykgaeirYEPLGVISSIVSWNYPFHNLLGPIIAALFT 264
Cdd:PRK03137 132 -AD---TAEAIDFLEYYARQMLKladgkpVESRPGEHNRYF---------YIPLGVGVVISPWNFPFAIMAGMTLAAIVA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 265 GNAIVVKCSEQVVWSSEFFVELirkcLEACDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCA 344
Cdd:PRK03137 199 GNTVLLKPASDTPVIAAKFVEV----LEEAGLPAGVVNFV----PGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 345 AKS------LTPVVVELGGKDAfIVLDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPL 418
Cdd:PRK03137 271 AKVqpgqiwLKRVIAEMGGKDA-IVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVEL--TKEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 419 RQGsdiDHLENVDMGAMISDNRFDElealVKDAVAKG---ARLLQGGSRFKhpkyPQGHYFQPTLLVDVTPEMKIAQNEV 495
Cdd:PRK03137 348 TVG---NPEDNAYMGPVINQASFDK----IMSYIEIGkeeGRLVLGGEGDD----SKGYFIQPTIFADVDPKARIMQEEI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 496 FGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFAT-FYVCQLPFGGINGSGY-GKFG 573
Cdd:PRK03137 417 FGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTgAIVGYHPFGGFNMSGTdSKAG 496
|
490
....*....|....
gi 6321828 574 GEEGLLGLCNAKSV 587
Cdd:PRK03137 497 GPDYLLLFLQAKTV 510
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
117-583 |
3.71e-53 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 191.17 E-value: 3.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:PLN02466 80 PRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAEL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQ----WTIK-HGQRAlqpsrrPGPTNFFMkwykgaEIRYEPLGVISSIVSWNYP---FHNLLGPiiaALFTGN 266
Cdd:PLN02466 160 PMFARLFRyyagWADKiHGLTV------PADGPHHV------QTLHEPIGVAGQIIPWNFPllmFAWKVGP---ALACGN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 267 AIVVKCSEQVVWSSEFFVELIrkcLEAcDEDPDLVQLCYCLPPTenddSANYFTSHPGFKHITFIGSQPVAHYILKCAAK 346
Cdd:PLN02466 225 TIVLKTAEQTPLSALYAAKLL---HEA-GLPPGVLNVVSGFGPT----AGAALASHMDVDKLAFTGSTDTGKIVLELAAK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 S-LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKI----LNDRMTANPLRQG 421
Cdd:PLN02466 297 SnLKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKakarALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 422 sdidhlenVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKhpkyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILV 501
Cdd:PLN02466 376 --------VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQS 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 502 MMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCqLPFGGINGSGYGKfggEEGLLGL 581
Cdd:PLN02466 444 ILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAA-IPFGGYKMSGIGR---EKGIYSL 519
|
..
gi 6321828 582 CN 583
Cdd:PLN02466 520 NN 521
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
117-587 |
5.07e-53 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 189.32 E-value: 5.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILV 196
Cdd:PRK13252 29 PATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSVVDIVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQW------TIkHGQRalQPSRrpgPTNFFmkwYKgaeiRYEPLGVISSIVSWNYPFHnllgpiIA------ALFT 264
Cdd:PRK13252 109 GADVLEYyaglapAL-EGEQ--IPLR---GGSFV---YT----RREPLGVCAGIGAWNYPIQ------IAcwksapALAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 265 GNAIVVKCSEQVVWS----SEFFVE--LirkcleacdedPD----LVQlcyclpptENDDSANYFTSHPGFKHITFIGSQ 334
Cdd:PRK13252 170 GNAMIFKPSEVTPLTalklAEIYTEagL-----------PDgvfnVVQ--------GDGRVGAWLTEHPDIAKVSFTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 335 PVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMT 414
Cdd:PRK13252 231 PTGKKVMAAAAASLKEVTMELGGKSPLIVFDDA-DLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 415 AnpLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNE 494
Cdd:PRK13252 310 R--IRIGDPMD--PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 495 VFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGG 574
Cdd:PRK13252 386 IFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPA-EMPVGGYKQSGIGRENG 464
|
490
....*....|...
gi 6321828 575 EEGLLGLCNAKSV 587
Cdd:PRK13252 465 IATLEHYTQIKSV 477
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
117-587 |
1.05e-52 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 188.88 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:PLN02766 43 PRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWTIK-----HGQrALQPSRRpgptnffmkwYKGAEIRyEPLGVISSIVSWNYP---FHNLLGPIIAAlftGN 266
Cdd:PLN02766 123 PAAAGLLRYYAGaadkiHGE-TLKMSRQ----------LQGYTLK-EPIGVVGHIIPWNFPstmFFMKVAPALAA---GC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 267 AIVVKCSEQVVWSSEFFVELIRKCleacdEDPD-LVQLCYCLPPTenddSANYFTSHPGFKHITFIGSQPVAHYILKCAA 345
Cdd:PLN02766 188 TMVVKPAEQTPLSALFYAHLAKLA-----GVPDgVINVVTGFGPT----AGAAIASHMDVDKVSFTGSTEVGRKIMQAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 346 KS-LTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLrqGSDI 424
Cdd:PLN02766 259 TSnLKQVSLELGGKSPLLIFDDA-DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVV--GDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 425 DhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSrfkhPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMK 504
Cdd:PLN02766 336 D--PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 505 AKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGKFGGEEGLLGLCNA 584
Cdd:PLN02766 410 FKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDP-DCPFGGYKMSGFGRDQGMDALDKYLQV 488
|
...
gi 6321828 585 KSV 587
Cdd:PLN02766 489 KSV 491
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
117-590 |
2.60e-52 |
|
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: 187.32 E-value: 2.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:cd07140 28 PTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKTHV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQ----WTIK-HGQRALQPSRRPGPTNFFMKwykgaeirYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIV 269
Cdd:cd07140 108 GMSIQTFRyfagWCDKiQGKTIPINQARPNRNLTLTK--------REPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 270 VKCSEQVVWSSEFFVELIRKCleacDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS-L 348
Cdd:cd07140 180 LKPAQVTPLTALKFAELTVKA----GFPKGVINIL----PGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSnL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 349 TPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQGSDIDhlE 428
Cdd:cd07140 252 KKVSLELGGKSPLIIFADC-DMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEE--VKKMKIGDPLD--R 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 429 NVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkypqGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNT 508
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP----GFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 509 D--HCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQlPFGGINGSGYGKFGGEEGLLGLCNAKS 586
Cdd:cd07140 403 DvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA-PFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
....
gi 6321828 587 VCFD 590
Cdd:cd07140 482 VTIE 485
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
117-588 |
3.69e-52 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 187.04 E-value: 3.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEILV 196
Cdd:PRK11241 33 PANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAK-GEISY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQRALQ---PSRRPGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFHNLL---GPIIAAlftGNAIVV 270
Cdd:PRK11241 112 AASFIEWFAEEGKRIYGdtiPGHQADKRLIVIK---------QPIGVTAAITPWNFPAAMITrkaGPALAA---GCTMVL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 271 KCSEQVVWSSEFFVELIRKCleacdedpDLVQLCYCLPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTP 350
Cdd:PRK11241 180 KPASQTPFSALALAELAIRA--------GIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 VVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILndRMTANPLRQGSDIDhlENV 430
Cdd:PRK11241 252 VSLELGGNAPFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKL--QQAVSKLHIGDGLE--KGV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 431 DMGAMISDNRFDELEALVKDAVAKGARLLQGGSrfkhPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDH 510
Cdd:PRK11241 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGGK----AHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 511 CVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINdfaTFYVCQ--LPFGGINGSGYGKFGGEEGLLGLCNAKSVC 588
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISNevAPFGGIKASGLGREGSKYGIEDYLEIKYMC 479
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
157-578 |
3.01e-51 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 182.63 E-value: 3.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 157 LRVLASLhdyILNNQDLIARVACRDSGKTMLDASMgEILVTLEKIQWTIKHGQR---ALQPSRRPGPTNFFMKwykgaei 233
Cdd:PRK10090 1 LRKIAAG---IRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEWARRyegEIIQSDRPGENILLFK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 234 ryEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCleacdedpDLVQLCYCLPPTEND 313
Cdd:PRK10090 70 --RALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI--------GLPKGVFNLVLGRGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 314 DSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIE 393
Cdd:PRK10090 140 TVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDA-DLDLAVKAIVDSRVINSGQVCNCAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 394 RVIVSKENYDDLVKILNDRMTA----NPLRQgsdidhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHpk 469
Cdd:PRK10090 219 RVYVQKGIYDQFVNRLGEAMQAvqfgNPAER-------NDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEG-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 470 ypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN 549
Cdd:PRK10090 290 --KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
410 420
....*....|....*....|....*....
gi 6321828 550 DfATFYVCQLPFGGINGSGYGKFGGEEGL 578
Cdd:PRK10090 368 R-ENFEAMQGFHAGWRKSGIGGADGKHGL 395
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
104-577 |
4.77e-51 |
|
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: 183.92 E-value: 4.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 104 WNPEEPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSG 183
Cdd:cd07086 7 WVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 184 KTMLDAsMGEIlvtlekiQWTIKHGQRALQPSRRP-GPT------NFFMKwykgaEIRyEPLGVISSIVSWNYPFHNLLG 256
Cdd:cd07086 87 KILPEG-LGEV-------QEMIDICDYAVGLSRMLyGLTipserpGHRLM-----EQW-NPLGVVGVITAFNFPVAVPGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 257 PIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLEACDEDPDLVQLCyclppTENDDSANYFTSHPGFKHITFIGSQPV 336
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV-----TGGGDGGELLVHDPRVPLVSFTGSTEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 337 AHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLD-ALSSIIMrGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtA 415
Cdd:cd07086 228 GRRVGETVARRFGRVLLELGGNNAIIVMDDA-DLDlAVRAVLF-AAVGTAGQRCTTTRRLIVHESVYDEFLERLVKA--Y 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 416 NPLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkyPQGHYFQPTLLVDVTPEMKIAQNEV 495
Cdd:cd07086 304 KQVRIGDPLD--EGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGG--EPGNYVEPTIVTGVTDDARIVQEET 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 496 FGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYV--ANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKfg 573
Cdd:cd07086 380 FAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGR-- 457
|
....
gi 6321828 574 gEEG 577
Cdd:cd07086 458 -ESG 460
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
119-594 |
9.34e-50 |
|
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: 181.24 E-value: 9.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 119 TGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQ-DLIArVACRDSGKTMLDAsMGEILvt 197
Cdd:cd07125 56 HERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRgELIA-LAAAEAGKTLADA-DAEVR-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 198 lEKI---QWTIKHGQRALQPSRRPGPTNffmkwyKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSE 274
Cdd:cd07125 132 -EAIdfcRYYAAQARELFSDPELPGPTG------ELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QVVWSSEFFVELIRKcleaCDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAK---SLTPV 351
Cdd:cd07125 205 QTPLIAARAVELLHE----AGVPRDVLQLV----PGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgPILPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 352 VVELGGKDAFIVlDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhLENvD 431
Cdd:cd07125 277 IAETGGKNAMIV-DSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMAS--LKVGDPWD-LST-D 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 432 MGAMISDNRFDELEALVKdavakgarLLQGGSRFKHPKY---PQGHYFQPTLLVDVTPEmkIAQNEVFGPILVMMKAKNT 508
Cdd:cd07125 352 VGPLIDKPAGKLLRAHTE--------LMRGEAWLIAPAPlddGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 509 --DHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQL-PFGGINGSGYG-KFGGEEGLLGLCNA 584
Cdd:cd07125 422 dlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRqPFGGWGLSGTGpKAGGPNYLLRFGNE 501
|
490
....*....|
gi 6321828 585 KSVCFDTLPF 594
Cdd:cd07125 502 KTVSLNTTAA 511
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
156-574 |
1.17e-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: 176.26 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 156 RLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQRALQPsrRPGPTNFfMKWYKGAEIRY 235
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP--EPVKKNL-ATLLDDVYIYK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 236 EPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdeDPDLVQLcYCLPPTENDDS 315
Cdd:cd07132 99 EPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYL-----DKECYPV-VLGGVEETTEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 316 ANYftshpGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERV 395
Cdd:cd07132 173 LKQ-----RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSC-DIDVAARRIAWGKFINAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 396 IVSKENYDDLVKILNDRMTAnplRQGSDIDhlENVDMGAMISDNRFDELEALVkdavaKGARLLQGGSRFKHPKypqghY 475
Cdd:cd07132 247 LCTPEVQEKFVEALKKTLKE---FYGEDPK--ESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTDEKER-----Y 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 476 FQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFY 555
Cdd:cd07132 312 IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHY 391
|
410 420
....*....|....*....|
gi 6321828 556 -VCQLPFGGINGSGYGKFGG 574
Cdd:cd07132 392 tLDSLPFGGVGNSGMGAYHG 411
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
111-578 |
1.60e-48 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 177.00 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 111 FIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAs 190
Cdd:TIGR01722 17 YIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 191 MGEILVTLEKIQW-----TIKHGQRALQPSRRpgptnffMKWYkgaEIRyEPLGVISSIVSWNYPFHNLLGPIIAALFTG 265
Cdd:TIGR01722 96 LGDVARGLEVVEHacgvnSLLKGETSTQVATR-------VDVY---SIR-QPLGVCAGITPFNFPAMIPLWMFPIAIACG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 266 NAIVVKCSEQVVWSSEFFVELIrkcLEAcdEDPDLVqlcycLPPTENDDSA-NYFTSHPGFKHITFIGSQPVAHYILKCA 344
Cdd:TIGR01722 165 NTFVLKPSEKVPSAAVKLAELF---SEA--GAPDGV-----LNVVHGDKEAvDRLLEHPDVKAVSFVGSTPIGRYIHTTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 345 AKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKEnYDDLVKILNDRmtANPLRQGSDI 424
Cdd:TIGR01722 235 SAHGKRVQALGGAKNHMVVMPDA-DKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRER--AEKIRIGPGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 425 DhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMK 504
Cdd:TIGR01722 311 D--PGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321828 505 AKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYG--KFGGEEGL 578
Cdd:TIGR01722 389 ADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGdhHIYGKQGT 464
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
156-574 |
1.00e-47 |
|
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: 173.37 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 156 RLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQRALQPSRRPGPTNFFMKWykgAEIRY 235
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLTTFPAK---AEIVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 236 EPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdeDPDLVQLCYCLPPTendds 315
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYL-----DTKAIKVIEGGVPE----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 316 ANYFTSHPGFKhITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIVlDSAKNLDALSSIIMRGTFQS-SGQNCIGIER 394
Cdd:cd07137 170 TTALLEQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIV-DSTVDLKVAVRRIAGGKWGCnNGQACIAPDY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 395 VIVSKENYDDLVKILNdrmtaNPLRQGSDIDHLENVDMGAMISDNRFDELEALVKD-AVAkgARLLQGGSRFKhpkypQG 473
Cdd:cd07137 248 VLVEESFAPTLIDALK-----NTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDpSVA--DKIVHGGERDE-----KN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 474 HYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFAT 553
Cdd:cd07137 316 LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVV 395
|
410 420
....*....|....*....|..
gi 6321828 554 FYVC-QLPFGGINGSGYGKFGG 574
Cdd:cd07137 396 QYAIdTLPFGGVGESGFGAYHG 417
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
117-573 |
4.46e-47 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 173.40 E-value: 4.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEILV 196
Cdd:PLN00412 38 PSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQRALQPSR----RPGPTNFFMKWYKGAEIryePLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKC 272
Cdd:PLN00412 117 SGDLISYTAEEGVRILGEGKflvsDSFPGNERNKYCLTSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 273 SEQVVWSSEFFVElirkCLEACDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPvahYILKCAAKSLTPVV 352
Cdd:PLN00412 194 PTQGAVAALHMVH----CFHLAGFPKGLISCV----TGKGSEIGDFLTMHPGVNCISFTGGDT---GIAISKKAGMVPLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 353 VELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLRQGSDidhleNVDM 432
Cdd:PLN00412 263 MELGGKDACIVLEDA-DLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-----DCDI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 433 GAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCV 512
Cdd:PLN00412 337 TPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGI 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321828 513 QLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYGKFG 573
Cdd:PLN00412 410 HHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQG 470
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
118-587 |
1.85e-46 |
|
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: 171.61 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 118 ATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASmGEILVT 197
Cdd:cd07083 41 APSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAI-DDVAEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 198 LEKIQWTIKH-----GQRALQPSRrPGPTNffmkwykgaEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKC 272
Cdd:cd07083 120 IDFIRYYARAalrlrYPAVEVVPY-PGEDN---------ESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 273 SEQVVWSSEFFVELIRkclEAcDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLT--- 349
Cdd:cd07083 190 AEDAVVVGYKVFEIFH---EA-GFPPGVVQFL----PGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPgqt 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 350 ---PVVVELGGKDAFIVlDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMT----ANPLRQGS 422
Cdd:cd07083 262 wfkRLYVETGGKNAIIV-DETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAErlsvGPPEENGT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 423 DIdhlenvdmGAMISDNRFDELEALVKDAVAKGaRLLQGGSRFKHpkypQGHYFQPTLLVDVTPEMKIAQNEVFGPILVM 502
Cdd:cd07083 341 DL--------GPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEG----EGYFVAPTVVEEVPPKARIAQEEIFGPVLSV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 503 MKAKNTD--HCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFAT-FYVCQLPFGGINGSGYG-KFGGEEGL 578
Cdd:cd07083 408 IRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgALVGVQPFGGFKLSGTNaKTGGPHYL 487
|
....*....
gi 6321828 579 LGLCNAKSV 587
Cdd:cd07083 488 RRFLEMKAV 496
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
112-570 |
1.88e-46 |
|
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: 170.68 E-value: 1.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAG---KAQSTWGNSdfSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLD 188
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHalfLDRNNWLPA--HERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 189 ASMgEILVTLEKIQWTIKH-GQRA-------LQPSRRpGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFHNLLGPIIA 260
Cdd:cd07148 79 AKV-EVTRAIDGVELAADElGQLGgreipmgLTPASA-GRIAFTTR---------EPIGVVVAISAFNHPLNLIVHQVAP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 261 ALFTGNAIVVKCSEQVVWSSEFFVELIRkclEAcdEDPDlvQLCYCLPPteNDDSANYFTSHPGFKHITFIGSQPVAHYi 340
Cdd:cd07148 148 AIAAGCPVIVKPALATPLSCLAFVDLLH---EA--GLPE--GWCQAVPC--ENAVAEKLVTDPRVAFFSFIGSARVGWM- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 341 LKCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRmtANPLRQ 420
Cdd:cd07148 218 LRSKLAPGTRCALEHGGAAPVIVDRSA-DLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAA--AEKLVV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 421 GSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYpqghyfQPTLLVDVTPEMKIAQNEVFGPIL 500
Cdd:cd07148 295 GDPTD--PDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPVV 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 501 VMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSGYG 570
Cdd:cd07148 367 CVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
133-568 |
5.95e-46 |
|
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: 168.60 E-value: 5.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 133 DIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEILVTLEKIQWTIKHGQRAL 212
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 213 QPSRRPGPtnffmkwYKGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVElirkCLE 292
Cdd:cd07095 80 GERATPMA-------QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVE----LWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 293 ACDEDPDLVQLCyclppTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAA----KSLTpvvVELGGKDAFIVLDSAk 368
Cdd:cd07095 149 EAGLPPGVLNLV-----QGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAgrpgKILA---LEMGGNNPLVVWDVA- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 369 NLDALSSIIMRGTFQSSGQNCIGIERVIV-SKENYDDLVkilnDRMTAnpLRQGSDIDHLENVD--MGAMISDNRFDELE 445
Cdd:cd07095 220 DIDAAAYLIVQSAFLTAGQRCTCARRLIVpDGAVGDAFL----ERLVE--AAKRLRIGAPDAEPpfMGPLIIAAAAARYL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 446 ALVKDAVAKGARLLQGGSRFkhpkyPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGS 525
Cdd:cd07095 294 LAQQDLLALGGEPLLAMERL-----VAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAG 368
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 6321828 526 VFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSG 568
Cdd:cd07095 369 LLSDDEALFERFLARIRAGIVNWNRPTTGASSTAPFGGVGLSG 411
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
117-571 |
2.51e-44 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 165.45 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKA--QSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEI 194
Cdd:PRK09847 42 PVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWTIKHGQRALQPSRRPGPTNFFMkwykgaeIRYEPLGVISSIVSWNYPFHNL---LGPiiaALFTGNAIVVK 271
Cdd:PRK09847 122 PGAARAIRWYAEAIDKVYGEVATTSSHELAM-------IVREPVGVIAAIVPWNFPLLLTcwkLGP---ALAAGNSVILK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 272 CSEQVVWSSEFFVELIRkclEAcdEDPDLVqlcYCLPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKS-LTP 350
Cdd:PRK09847 192 PSEKSPLSAIRLAGLAK---EA--GLPDGV---LNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMKR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 351 VVVELGGKDAFIVLDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILndRMTANPLRQGSDIDhlENV 430
Cdd:PRK09847 264 VWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALL--KQQAQNWQPGHPLD--PAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 431 DMGAMISDNRFDELEALVKDAVAKGARLLQGGSrfkhpkypQGH--YFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNT 508
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESKGQLLLDGRN--------AGLaaAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321828 509 DHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVcQLPFGGINGSGYGK 571
Cdd:PRK09847 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM-TVPFGGYKQSGNGR 473
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
117-571 |
5.56e-42 |
|
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: 158.38 E-value: 5.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILV 196
Cdd:cd07116 23 PVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADIPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQW---TIKHGQRALqpSRRPGPTNffmkwykgAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCS 273
Cdd:cd07116 103 AIDHFRYfagCIRAQEGSI--SEIDENTV--------AYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 274 EQVVWSSEFFVELIRKCLEacdedPDLVQLCYCLPPtendDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVV 353
Cdd:cd07116 173 EQTPASILVLMELIGDLLP-----PGVVNVVNGFGL----EAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 354 ELGGKDAFIVLDSAKNLD------ALSSIIMRGTFQssGQNCIGIERVIVSKENYDDLVKILNDRMTAnpLRQGSDIDhl 427
Cdd:cd07116 244 ELGGKSPNIFFADVMDADdaffdkALEGFVMFALNQ--GEVCTCPSRALIQESIYDRFMERALERVKA--IKQGNPLD-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 428 ENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLlVDVTPEMKIAQNEVFGPILVMMKAKN 507
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTT-FKGGNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321828 508 TDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATfYVCQLPFGGINGSGYGK 571
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHL-YPAHAAFGGYKQSGIGR 459
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
131-574 |
8.15e-42 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 158.35 E-value: 8.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 131 EADIDEM--VSKAGKAQS-TWGNSdfsrRLRVLASLhdyILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKH 207
Cdd:PLN02203 9 EGSVAELreTYESGRTRSlEWRKS----QLKGLLRL---LKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 208 GQRALQPSRRPGPTNFFMKwykGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELI 287
Cdd:PLN02203 82 LKKWMAPKKAKLPLVAFPA---TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 288 RKCLeacdeDPDLVQLCYCLPptendDSANYFTSHPGFKhITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAFIV--LD 365
Cdd:PLN02203 159 PKYL-----DSKAVKVIEGGP-----AVGEQLLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 366 SAKNLDALSSIIMRGTFQS-SGQNCIGIERVIVSKENYDDLVKILNDR----MTANPLRQGSdidhlenvdMGAMISDNR 440
Cdd:PLN02203 228 SSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTikkfFGENPRESKS---------MARILNKKH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 441 FDELEALVKDAVAKgARLLQGGSrfkhpKYPQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPF 520
Cdd:PLN02203 299 FQRLSNLLKDPRVA-ASIVHGGS-----IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 6321828 521 GLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQ-LPFGGINGSGYGKFGG 574
Cdd:PLN02203 373 PLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDsLPFGGVGESGFGRYHG 427
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
107-573 |
9.49e-41 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 157.22 E-value: 9.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 107 EEPNFIQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTM 186
Cdd:PLN02419 126 QSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 187 LDaSMGEILVTLEKIQWTIkhGQRALQ-----PSRRPGPTNFFMKwykgaeiryEPLGVISSIVSWNYPFHNLLGPIIAA 261
Cdd:PLN02419 206 KD-SHGDIFRGLEVVEHAC--GMATLQmgeylPNVSNGVDTYSIR---------EPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 262 LFTGNAIVVKCSEQVVWSSEFFVELirkCLEACDEDpDLVQLCYclpptENDDSANYFTSHPGFKHITFIGSQPVAHYIL 341
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAEL---AMEAGLPD-GVLNIVH-----GTNDTVNAICDDEDIRAVSFVGSNTAGMHIY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 342 KCAAKSLTPVVVELGGKDAFIVLDSAkNLDALSSIIMRGTFQSSGQNCIGIERVIV---SKENYDDLVkilnDRMTANPL 418
Cdd:PLN02419 345 ARAAAKGKRIQSNMGAKNHGLVLPDA-NIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLV----ERAKALKV 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 419 RQGSDIDhlenVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQGHYFQPTLLVDVTPEMKIAQNEVFGP 498
Cdd:PLN02419 420 TCGSEPD----ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGP 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 499 ILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN-------DFATFYVCQLPFGGiNGSGYGK 571
Cdd:PLN02419 496 VLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINvpipvplPFFSFTGNKASFAG-DLNFYGK 574
|
..
gi 6321828 572 FG 573
Cdd:PLN02419 575 AG 576
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
156-592 |
4.02e-38 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 147.89 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 156 RLRVLASLHDYILNNQDLIARVACRDSGKTMLDASMGEILVTLEKIQWTIKHGQRALQPSRRPGPTNFFMKwykGAEIRY 235
Cdd:PLN02174 34 RVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPA---SAEIVS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 236 EPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLeacdeDPDLVQLcyclppTENDDS 315
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYL-----DSSAVRV------VEGAVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 316 ANYFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVVELGGKDAfIVLDSAKNLDALSSIIMRGTFQ-SSGQNCIGIER 394
Cdd:PLN02174 180 ETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSP-VVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 395 VIVSKENYDDLVKILNDRMTA----NPlrqgsdidhLENVDMGAMISDNRFDELEALVkDAVAKGARLLQGGSRFKhpky 470
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETfygkNP---------MESKDMSRIVNSTHFDRLSKLL-DEKEVSDKIVYGGEKDR---- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 471 pQGHYFQPTLLVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIND 550
Cdd:PLN02174 325 -ENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVND 403
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 6321828 551 FATFYVCQ-LPFGGINGSGYGKFGGEEGLLGLCNAKSVCFDTL 592
Cdd:PLN02174 404 IAVHLALHtLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSL 446
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
112-533 |
9.81e-32 |
|
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: 128.86 E-value: 9.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsM 191
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEG-L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 192 GEI---------LVTLEKIQwtikHGQraLQPSRRPGptNFFMKwykgaeiRYEPLGVISSIVSWNYPfhnllgpiIA-- 260
Cdd:cd07130 93 GEVqemidicdfAVGLSRQL----YGL--TIPSERPG--HRMME-------QWNPLGVVGVITAFNFP--------VAvw 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 261 ------ALFTGNAIVVKCSEQVVWSSEFFVELIRKCLEACDEDPDLVQLCYClppteNDDSANYFTSHPGFKHITFIGSQ 334
Cdd:cd07130 150 gwnaaiALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCG-----GADVGEALVKDPRVPLVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 335 PVAHYILKCAAKSLTPVVVELGGKDAFIVLDSAkNLD-ALSSIIMR--GTfqsSGQNCIGIERVIVSKENYDDLVkilnD 411
Cdd:cd07130 225 AVGRQVGQAVAARFGRSLLELGGNNAIIVMEDA-DLDlAVRAVLFAavGT---AGQRCTTTRRLIVHESIYDEVL----E 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 412 RMTA--NPLRQGSDIDhlENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPkypqGHYFQPTLlVDVTPEMK 489
Cdd:cd07130 297 RLKKayKQVRIGDPLD--DGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP----GNYVEPTI-VEGLSDAP 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 6321828 490 IAQNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGADIKE 533
Cdd:cd07130 370 IVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRN 413
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
112-568 |
1.56e-29 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 122.37 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 112 IQCHCPATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDASM 191
Cdd:PRK09457 17 FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 192 gEILVTLEKIQWTIKHGQRALQPSRRPGPTNffmkwykGAEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVK 271
Cdd:PRK09457 97 -EVTAMINKIAISIQAYHERTGEKRSEMADG-------AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 272 CSEQVVWSSEFFVELIRKC-LEAcdEDPDLVQlcyclpptENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAA----K 346
Cdd:PRK09457 169 PSELTPWVAELTVKLWQQAgLPA--GVLNLVQ--------GGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAgqpeK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 SLTpvvVELGGKDAFIVlDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSK-ENYDDLVKILNDrmTANPLRQGSDID 425
Cdd:PRK09457 239 ILA---LEMGGNNPLVI-DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQgAQGDAFLARLVA--VAKRLTVGRWDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 426 HLENVdMGAMISDNRFDELEALVKDAVAKGARLLqggsrfKHPKYPQ-GHYFQPTLLVDVTPEMKIAQNEVFGPILVMMK 504
Cdd:PRK09457 313 EPQPF-MGAVISEQAAQGLVAAQAQLLALGGKSL------LEMTQLQaGTGLLTPGIIDVTGVAELPDEEYFGPLLQVVR 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321828 505 AKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAINDFATFYVCQLPFGGINGSG 568
Cdd:PRK09457 386 YDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASG 449
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-574 |
4.89e-28 |
|
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: 118.09 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 103 IWNPEEPNFIqchcpatgqyLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDS 182
Cdd:TIGR01238 55 VTNPADRRDI----------VGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 183 GKTMLDAsmgeilvtlekiqwtIKHGQRALQpsrrpgptnfFMKWYKG------AEIRYEPLGVISSIVSWNYPFHNLLG 256
Cdd:TIGR01238 125 GKTIHNA---------------IAEVREAVD----------FCRYYAKqvrdvlGEFSVESRGVFVCISPWNFPLAIFTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 257 PIIAALFTGNAIVVKCSEQVVWSSEFFVELIrkcLEAcDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPV 336
Cdd:TIGR01238 180 QISAALAAGNTVIAKPAEQTSLIAYRAVELM---QEA-GFPAGTIQLL----PGRGADVGAALTSDPRIAGVAFTGSTEV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 337 AHYILKCAAKSL---TPVVVELGGKDAFIVlDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRM 413
Cdd:TIGR01238 252 AQLINQTLAQREdapVPLIAETGGQNAMIV-DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 414 taNPLRQGsdIDHLENVDMGAMISDNRFDELEALVKDAVAKGARLLQgGSRFKHPKYPQGHYFQPTLL-VDVTPEMkiaQ 492
Cdd:TIGR01238 331 --QELKVG--VPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQ-LTLDDSRACQHGTFVAPTLFeLDDIAEL---S 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 493 NEVFGPIL--VMMKAKNTDHCVQLANSAPFGLGGSVFGADIKECNYVANSLQTGNVAIN-DFATFYVCQLPFGGINGSGY 569
Cdd:TIGR01238 403 EEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrNQVGAVVGVQPFGGQGLSGT 482
|
....*.
gi 6321828 570 G-KFGG 574
Cdd:TIGR01238 483 GpKAGG 488
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
116-591 |
9.33e-26 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 113.37 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 116 CPA-TGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQD-LIArVACRDSGKTMLDAsMGE 193
Cdd:PRK11904 568 SPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAeLIA-LCVREAGKTLQDA-IAE 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 194 ILvtlEKI---QWTIKHGQRAL-QPSRRPGPT---NffmkwykgaEIRYEPLGVISSIVSWNYPFHNLLGPIIAALFTGN 266
Cdd:PRK11904 646 VR---EAVdfcRYYAAQARRLFgAPEKLPGPTgesN---------ELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGN 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 267 AIVVKCSEQVVWSSEFFVELirkcLEACDEDPDLVQLcycLPptenDDSA---NYFTSHPGFKHITFIGSQPVAHYI--- 340
Cdd:PRK11904 714 TVIAKPAEQTPLIAAEAVKL----LHEAGIPKDVLQL---LP----GDGAtvgAALTADPRIAGVAFTGSTETARIInrt 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 341 LkcAAKS--LTPVVVELGGKDAFIVLDSAknL------DALSSiimrgTFQSSGQNCIGIeRVI-VSKENYDDLVKILND 411
Cdd:PRK11904 783 L--AARDgpIVPLIAETGGQNAMIVDSTA--LpeqvvdDVVTS-----AFRSAGQRCSAL-RVLfVQEDIADRVIEMLKG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 412 RMTAnpLRQGSDIDHleNVDMGAMISDNRFDELEALVkDAVAKGARLLQGGSRfkhPKYPQ-GHYFQPTLLvdvtpEMK- 489
Cdd:PRK11904 853 AMAE--LKVGDPRLL--STDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPL---PAGTEnGHFVAPTAF-----EIDs 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 490 IAQ--NEVFGPIL--VMMKAKNTDHCVQLANSAPFGLggsVFG--ADIKE-CNYVANSLQTGNVAIN-DFATFYVCQLPF 561
Cdd:PRK11904 920 ISQleREVFGPILhvIRYKASDLDKVIDAINATGYGL---TLGihSRIEEtADRIADRVRVGNVYVNrNQIGAVVGVQPF 996
|
490 500 510
....*....|....*....|....*....|.
gi 6321828 562 GGINGSGYG-KFGGEEGLLGLCNAKSVCFDT 591
Cdd:PRK11904 997 GGQGLSGTGpKAGGPHYLLRFATEKTVTVNT 1027
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
110-568 |
1.54e-25 |
|
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: 110.75 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 110 NFIQCHCPAT-GQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILN--NQDLIArvacrdsgKTM 186
Cdd:cd07123 46 NTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGkyRYELNA--------ATM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 187 LDAS----MGEILVTLEKI---QWTIKHGQRALQ---PSRRPGPTNFfmkwykgaeIRYEPL-GVISSIVswnyPFH--- 252
Cdd:cd07123 118 LGQGknvwQAEIDAACELIdflRFNVKYAEELYAqqpLSSPAGVWNR---------LEYRPLeGFVYAVS----PFNfta 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 253 ---NLlgPIIAALFtGNAIVVKCSEQVVWSSEFFVELirkcLEACDEDPDLVQLCYCLPPTENDdsanYFTSHPGFKHIT 329
Cdd:cd07123 185 iggNL--AGAPALM-GNVVLWKPSDTAVLSNYLVYKI----LEEAGLPPGVINFVPGDGPVVGD----TVLASPHLAGLH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 330 FIGSQPVAHYILKCAAKSLT-----PVVV-ELGGKDaFIVLDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKENYD 403
Cdd:cd07123 254 FTGSTPTFKSLWKQIGENLDryrtyPRIVgETGGKN-FHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 404 DLVKILNDRMTAnpLRQGSDIDHleNVDMGAMISDNRFDELEALVKDAVA-KGARLLQGGSRFKHpkypQGHYFQPTLLV 482
Cdd:cd07123 333 EVKERLLEELKE--IKMGDPDDF--SNFMGAVIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDS----VGYFVEPTVIE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 483 DVTPEMKIAQNEVFGPILVMM--KAKNTDHCVQLANSA-PFGLGGSVFGADIKECNYVANSLQ--TGNVAINDFAT-FYV 556
Cdd:cd07123 405 TTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTgAVV 484
|
490
....*....|..
gi 6321828 557 CQLPFGGINGSG 568
Cdd:cd07123 485 GQQPFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
130-574 |
1.23e-20 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 97.24 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 130 TEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKTMLDAsMGEILvtlEKIQwtikhgq 209
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANA-IAEVR---EAVD------- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 210 ralqpsrrpgptnfFMKWYkGAEIR-------YEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEF 282
Cdd:PRK11905 657 --------------FLRYY-AAQARrllngpgHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAAR 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 283 FVELirkcLEACDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSL---TPVVVELGGKD 359
Cdd:PRK11905 722 AVRL----LHEAGVPKDALQLL----PGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSgppVPLIAETGGQN 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 360 AFIVLDSAknL------DALSSiimrgTFQSSGQNCIGIeRVI-VSKENYDDLVKILNDRMTAnpLRQGsDIDHLeNVDM 432
Cdd:PRK11905 794 AMIVDSSA--LpeqvvaDVIAS-----AFDSAGQRCSAL-RVLcLQEDVADRVLTMLKGAMDE--LRIG-DPWRL-STDV 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 433 GAMISDNRFDELEALVKDAVAKGARLLQGGSRfkhPKYPQGHYFQPTLL-VDVTPEMKiaqNEVFGPIL--VMMKAKNTD 509
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRLVHQLPLP---AETEKGTFVAPTLIeIDSISDLE---REVFGPVLhvVRFKADELD 935
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321828 510 HCVQLANSAPFGLggsVFG--ADIKE-CNYVANSLQTGNVAINDF---ATFYVcQlPFGGINGSGYG-KFGG 574
Cdd:PRK11905 936 RVIDDINATGYGL---TFGlhSRIDEtIAHVTSRIRAGNIYVNRNiigAVVGV-Q-PFGGEGLSGTGpKAGG 1002
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
130-591 |
1.48e-20 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 96.93 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 130 TEADIDEMVSKAGKAQSTWGNSDFSRR---LRVLASLhdYILNNQDLIArVACRDSGKTMLDAsMGEIlvtlekiqwtik 206
Cdd:COG4230 591 TAADVEAALAAAQAAFPAWSATPVEERaaiLERAADL--LEAHRAELMA-LLVREAGKTLPDA-IAEV------------ 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 207 hgqR---------ALQpSRRpgptNFfmkwykGAEIRYEPLGVISSIVSWNYP---FhnlLGPIIAALFTGNAIVVKCSE 274
Cdd:COG4230 655 ---ReavdfcryyAAQ-ARR----LF------AAPTVLRGRGVFVCISPWNFPlaiF---TGQVAAALAAGNTVLAKPAE 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QVVwsseffveLI-----RKCLEAcDEDPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYI---LkcAAK 346
Cdd:COG4230 718 QTP--------LIaaravRLLHEA-GVPADVLQLL----PGDGETVGAALVADPRIAGVAFTGSTETARLInrtL--AAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 --SLTPVVVELGGKDAFIVLDSAknL------DALSSiimrgTFQSSGQNCIGIeRVI-VSKENYDDLVKILNDRMTAnp 417
Cdd:COG4230 783 dgPIVPLIAETGGQNAMIVDSSA--LpeqvvdDVLAS-----AFDSAGQRCSAL-RVLcVQEDIADRVLEMLKGAMAE-- 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 418 LRQGsDIDHLEnVDMGAMISDNRFDELEALVKDAVAKGARLLQGgsrfKHPKYP-QGHYFQPTLlvdvtpeMKIA----- 491
Cdd:COG4230 853 LRVG-DPADLS-TDVGPVIDAEARANLEAHIERMRAEGRLVHQL----PLPEECaNGTFVAPTL-------IEIDsisdl 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 492 QNEVFGPIL--VMMKAKNTDHCVQLANSAPFGLggsVFG--ADIKE-CNYVANSLQTGNVaindfatfYV---------- 556
Cdd:COG4230 920 EREVFGPVLhvVRYKADELDKVIDAINATGYGL---TLGvhSRIDEtIDRVAARARVGNV--------YVnrniigavvg 988
|
490 500 510
....*....|....*....|....*....|....*.
gi 6321828 557 CQlPFGGINGSGYG-KFGGEEGLLGLCNAKSVCFDT 591
Cdd:COG4230 989 VQ-PFGGEGLSGTGpKAGGPHYLLRFATERTVTVNT 1023
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
117-527 |
3.91e-20 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 94.13 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 117 PATGQYLGSFPSKTEADIDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSGKtMLDASMGEILV 196
Cdd:PLN02315 41 PANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGK-ILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 197 TLEKIQWTIKHGQR---ALQPSRRPgptNFFMkwykgAEIrYEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCS 273
Cdd:PLN02315 120 IIDMCDFAVGLSRQlngSIIPSERP---NHMM-----MEV-WNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 274 EQVVWSSEFFVELIRKCLEAcDEDPDLVQLCYClPPTENDDSANYFTSHPgfkHITFIGSQPVAHYILKCAAKSLTPVVV 353
Cdd:PLN02315 191 PTTPLITIAMTKLVAEVLEK-NNLPGAIFTSFC-GGAEIGEAIAKDTRIP---LVSFTGSSKVGLMVQQTVNARFGKCLL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 354 ELGGKDAFIVLDSAKNLDALSSIIMrGTFQSSGQNCIGIERVIVSKENYDD----LVKILNDRMTANPLRQGSDIdhlen 429
Cdd:PLN02315 266 ELSGNNAIIVMDDADIQLAVRSVLF-AAVGTAGQRCTTCRRLLLHESIYDDvleqLLTVYKQVKIGDPLEKGTLL----- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 430 vdmGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKhpkyPQGHYFQPTLlVDVTPEMKIAQNEVFGPILVMMKAKNTD 509
Cdd:PLN02315 340 ---GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLE 411
|
410
....*....|....*...
gi 6321828 510 HCVQLANSAPFGLGGSVF 527
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIF 429
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
224-574 |
2.58e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 83.10 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 224 FMKWYkGAEIR-------YEPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQvvwSSEFFVELIRKCLEAcDE 296
Cdd:PRK11809 749 FLRYY-AGQVRddfdndtHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQ---TPLIAAQAVRILLEA-GV 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 297 DPDLVQLCyclpPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAKSL------TPVVVELGGKDAFIVLDSAKN- 369
Cdd:PRK11809 824 PAGVVQLL----PGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTe 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 370 ---LDALSSiimrgTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMT----ANPlrqgsdiDHLeNVDMGAMISDNRFD 442
Cdd:PRK11809 900 qvvADVLAS-----AFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAecrmGNP-------DRL-STDIGPVIDAEAKA 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 443 ELEALVKDAVAKGARLLQGGsRFKHPKYPQGHYFQPTLL-VDVTPEMKiaqNEVFGPIL--VMMKAKNTDHCVQLANSAP 519
Cdd:PRK11809 967 NIERHIQAMRAKGRPVFQAA-RENSEDWQSGTFVPPTLIeLDSFDELK---REVFGPVLhvVRYNRNQLDELIEQINASG 1042
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 520 FGLggsVFG--ADIKEC-NYVANSLQTGNVAIN-DFATFYVCQLPFGGINGSGYG-KFGG 574
Cdd:PRK11809 1043 YGL---TLGvhTRIDETiAQVTGSAHVGNLYVNrNMVGAVVGVQPFGGEGLSGTGpKAGG 1099
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
237-570 |
5.93e-16 |
|
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: 80.74 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 237 PLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLEACDEDPDLVQlcyclpptENDDSA 316
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLIN--------GDGKTM 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 317 NYFTSHPGFKHITFIGSQPVAHYILKCAAKSltPVVVELGGKDAFIVLDSAKNLDALSSIIMRGTFQSSGQNCIGIERVI 396
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTACSGQKCTAQSMLF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 397 V----SKENYDDLVKILndrmtanpLRQGSDIDHLenvdMGAMISDNRFDELEALVKDAvakGARLLQGGSRFKHPKYPQ 472
Cdd:cd07084 250 VpenwSKTPLVEKLKAL--------LARRKLEDLL----LGPVQTFTTLAMIAHMENLL---GSVLLFSGKELKNHSIPS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 473 --GHYFQPTLLVDVTPEMK---IAQNEVFGPILVMMKAKNTD--HCVQLANSAPFGLGGSVFGADIKECNYV-------- 537
Cdd:cd07084 315 iyGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQlaLVLELLERMHGSLTAAIYSNDPIFLQELignlwvag 394
|
330 340 350
....*....|....*....|....*....|....*.
gi 6321828 538 ---ANSLQTGNVAINdfatfyvcQLPFGGINGSGYG 570
Cdd:cd07084 395 rtyAILRGRTGVAPN--------QNHGGGPAADPRG 422
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
132-515 |
9.10e-16 |
|
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: 80.60 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 132 ADIDEMVSKAGKAQSTWgnSDFSRRLRVLASLHdyILnnQDLIAR-----------------VACRDSGKTMLDASMgEI 194
Cdd:cd07127 84 CDPDALLAAARAAMPGW--RDAGARARAGVCLE--IL--QRLNARsfemahavmhttgqafmMAFQAGGPHAQDRGL-EA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 195 LVTLEKIQWTIKHGQRALQPSRRPGPTNFfmkwykgaEIRYEPLG-----VI--SSIVSWN-YPfhnllgPIIAALFTGN 266
Cdd:cd07127 157 VAYAWREMSRIPPTAEWEKPQGKHDPLAM--------EKTFTVVPrgvalVIgcSTFPTWNgYP------GLFASLATGN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 267 AIVVKCSEQVVWSSEFFVELIRKCLEACDEDPDLVQLCyclPPTENDDSANYFTSHPGFKHITFIGSQPVAHYILKCAAK 346
Cdd:cd07127 223 PVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLA---ADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 347 SLtpVVVELGGKDAFIVlDSAKNLDALSSIIMRGTFQSSGQNCIGIERVIVSKE---------NYDDLVKILN---DRMT 414
Cdd:cd07127 300 AQ--VYTEKAGVNTVVV-DSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAaaiDGLL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 415 ANPLRQgsdidhleNVDMGAMISDNRFDELEAlvkdaVAKGARLLQGGSRFKHPKYPQGHYFQPTLL-VDVTPEMKIAQn 493
Cdd:cd07127 377 ADPARA--------AALLGAIQSPDTLARIAE-----ARQLGEVLLASEAVAHPEFPDARVRTPLLLkLDASDEAAYAE- 442
|
410 420
....*....|....*....|..
gi 6321828 494 EVFGPILVMMKAKNTDHCVQLA 515
Cdd:cd07127 443 ERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
383-530 |
8.10e-11 |
|
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: 64.98 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 383 QSSGQNCIGIERVIVSKENYDDLVKILNDRMTANPLRQGSDidhlENVDMGAMISDNRFDELEALVkDAVAKGARLLQGG 462
Cdd:cd07128 286 VKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRL----EGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGG 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321828 463 SRFKHPK---YPQGHYFQPTLLVDVTPEMKIA--QNEVFGPILVMMKAKNTDHCVQLANSAPFGLGGSVFGAD 530
Cdd:cd07128 361 PDRFEVVgadAEKGAFFPPTLLLCDDPDAATAvhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
371-530 |
2.18e-10 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 63.57 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 371 DALSSIIMRGTFQSSGQNCIGIERVIVSKENYDDLVKILNDRMTA----NPlRQgsdidhlENVDMGAMISDNRFDELEA 446
Cdd:PRK11903 278 DLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKttvgNP-RN-------DGVRMGPLVSRAQLAAVRA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 447 LVkDAVAKGARLLQGGSRFKHPKY-PQGHYF-QPTLLV--DVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLANSAPFGL 522
Cdd:PRK11903 350 GL-AALRAQAEVLFDGGGFALVDAdPAVAACvGPTLLGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSL 428
|
....*...
gi 6321828 523 GGSVFGAD 530
Cdd:PRK11903 429 VASVYSDD 436
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
237-537 |
5.82e-08 |
|
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: 55.58 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 237 PLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKC-LEACDEDpdlvqLCYCLPPTENDds 315
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVD-----LIHSDGPTMNK-- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 316 anyFTSHPGFKHITFIGSQPVAHyilKCAAKSLTPVVVELGGKDAFIVLDSAKNLDALSSIIMRGTFQSSGQNCiGIERV 395
Cdd:cd07126 215 ---ILLEANPRMTLFTGSSKVAE---RLALELHGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKC-SAQSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 396 IVSKENYDDlVKILNDRMTANPLRQgsdidhLENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGSRFKHPKYPQ--G 473
Cdd:cd07126 288 LFAHENWVQ-AGILDKLKALAEQRK------LEDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLTNHSIPSiyG 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321828 474 HYfQPTLLVDVTPEMKIAQN------EVFGPILVMMKAKNT--DHCVQLANSAPFGLGGSVFGADIKECNYV 537
Cdd:cd07126 361 AY-EPTAVFVPLEEIAIEENfelvttEVFGPFQVVTEYKDEqlPLVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
236-549 |
1.29e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 54.58 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 236 EPLGVISSIVSWNYPFHNLLGPIIAALFTGNAIVVKCSEQVVWSSEFFVELIRKCLEACDEDPDLVqLCYCLPPTEnddS 315
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLI-GWIDNPSIE---L 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 316 ANYFTSHPGFKHITFIGSQPVahyiLKCAAKSLTPVVVELGGKDAFIVLDSAKNLDALSSIIMRGTFqSSGQNCIGIERV 395
Cdd:cd07081 170 AQRLMKFPGIGLLLATGGPAV----VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTF-DNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 396 IVSKENYDDLVKILNDR----MTANPLRQGSDIdHLENVDMGAMISDNRFDELEALVKDAVAKGARLLQGGsrfkhpkyp 471
Cdd:cd07081 245 IVVDSVYDEVMRLFEGQgaykLTAEELQQVQPV-ILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGE--------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 472 qghyfqptllVDVTPEMKIAQNEVFGPILVMMKAKNTDHCVQLAnSAPFGLGG----SVFGAD----IKECNYVANSLQT 543
Cdd:cd07081 315 ----------VTSLAEHEPFAHEKLSPVLAMYRAANFADADAKA-LALKLEGGcghtSAMYSDnikaIENMNQFANAMKT 383
|
....*.
gi 6321828 544 GNVAIN 549
Cdd:cd07081 384 SRFVKN 389
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
134-553 |
1.09e-06 |
|
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: 51.39 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 134 IDEMVSKAGKAQSTWGNSDFSRRLRVLASLHDYILNNQDLIARVACRDSG--KTMLDasmGEILVT----------LEKI 201
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpEARLQ---GELGRTtgqlrlfadlVREG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 202 QW---TIKHGQralqPSRRPGPtnffmkwykGAEIR--YEPLGVISSIVSWNYP--FHNLLGPIIAALFTGNAIVVKCSE 274
Cdd:cd07129 78 SWldaRIDPAD----PDRQPLP---------RPDLRrmLVPLGPVAVFGASNFPlaFSVAGGDTASALAAGCPVVVKAHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 275 QVVWSSEFFVELIRKCLEACDEDPDLVQLCYClppTENDDSANyFTSHPGFKHITFIGSQPVAHYILKCAAKSLTPVVV- 353
Cdd:cd07129 145 AHPGTSELVARAIRAALRATGLPAGVFSLLQG---GGREVGVA-LVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIPFy 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 354 -ELGGKDAFIVLDSAknLDALSSIIMRGTFQS----SGQNCI--GIerVIVSK-ENYDDLVKILndrmtanplrqgsdID 425
Cdd:cd07129 221 aELGSVNPVFILPGA--LAERGEAIAQGFVGSltlgAGQFCTnpGL--VLVPAgPAGDAFIAAL--------------AE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 426 HLENVDMGAMISDN---RFDE-LEALVKdavAKGARLLQGGsrfkhPKYPQGHYFQPTLL-VDVTPEMK--IAQNEVFGP 498
Cdd:cd07129 283 ALAAAPAQTMLTPGiaeAYRQgVEALAA---APGVRVLAGG-----AAAEGGNQAAPTLFkVDAAAFLAdpALQEEVFGP 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321828 499 ILVMMKAKNTDHCVQLANSAPFGLGGSVFGA--DIKECNYVANSLQ--TGNVAINDFAT 553
Cdd:cd07129 355 ASLVVRYDDAAELLAVAEALEGQLTATIHGEedDLALARELLPVLErkAGRLLFNGWPT 413
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
236-517 |
1.14e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 48.26 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 236 EPLGVISSIV-SWNyPFHNLLGPIIAALFTGNAIV-------VKCSEQVvwsseffVELIRKCLEACDEDPDLVQlcyCL 307
Cdd:cd07122 94 EPVGVIAALIpSTN-PTSTAIFKALIALKTRNAIIfsphpraKKCSIEA-------AKIMREAAVAAGAPEGLIQ---WI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 308 P-PTenDDSANYFTSHPGFKHITFIGSQPVahyiLKCAAKSLTPVvveLG---GKDAFIVLDSAKNLDALSSIIMRGTFQ 383
Cdd:cd07122 163 EePS--IELTQELMKHPDVDLILATGGPGM----VKAAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321828 384 -----SSGQNcigierVIVSKENYDDLVKILndrmtanpLRQGSdidHLENVDMGAMISDNRFDELEALVKDAVAKGARL 458
Cdd:cd07122 234 ngticASEQS------VIVDDEIYDEVRAEL--------KRRGA---YFLNEEEKEKLEKALFDDGGTLNPDIVGKSAQK 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321828 459 LQGGSRFKHPKypqghyfqPT--LLVDVTpemKIAQNEVF-----GPILVMMKAKNTDHCVQLANS 517
Cdd:cd07122 297 IAELAGIEVPE--------DTkvLVAEET---GVGPEEPLsreklSPVLAFYRAEDFEEALEKARE 351
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