|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
104-579 |
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: 758.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 104 HCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEI 183
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 184 MATIDKLNWIIRYGPKHLQPSARSGTtnyFMEWYRGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSE 263
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGG---LLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 264 QVIWSSEFFISIVRKCLEVCNEDPDLVQLCYCLPksdkyNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVE 343
Cdd:cd07098 158 QVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLP-----ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 344 LCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTQPLRLGSDmdhlENIDVGA 423
Cdd:cd07098 233 LGGKDPAIVLDD-ADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLD----GDVDVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 424 MISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITI 503
Cdd:cd07098 308 MISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156847713 504 ANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF-TTFYVRQTPFGGISGSGSGKFGSKEGLLSLCYTKSISFN 579
Cdd:cd07098 388 ANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTED 464
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
95-549 |
9.45e-112 |
|
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: 342.97 E-value: 9.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 95 PSQPNIIQSHCPATGQHLSSYlPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGK 173
Cdd:pfam00171 3 DSESETIEVINPATGEVIATV-PAATaEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 174 TMLDAsLGEIMATIDKLNWIIRYGpKHLQPSARSGTTNYFmewyrgTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFT 253
Cdd:pfam00171 82 PLAEA-RGEVDRAIDVLRYYAGLA-RRLDGETLPSDPGRL------AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 254 GNAIIVKCSEQVIWSSEFFISIVRKClevcNEDPDLVQLcycLPKSDKyNATNYFISHPGFKHITFIGRKTVANKILNCA 333
Cdd:pfam00171 154 GNTVVLKPSELTPLTALLLAELFEEA----GLPAGVLNV---VTGSGA-EVGEALVEHPDVRKVSFTGSTAVGRHIAEAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 334 AESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDM 413
Cdd:pfam00171 226 AQNLKRVTLELGGKNPLIVLED-ADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK--LKVGDPL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 414 DhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGsrynHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMK 493
Cdd:pfam00171 303 D--PDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGG----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIR 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 156847713 494 ANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVRQTP 549
Cdd:pfam00171 377 FKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLP 432
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
87-549 |
1.60e-98 |
|
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: 309.36 E-value: 1.60e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 87 LVNTEIIDPSQPNIIQSHCPATGQHLSSYlPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIAR 165
Cdd:COG1012 9 FIGGEWVAAASGETFDVINPATGEVLARV-PAATaEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 166 VTCRDTGKTMLDAsLGEIMATIDKLNWIIRYGPKHL---QPSARSGTTNYfmewyrgteVHYEPLGVVSSIISWNYPFYN 242
Cdd:COG1012 88 LLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYgetIPSDAPGTRAY---------VRREPLGVVGAITPWNFPLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 243 VISPIISAIFTGNAIIVKCSEQVIWSSEFFIsivrkclEVCNE---DPDLVQLCYCLPKSdkynATNYFISHPGFKHITF 319
Cdd:COG1012 158 AAWKLAPALAAGNTVVLKPAEQTPLSALLLA-------ELLEEaglPAGVLNVVTGDGSE----VGAALVAHPDVDKISF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 320 IGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLK 399
Cdd:COG1012 227 TGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDD-ADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 400 DRLTTqpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynhPNYPQGHYFQPTLLVDVTSDMKI 479
Cdd:COG1012 306 AAAKA--LKVGDPLD--PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRR---PDGEGGYFVEPTVLADVTPDMRI 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 480 ANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVRQTP 549
Cdd:COG1012 379 AREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAP 448
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
124-549 |
3.47e-93 |
|
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: 294.12 E-value: 3.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 124 DEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTmLDASLGEIMATIDKLNWIIRYGPK---H 200
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRlhgE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 201 LQPSARSGTTNYfmewyrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCL 280
Cdd:cd07078 80 VIPSPDPGELAI---------VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 281 EvcneDPDLVQLcycLPkSDKYNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESQkDVS 360
Cdd:cd07078 151 L----PPGVLNV---VT-GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDA-DLD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 361 SVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDA 440
Cdd:cd07078 222 AAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKA--LKVGNPLD--PDTDMGPLISAAQLDRVLAYIEDA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 441 VESGATLICGGSRynhPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNV 520
Cdd:cd07078 298 KAEGAKLLCGGKR---LEGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDL 374
|
410 420
....*....|....*....|....*....
gi 156847713 521 KQCRYVAKKLKTTDVTINDFTTFYVRQTP 549
Cdd:cd07078 375 ERALRVAERLEAGTVWINDYSVGAEPSAP 403
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
104-544 |
6.63e-84 |
|
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: 270.63 E-value: 6.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 104 HCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMlDASLGEI 183
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR-ADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 184 MATIDKLNWIIRYGPKHLQPSARSgtTNYFMEWYRGTeVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSE 263
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVP--TGLLMPNKKAT-VEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 264 QVIWSSEFFisivRKCLEVCNEDPDLVQLCYclpksdKYNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVE 343
Cdd:cd07099 157 VTPLVGELL----AEAWAAAGPPQGVLQVVT------GDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 344 LCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENIDVGA 423
Cdd:cd07099 227 LGGKDPMIVLAD-ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAK--ARALRPGADDI--GDADIGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 424 MISPKTFDSLEELIKDAVESGATLICGGSRYNhpnyPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITI 503
Cdd:cd07099 302 MTTARQLDIVRRHVDDAVAKGAKALTGGARSN----GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIAL 377
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 156847713 504 ANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFY 544
Cdd:cd07099 378 ANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTA 418
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
123-542 |
1.80e-68 |
|
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: 229.27 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 123 IDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTmLDASLGEImatiDKLNWIIRY----GP 198
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKP-IAEARAEV----EKCAWICRYyaenAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 199 KHLQPSARSGTTnyfmewyRGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRK 278
Cdd:cd07100 76 AFLADEPIETDA-------GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 279 ------CLEVCNEDPDLVqlcyclpksdkynatNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIV 352
Cdd:cd07100 149 agfpegVFQNLLIDSDQV---------------EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 353 LESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLttQPLRLGSDMDhlENIDVGAMISPKTFDS 432
Cdd:cd07100 214 LDD-ADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAM--AALKVGDPMD--EDTDLGPLARKDLRDE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 433 LEELIKDAVESGATLICGGSRYNHPnypqGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVG 512
Cdd:cd07100 289 LHEQVEEAVAAGATLLLGGKRPDGP----GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLG 364
|
410 420 430
....*....|....*....|....*....|
gi 156847713 513 TCVFGKNVKQCRYVAKKLKTTDVTINDFTT 542
Cdd:cd07100 365 GSVFTTDLERAERVARRLEAGMVFINGMVK 394
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
81-541 |
3.81e-68 |
|
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: 229.77 E-value: 3.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 81 NWKSKRLvntEIIDPSQPNIIqshcpATGQHLSSylpkynEDIDEMVTIAQNAQEEWAKA-DLDRRLKVLHTLHEYIINN 159
Cdd:cd07082 12 ESSGKTI---EVYSPIDGEVI-----GSVPALSA------LEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 160 QEIIARVTCRDTGKTmLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTNYfmewYRGTEVHY--EPLGVVSSIISWN 237
Cdd:cd07082 78 KEEVANLLMWEIGKT-LKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPG----TKGKIAQVrrEPLGVVLAIGPFN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 238 YPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFIsivrKCLEVCNEDPDLVQLCYcLPKSDkynATNYFISHPGFKHI 317
Cdd:cd07082 153 YPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLA----EAFHDAGFPKGVVNVVT-GRGRE---IGDPLVTHGRIDVI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 318 TFIGRKTVANKILNCAaeSLTPVVVELCGKDSYIVLEsQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQL 397
Cdd:cd07082 225 SFTGSTEVGNRLKKQH--PMKRLVLELGGKDPAIVLP-DADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 398 LKDRLTTqpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRyNHPNYpqghyFQPTLLVDVTSDM 477
Cdd:cd07082 302 LKEEVAK--LKVGMPWD--NGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR-EGGNL-----IYPTLLDPVTPDM 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156847713 478 KIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFT 541
Cdd:cd07082 372 RLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKC 435
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
104-543 |
2.44e-65 |
|
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: 221.73 E-value: 2.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 104 HCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWA-KADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGE 182
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 183 IMATIDKLNWIIRYGPKHLQPSARSGTTNYFMEwYRGTeVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCS 262
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLPVPALRGGP-GRRV-VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 263 EQVIWSSEFFISIVrkclevcnEDPDL----VQLcycLPKSDKYNATnYFISHPGFKHITFIGRKTVANKILNCAAESLT 338
Cdd:cd07089 160 PDTPLSALLLGEII--------AETDLpagvVNV---VTGSDNAVGE-ALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 339 PVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhlEN 418
Cdd:cd07089 228 RVLLELGGKSANIVLDD-ADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEA--LPVGDPAD--PG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 419 IDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDE 498
Cdd:cd07089 303 TVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDD 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 156847713 499 DCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTF 543
Cdd:cd07089 381 EAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGY 425
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
106-540 |
2.49e-65 |
|
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: 221.54 E-value: 2.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSyLPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIM 184
Cdd:cd07103 4 PATGEVIGE-VPDAGaADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 185 ATIDKLNW----IIR-YGpkHLQPSARSGTTNYfmewyrgteVHYEPLGVVSSIISWNYPFYNV---ISPIISAiftGNA 256
Cdd:cd07103 82 YAASFLEWfaeeARRiYG--RTIPSPAPGKRIL---------VIKQPVGVVAAITPWNFPAAMItrkIAPALAA---GCT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 257 IIVKCSEQVIWSSeffISIVRkCLEVCNEDPDLVQLCYCLPKsdkyNATNYFISHPGFKHITFIGRKTVANKILNCAAES 336
Cdd:cd07103 148 VVLKPAEETPLSA---LALAE-LAEEAGLPAGVLNVVTGSPA----EIGEALCASPRVRKISFTGSTAVGKLLMAQAADT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 337 LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhl 416
Cdd:cd07103 220 VKRVSLELGGNAPFIVFDD-ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVER--VKKLKVGNGLD-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 417 ENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANS 496
Cdd:cd07103 295 EGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKR--LGL--GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDT 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 156847713 497 DEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:cd07103 371 EDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTG 414
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
88-538 |
4.59e-64 |
|
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: 218.67 E-value: 4.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 88 VNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVT 167
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 168 CRDTGKTMLDASlGEIMATIDKL----NWIIRYGPKHLqPSARSGTTNYfmewyrgteVHYEPLGVVSSIISWNYPFYNV 243
Cdd:cd07088 82 VEEQGKTLSLAR-VEVEFTADYIdymaEWARRIEGEII-PSDRPNENIF---------IFKVPIGVVAGILPWNFPFFLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 244 ISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKClevcnEDPDLVQLCYCLPKSDkynATNYFISHPGFKHITFIGRK 323
Cdd:cd07088 151 ARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEA-----GLPAGVLNIVTGRGSV---VGDALVAHPKVGMISLTGST 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 324 TVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLt 403
Cdd:cd07088 223 EAGQKIMEAAAENITKVSLELGGKAPAIVMKD-ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKM- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 404 tQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynhPNYPQGHYFQPTLLVDVTSDMKIANSD 483
Cdd:cd07088 301 -KAVKVGDPFD--AATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKR---PEGEKGYFYEPTVLTNVRQDMEIVQEE 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 156847713 484 LFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07088 375 IFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
104-539 |
3.55e-62 |
|
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: 212.94 E-value: 3.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 104 HCPATGQHLSSyLPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGE 182
Cdd:cd07101 1 EAPFTGEPLGE-LPQSTpADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHA-FEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 183 IMATIDKLNWIIRYGPKHLQPSARSGTTNYFMEwyrgTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCS 262
Cdd:cd07101 79 VLDVAIVARYYARRAERLLKPRRRRGAIPVLTR----TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 263 EQVIWSSeffiSIVRKCLEVCNEDPDLVQLCyCLPKSDKYNAtnyFISHPGFkhITFIGRKTVANKILNCAAESLTPVVV 342
Cdd:cd07101 155 SQTALTA----LWAVELLIEAGLPRDLWQVV-TGPGSEVGGA---IVDNADY--VMFTGSTATGRVVAERAGRRLIGCSL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 343 ELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDHleNIDVG 422
Cdd:cd07101 225 ELGGKNPMIVLED-ADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVAR--TRALRLGAALDY--GPDMG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 423 AMISPKTFDSLEELIKDAVESGATLICGGSRynHPNYpqGHYF-QPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCI 501
Cdd:cd07101 300 SLISQAQLDRVTAHVDDAVAKGATVLAGGRA--RPDL--GPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAI 375
|
410 420 430
....*....|....*....|....*....|....*...
gi 156847713 502 TIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:cd07101 376 ELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE 413
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
130-549 |
3.69e-62 |
|
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: 210.55 E-value: 3.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 130 AQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLdASLGEIMATIDKLNWIIRYGPKHLQPSARSGT 209
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 210 TNyfmewyRGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcnEDPDL 289
Cdd:cd06534 82 PG------GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 290 VQLcycLPkSDKYNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESQkDVSSVSSLILRT 369
Cdd:cd06534 152 VNV---VP-GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDA-DLDAAVEGAVFG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 370 TFQSSGQSCIGIERIIVSSKRYKQtvqlLKDRLTtqplrlgsdmdhlenidvgamispktfdsleelikdavesgatlic 449
Cdd:cd06534 227 AFFNAGQICTAASRLLVHESIYDE----FVEKLV---------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 450 ggsrynhpnypqghyfqpTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKK 529
Cdd:cd06534 257 ------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAER 318
|
410 420
....*....|....*....|
gi 156847713 530 LKTTDVTINDFTTFYVRQTP 549
Cdd:cd06534 319 LRAGTVYINDSSIGVGPEAP 338
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
103-546 |
1.05e-61 |
|
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: 212.04 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 103 SHCPATGQHLSSyLPKYNE-DIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLG 181
Cdd:cd07093 1 NFNPATGEVLAK-VPEGGAaEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 182 EIMATIDKLNW---IIRYGPKHLQPSARsGTTNYfmewyrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:cd07093 80 DIPRAAANFRFfadYILQLDGESYPQDG-GALNY---------VLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEqviWSSeffISIVRKClEVCNED--PD----LVQlcyclpkSDKYNATNYFISHPGFKHITFIGRKTVANKILNC 332
Cdd:cd07093 150 LKPSE---WTP---LTAWLLA-ELANEAglPPgvvnVVH-------GFGPEAGAALVAHPDVDLISFTGETATGRTIMRA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 333 AAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSD 412
Cdd:cd07093 216 AAPNLKPVSLELGGKNPNIVFAD-ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVER--AKALKVGDP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 413 MDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVM 492
Cdd:cd07093 293 LD--PDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVI 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 156847713 493 KANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINdftTFYVR 546
Cdd:cd07093 371 PFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN---CWLVR 421
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
106-540 |
2.08e-61 |
|
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: 210.94 E-value: 2.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWA-KADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASlGEIM 184
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 185 A----------TIDKLNW-IIRYGPkhlqpsarsGTTNYfmewyrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFT 253
Cdd:cd07109 83 AaaryfeyyggAADKLHGeTIPLGP---------GYFVY---------TVREPHGVTGHIIPWNYPLQITGRSVAPALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 254 GNAIIVKCSEQVIWSSeffISIVRKCLEVCnedpdlvqlcycLPKSdKYN--------ATNYFISHPGFKHITFIGRKTV 325
Cdd:cd07109 145 GNAVVVKPAEDAPLTA---LRLAELAEEAG------------LPAG-ALNvvtglgaeAGAALVAHPGVDHISFTGSVET 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 326 ANKILNCAAESLTPVVVELCGKDSYIVLeSQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQ 405
Cdd:cd07109 209 GIAVMRAAAENVVPVTLELGGKSPQIVF-ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVER--FR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 406 PLRLGSDmdhLENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnYPQGHYFQPTLLVDVTSDMKIANSDLF 485
Cdd:cd07109 286 ALRVGPG---LEDPDLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIF 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 156847713 486 GPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:cd07109 362 GPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNY 416
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
122-541 |
7.82e-59 |
|
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: 203.53 E-value: 7.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 122 DIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASlGEIMATIDKL----NWIIRYG 197
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAA-FEVGAAIAILreaaGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 198 PKHLqPSARSGTTNYfmeWYRgtevhyEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISivr 277
Cdd:cd07104 80 GEIL-PSDVPGKESM---VRR------VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIA--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 278 KCLEVCNEDPDLVQLCYCLPKSdkynATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqK 357
Cdd:cd07104 147 EIFEEAGLPKGVLNVVPGGGSE----IGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDD-A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 358 DVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELI 437
Cdd:cd07104 222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAK--AKALPVGDPRD--PDTVIGPLINERQVDRVHAIV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 438 KDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFG 517
Cdd:cd07104 298 EDAVAAGARLLTGGTY-------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFT 370
|
410 420
....*....|....*....|....
gi 156847713 518 KNVKQCRYVAKKLKTTDVTINDFT 541
Cdd:cd07104 371 RDLERAMAFAERLETGMVHINDQT 394
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
106-538 |
8.34e-59 |
|
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: 203.91 E-value: 8.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASlGEIMA 185
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEVGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDklnWI-----IRYGPKHLQPSARsgttnyfmewyRGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVK 260
Cdd:cd07106 83 AVA---WLrytasLDLPDEVIEDDDT-----------RRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 261 cseqviwSSEFFISIVRKCLEVCNE--DPDLVQLcycLPKSDKYNA--TnyfiSHPGFKHITFIGRKTVANKILNCAAES 336
Cdd:cd07106 149 -------PSPFTPLCTLKLGELAQEvlPPGVLNV---VSGGDELGPalT----SHPDIRKISFTGSTATGKKVMASAAKT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 337 LTPVVVELCGKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTQPLRLGSDmdhl 416
Cdd:cd07106 215 LKRVTLELGGNDAAIVLPDV-DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLD---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 417 ENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnypqGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANS 496
Cdd:cd07106 290 PGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGP----GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSD 365
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 156847713 497 DEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07106 366 EDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN 407
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
93-541 |
1.48e-58 |
|
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: 203.96 E-value: 1.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 93 IDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEE--WAKADLDRRLKVLHTLHEYIINNQEIIARVTCRD 170
Cdd:cd07139 8 VAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 171 TGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTnyfmewYRGTEVHYEPLGVVSSIISWNYPFYNVISPIISA 250
Cdd:cd07139 88 NGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSG------GGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 251 IFTGNAIIVKCS-EQVIWSSEFfisivrkcLEVCNE---DPDLVQLcycLPkSDKyNATNYFISHPGFKHITFIGRKTVA 326
Cdd:cd07139 162 LAAGCTVVLKPSpETPLDAYLL--------AEAAEEaglPPGVVNV---VP-ADR-EVGEYLVRHPGVDKVSFTGSTAAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 327 NKILNCAAESLTPVVVELCGKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqp 406
Cdd:cd07139 229 RRIAAVCGERLARVTLELGGKSAAIVLDDA-DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAA-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 407 LRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnyPQGHYFQPTLLVDVTSDMKIANSDLFG 486
Cdd:cd07139 306 LKVGDPLD--PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGL--DRGWFVEPTLFADVDNDMRIAQEEIFG 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 156847713 487 PILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFT 541
Cdd:cd07139 382 PVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR 436
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
87-538 |
1.20e-57 |
|
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: 201.53 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 87 LVNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARV 166
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 167 TCRDTGKTMLDASLGEIMATIDKLNW---IIRygpkhlqpsARSGTTNYFMEWYRGTEVHyEPLGVVSSIISWNYPFYNV 243
Cdd:cd07117 84 ETLDNGKPIRETRAVDIPLAADHFRYfagVIR---------AEEGSANMIDEDTLSIVLR-EPIGVVGQIIPWNFPFLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 244 ISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLE--VCNedpdlvqlcycLPKSDKYNATNYFISHPGFKHITFIG 321
Cdd:cd07117 154 AWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPkgVVN-----------IVTGKGSKSGEYLLNHPGLDKLAFTG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 322 RKTVANKILNCAAESLTPVVVELCGKDSYIVLESQKDVSSVSSLILRTTFqSSGQSCIGIERIIVSSKRYKQTVQLLKDR 401
Cdd:cd07117 223 STEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILF-NQGQVCCAGSRIFVQEGIYDEFVAKLKEK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 402 LttQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIAN 481
Cdd:cd07117 302 F--ENVKVGNPLD--PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQ 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 156847713 482 SDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07117 378 EEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN 434
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
106-543 |
1.30e-57 |
|
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: 201.04 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSsYLPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDaSLGEIM 184
Cdd:cd07145 6 PANGEVID-TVPSLSrEEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ-SRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 185 ATIDKLnwiirygpKHLQPSARSGTTNYF-MEWYRGTEVHY-----EPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:cd07145 84 RTIRLF--------KLAAEEAKVLRGETIpVDAYEYNERRIaftvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEQVIWSSEFFISIVrkclevcnEDPDLVQLCYCLPKSDKYNATNYFISHPGFKHITFIGRKTVANKILNCAAESLT 338
Cdd:cd07145 156 VKPSSNTPLTAIELAKIL--------EEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 339 PVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlEN 418
Cdd:cd07145 228 KVALELGGSDPMIVLKD-ADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEK--VKKLKVGDPLD--ES 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 419 IDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynhpnyPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDE 498
Cdd:cd07145 303 TDLGPLISPEAVERMENLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 156847713 499 DCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTF 543
Cdd:cd07145 377 EAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRF 421
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
90-539 |
2.53e-57 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 202.03 E-value: 2.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 90 TEIIDPSQPNIIQSHCPATGQHLSSyLPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTC 168
Cdd:PRK09407 23 TARVDGAAGPTREVTAPFTGEPLAT-VPVSTaADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 169 RDTGKTMLDAsLGEIMATIDKLNWIIRYGPKHLQPSARSG-----TTnyfmewyrgTEVHYEPLGVVSSIISWNYPFYNV 243
Cdd:PRK09407 102 LETGKARRHA-FEEVLDVALTARYYARRAPKLLAPRRRAGalpvlTK---------TTELRQPKGVVGVISPWNYPLTLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 244 ISPIISAIFTGNAIIVKCSEQVIWSSeffiSIVRKCLEVCNEDPDLVQLCyCLPKSDKYNAtnyFISHPgfKHITFIGR- 322
Cdd:PRK09407 172 VSDAIPALLAGNAVVLKPDSQTPLTA----LAAVELLYEAGLPRDLWQVV-TGPGPVVGTA---LVDNA--DYLMFTGSt 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 323 ---KTVANKilncAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLK 399
Cdd:PRK09407 242 atgRVLAEQ----AGRRLIGFSLELGGKNPMIVLDD-ADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 400 DRltTQPLRLGSDMDHleNIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNYpqGHYF-QPTLLVDVTSDMK 478
Cdd:PRK09407 317 AA--VRAMRLGAGYDY--SADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKA--RPDL--GPLFyEPTVLTGVTPDME 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156847713 479 IANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:PRK09407 389 LAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNE 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
106-538 |
3.21e-57 |
|
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: 199.89 E-value: 3.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMA 185
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDklnwIIRY--GpkhLQPSARsGTTNYFMEwyrgTEVHY---EPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVK 260
Cdd:cd07108 84 LAD----LFRYfgG---LAGELK-GETLPFGP----DVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 261 CSEQVIWSseffisiVRKCLEVCNED-PDLVQLCYCLPKSDKYNAtnyFISHPGFKHITFIGRKTVANKILNCAAESLTP 339
Cdd:cd07108 152 AAEDAPLA-------VLLLAEILAQVlPAGVLNVITGYGEECGAA---LVDHPDVDKVTFTGSTEVGKIIYRAAADRLIP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 340 VVVELCGKDSYIVLESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhlENI 419
Cdd:cd07108 222 VSLELGGKSPMIVFPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSK--LKIGDPLD--EAT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 420 DVGAMISPKTFDSLEELIKDAVE-SGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDE 498
Cdd:cd07108 298 DIGAIISEKQFAKVCGYIDLGLStSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDED 377
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 156847713 499 DCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07108 378 EVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVN 417
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
131-539 |
3.37e-56 |
|
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: 196.29 E-value: 3.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 131 QNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTT 210
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 211 NYFmewyrGT--EVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcneDPD 288
Cdd:cd07134 88 LLF-----GTksKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAF-----DED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 289 LVQLCyclpkSDKYNATNYFISHPgFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILR 368
Cdd:cd07134 158 EVAVF-----EGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDET-ADLKKAAKKIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 369 TTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTQplrLGSDMDHLENIDVGAMISPKTFDSLEELIKDAVESGATLI 448
Cdd:cd07134 231 GKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKF---YGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 449 CGGSRynhpnYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAK 528
Cdd:cd07134 308 FGGQF-----DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLA 382
|
410
....*....|.
gi 156847713 529 KLKTTDVTIND 539
Cdd:cd07134 383 RTSSGGVVVND 393
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
103-540 |
7.16e-56 |
|
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: 196.23 E-value: 7.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 103 SHCPATGQHLSSyLPKYN-EDIDEMVTIAQNAQE--EWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTmldas 179
Cdd:cd07114 1 SINPATGEPWAR-VPEASaADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 180 lgeimatIDKLNWIIRYGPKHLQ--------------PSARSGTTNYFMewyrgtevhYEPLGVVSSIISWNYPFYNVIS 245
Cdd:cd07114 75 -------IRETRAQVRYLAEWYRyyagladkiegaviPVDKGDYLNFTR---------REPLGVVAAITPWNSPLLLLAK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 246 PIISAIFTGNAIIVKCSEQVIWSSeffisivrkcLEvcnedpdLVQLCY--CLPK-------SDKYNATNYFISHPGFKH 316
Cdd:cd07114 139 KLAPALAAGNTVVLKPSEHTPAST----------LE-------LAKLAEeaGFPPgvvnvvtGFGPETGEALVEHPLVAK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 317 ITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQ 396
Cdd:cd07114 202 IAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD-ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 397 LLKDRltTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSD 476
Cdd:cd07114 281 RLVAR--ARAIRVGDPLD--PETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTND 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156847713 477 MKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:cd07114 357 MRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTY 420
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
85-538 |
1.55e-54 |
|
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: 193.12 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 85 KRLVNTEIIDPSQPNIIQSHCPATGQ-----HLSSylpkyNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINN 159
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEviarvPLAT-----AEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 160 QEIIARVTCRDTGKTMLDAsLGEIMATIDKLNWIIryGPKHLQ-----PSARSGTTNYFMewyrgtevhYEPLGVVSSII 234
Cdd:cd07085 77 LDELARLITLEHGKTLADA-RGDVLRGLEVVEFAC--SIPHLLkgeylENVARGIDTYSY---------RQPLGVVAGIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 235 SWNYPfynVISP---IISAIFTGNAIIVKCSEQVIWSSEFFisivrkcLEVCNED--PD-LVQLCYClpksDKyNATNYF 308
Cdd:cd07085 145 PFNFP---AMIPlwmFPMAIACGNTFVLKPSERVPGAAMRL-------AELLQEAglPDgVLNVVHG----GK-EAVNAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 309 ISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSS 388
Cdd:cd07085 210 LDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPD-ADLEQTANALVGAAFGAAGQRCMALSVAVAVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 389 KRYKQTVQLLKDRLttQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPT 468
Cdd:cd07085 289 DEADEWIPKLVERA--KKLKVGAGDD--PGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPT 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 469 LLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07085 365 ILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN 434
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
121-549 |
3.33e-53 |
|
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: 188.96 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIMATIDKLnwiirygpkh 200
Cdd:cd07149 21 EDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA-RKEVDRAIETL---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 201 lQPSARSGTTNYF----MEWYRGTE--VHY---EPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEF 271
Cdd:cd07149 90 -RLSAEEAKRLAGetipFDASPGGEgrIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 272 FISIVRKC------LEVCNEDPDLVqlcyclpksdkynaTNYFISHPGFKHITFIGRKTVANKILNCAAesLTPVVVELC 345
Cdd:cd07149 169 LAELLLEAglpkgaLNVVTGSGETV--------------GDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 346 GKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENIDVGAMI 425
Cdd:cd07149 233 SNAAVIVDADA-DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAA--TKKLVVGDPLD--EDTDVGPMI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 426 SPKTFDSLEELIKDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIAN 505
Cdd:cd07149 308 SEAEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAN 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 156847713 506 AAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVRQTP 549
Cdd:cd07149 381 DSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHMP 424
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
106-509 |
4.84e-53 |
|
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: 189.00 E-value: 4.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIM 184
Cdd:cd07097 21 PSDTSDVVGKYARASaEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEA-RGEVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 185 ATIDklnwIIRY-------GPKHLQPSARSGTtnyfmewyrGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAI 257
Cdd:cd07097 100 RAGQ----IFRYyagealrLSGETLPSTRPGV---------EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 258 IVKCSEQVIWSSEFFISIVRKC---LEVCNedpdLVqlcyCLPKSDKYNAtnyFISHPGFKHITFIGRKTVANKILNCAA 334
Cdd:cd07097 167 VFKPAELTPASAWALVEILEEAglpAGVFN----LV----MGSGSEVGQA---LVEHPDVDAVSFTGSTAVGRRIAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 335 ESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMD 414
Cdd:cd07097 236 ARGARVQLEMGGKNPLVVLDD-ADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVER--TKALKVGDALD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 415 hlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYpqGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKA 494
Cdd:cd07097 313 --EGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDE--GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV 388
|
410
....*....|....*
gi 156847713 495 NSDEDCITIANAAPY 509
Cdd:cd07097 389 RDYDEALAIANDTEF 403
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
88-539 |
6.45e-53 |
|
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: 188.48 E-value: 6.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 88 VNTEIIDPSQPNIIQSHCPATGQ-----HLSSylpkyNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEI 162
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEvigtvPLGT-----AADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 163 IARVTCRDTGktmldaslgeimATIDKLNWI-IRYGPKHLQpSARSGTTNYFMEWYRG-TEVHYEPLGVVSSIISWNYPF 240
Cdd:cd07138 78 LAQAITLEMG------------APITLARAAqVGLGIGHLR-AAADALKDFEFEERRGnSLVVREPIGVCGLITPWNWPL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 241 YNVISPIISAIFTGNAIIVKCSEQVIWSSEFFIsivrkclEVCNED--PDLVqlcyclpksdkYNATN--------YFIS 310
Cdd:cd07138 145 NQIVLKVAPALAAGCTVVLKPSEVAPLSAIILA-------EILDEAglPAGV-----------FNLVNgdgpvvgeALSA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 311 HPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKR 390
Cdd:cd07138 207 HPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDA-DLEKAVPRGVAACFANSGQSCNAPTRMLVPRSR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 391 YKQTVQLLKDrlTTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSryNHP-NYPQGHYFQPTL 469
Cdd:cd07138 286 YAEAEEIAAA--AAEAYVVGDPRD--PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGP--GRPeGLERGYFVKPTV 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 470 LVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:cd07138 360 FADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING 429
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
87-538 |
1.19e-52 |
|
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: 187.94 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 87 LVNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARV 166
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 167 TCRDTGKTMLDASLGEIMATIDKLNW---IIRygpkhlqpsARSGTTNYFMEWYRGTEVHyEPLGVVSSIISWNYPFYNV 243
Cdd:cd07559 84 ETLDNGKPIRETLAADIPLAIDHFRYfagVIR---------AQEGSLSEIDEDTLSYHFH-EPLGVVGQIIPWNFPLLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 244 ISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLEvcnedPDLVQLCYCL-PKSDKYNAtnyfiSHPGFKHITFIGR 322
Cdd:cd07559 154 AWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLP-----KGVVNVVTGFgSEAGKPLA-----SHPRIAKLAFTGS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 323 KTVANKILNCAAESLTPVVVELCGKDSYIVLEsqkDVSSVSSLILRTTFQ-------SSGQSCIGIERIIVSSKRYKQTV 395
Cdd:cd07559 224 TTVGRLIMQYAAENLIPVTLELGGKSPNIFFD---DAMDADDDFDDKAEEgqlgfafNQGEVCTCPSRALVQESIYDEFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 396 QLLKDRltTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTS 475
Cdd:cd07559 301 ERAVER--FEAIKVGNPLD--PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNN 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156847713 476 DMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07559 377 DMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN 439
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
91-541 |
2.14e-52 |
|
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: 187.13 E-value: 2.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 91 EIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRD 170
Cdd:cd07151 2 EWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 171 TGKTMLDAS--LGEIMATIDK-LNWIIRYGPKHLqPSARSGTTNYFmewYRgtevhyEPLGVVSSIISWNYPFYNVISPI 247
Cdd:cd07151 82 SGSTRIKANieWGAAMAITREaATFPLRMEGRIL-PSDVPGKENRV---YR------EPLGVVGVISPWNFPLHLSMRSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 248 ISAIFTGNAIIVKCSEQVIWSSEFFISivrKCLEVCNedpdlvqlcycLPK-------SDKYNATNYFISHPGFKHITFI 320
Cdd:cd07151 152 APALALGNAVVLKPASDTPITGGLLLA---KIFEEAG-----------LPKgvlnvvvGAGSEIGDAFVEHPVPRLISFT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 321 GRKTVANKILNCAAESLTPVVVELCGKDSYIVLESQKDVSSVSSLILrTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKD 400
Cdd:cd07151 218 GSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVF-GKFLHQGQICMAINRIIVHEDVYDEFVEKFVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 401 RLTTqpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSrynhpnyPQGHYFQPTLLVDVTSDMKIA 480
Cdd:cd07151 297 RVKA--LPYGDPSD--PDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIA 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156847713 481 NSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFT 541
Cdd:cd07151 366 REEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQP 426
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
88-542 |
2.34e-52 |
|
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: 187.35 E-value: 2.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 88 VNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNA-QEEWA-KADLDRRLKVLHTLHEYIINNQEIIAR 165
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 166 VTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTnyfmewyRGTEVHYEPLGVVSSIISWNYPFYNVIS 245
Cdd:cd07143 91 IEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIK-------KLTYTRHEPIGVCGQIIPWNFPLLMCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 246 PIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKClevcNEDPDLVQLCyclpKSDKYNATNYFISHPGFKHITFIGRKTV 325
Cdd:cd07143 164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVV----SGYGRTCGNAISSHMDIDKVAFTGSTLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 326 ANKILNCAAES-LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltT 404
Cdd:cd07143 236 GRKVMEAAAKSnLKKVTLELGGKSPNIVFDD-ADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEK--A 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 405 QPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNypQGHYFQPTLLVDVTSDMKIANSDL 484
Cdd:cd07143 313 KKLKVGDPFA--EDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKR--HGN--EGYFIEPTIFTDVTEDMKIVKEEI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 156847713 485 FGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTT 542
Cdd:cd07143 387 FGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNL 444
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
106-538 |
2.85e-52 |
|
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: 186.30 E-value: 2.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTmLDASLGEIMA 185
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP-IAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDKLNWIIRYGPKHLQPSaRSGTTNYFMEWYRgtevhYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQV 265
Cdd:cd07102 82 MLERARYMISIAEEALADI-RVPEKDGFERYIR-----REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 266 IWSSEFFISIVRKC-LEvcnedPDLVQlcYCLPKSDkynATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVEL 344
Cdd:cd07102 156 PLCGERFAAAFAEAgLP-----EGVFQ--VLHLSHE---TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 345 CGKDSYIVLESQKDVSSVSSLIlRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDrlTTQPLRLGSDMDhlENIDVGAM 424
Cdd:cd07102 226 GGKDPAYVRPDADLDAAAESLV-DGAFFNSGQSCCSIERIYVHESIYDAFVEAFVA--VVKGYKLGDPLD--PSTTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 425 ISPKTFDSLEELIKDAVESGATLICGGSRYNHPNyPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIA 504
Cdd:cd07102 301 VSARAADFVRAQIADAIAKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALM 379
|
410 420 430
....*....|....*....|....*....|....
gi 156847713 505 NAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07102 380 NDSEYGLTASVWTKDIARAEALGEQLETGTVFMN 413
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
91-549 |
8.20e-52 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 185.40 E-value: 8.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 91 EIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRD 170
Cdd:TIGR01804 5 EYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 171 TGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTNYfmewyrgTEVHYEPLGVVSSIISWNYPFYNVISPIISA 250
Cdd:TIGR01804 85 TGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSF-------AYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 251 IFTGNAIIVKCSEQVIWSSeffisivRKCLEVCNED--PDLVqlcYCLPKSDKYNATNYFISHPGFKHITFIGRKTVANK 328
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTA-------LKVAEIMEEAglPKGV---FNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 329 ILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLR 408
Cdd:TIGR01804 228 IMAAAAGHLKHVTMELGGKSPLIVFDD-ADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVER--TERIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 409 LGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPI 488
Cdd:TIGR01804 305 LGDPFD--EATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPV 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156847713 489 LLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVrQTP 549
Cdd:TIGR01804 383 MTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPA-EAP 442
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
106-544 |
8.59e-52 |
|
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: 185.27 E-value: 8.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMlDASLGEIMA 185
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPV-SAMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDKLNWI-----------IRYGPKHLQPSARsgttnyfmewyrgtevhyEPLGVVSSIISWNYPFYNVISPIISAIFTG 254
Cdd:cd07107 83 AAALLDYFaglvtelkgetIPVGGRNLHYTLR------------------EPYGVVARIVAFNHPLMFAAAKIAAPLAAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 255 NAIIVKCSEQVIWSSEFFISIVRKCLEvcnedPDLVQLcycLPkSDKYNATNYFISHPGFKHITFIGRKTVANKILNCAA 334
Cdd:cd07107 145 NTVVVKPPEQAPLSALRLAELAREVLP-----PGVFNI---LP-GDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 335 ESLTPVVVELCGKDSYIVLESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMD 414
Cdd:cd07107 216 EGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAA--IKVGDPTD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 415 hlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKA 494
Cdd:cd07107 294 --PATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRW 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 156847713 495 NSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFY 544
Cdd:cd07107 372 RDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHF 421
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
106-546 |
2.08e-51 |
|
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: 183.79 E-value: 2.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMA 185
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDKL----NWIIRYGPKHLqpSARSGTTNYfmewyrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKC 261
Cdd:cd07115 84 AADTFryyaGWADKIEGEVI--PVRGPFLNY---------TVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 262 SEQVIWSSeffISIVRKCLEVcNEDPDLVQLcycLPKSDKyNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVV 341
Cdd:cd07115 153 AELTPLSA---LRIAELMAEA-GFPAGVLNV---VTGFGE-VAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 342 VELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENIDV 421
Cdd:cd07115 225 LELGGKSANIVFAD-ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSL--ARSLRPGDPLD--PKTQM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 422 GAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnypqGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCI 501
Cdd:cd07115 300 GPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGAR----GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEAL 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 156847713 502 TIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVR 546
Cdd:cd07115 376 RIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDPG 420
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
106-540 |
2.37e-51 |
|
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: 184.04 E-value: 2.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLgEIMA 185
Cdd:cd07090 4 PATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV-DIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDKLNW----IIRYGPKHLQpsarsgttnyfmewYRGTEVHY---EPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:cd07090 83 SADCLEYyaglAPTLSGEHVP--------------LPGGSFAYtrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEQVIWSSEFFISIVRK------CLEVCNEDPDLVQlcyclpksdkynatnYFISHPGFKHITFIGRKTVANKILNC 332
Cdd:cd07090 149 YKPSPFTPLTALLLAEILTEaglpdgVFNVVQGGGETGQ---------------LLCEHPDVAKVSFTGSVPTGKKVMSA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 333 AAESLTPVVVELCGKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSD 412
Cdd:cd07090 214 AAKGIKHVTLELGGKSPLIIFDDA-DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVER--TKKIRIGDP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 413 MDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYN-HPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLV 491
Cdd:cd07090 291 LD--EDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSI 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 156847713 492 MKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:cd07090 369 LPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTY 417
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
121-541 |
3.23e-50 |
|
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: 180.60 E-value: 3.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIMATIDKL----NWIIRY 196
Cdd:cd07150 21 QDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFETTFTPELLraaaGECRRV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 197 GPKHLqPSARSGTTNYFMEwyrgtevhyEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIV 276
Cdd:cd07150 100 RGETL-PSDSPGTVSMSVR---------RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 277 rkclEVCNEDPDLVQLCYCLPKSdkynATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESq 356
Cdd:cd07150 170 ----EEAGLPKGVFNVVTGGGAE----VGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 357 KDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVqllkDRLTTQPLRLGSDMDHLENIDVGAMISPKTFDSLEEL 436
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFV----KKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 437 IKDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVF 516
Cdd:cd07150 317 VEDAVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420
....*....|....*....|....*
gi 156847713 517 GKNVKQCRYVAKKLKTTDVTINDFT 541
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPT 414
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
88-538 |
4.51e-50 |
|
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: 181.07 E-value: 4.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 88 VNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNA-QEEWAKADLDRRLKVLHTLHEYIINNQEIIARV 166
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 167 TCRDTGKTMLDASLGEImatiDKLNWIIRY---GPKHLQPSARSGTTNYFMEWYRgtevhyEPLGVVSSIISWNYPFYNV 243
Cdd:cd07144 92 EALDSGKPYHSNALGDL----DEIIAVIRYyagWADKIQGKTIPTSPNKLAYTLH------EPYGVCGQIIPWNYPLAMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 244 ISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKC---LEVCNEDPDLVQLcyclpksdkynATNYFISHPGFKHITFI 320
Cdd:cd07144 162 AWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgfpPGVVNIIPGYGAV-----------AGSALAEHPDVDKIAFT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 321 GRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKD 400
Cdd:cd07144 231 GSTATGRLVMKAAAQNLKAVTLECGGKSPALVFED-ADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 401 RlTTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNYP-QGHYFQPTLLVDVTSDMKI 479
Cdd:cd07144 310 H-VKQNYKVGSPFD--DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK--APEGLgKGYFIPPTIFTDVPQDMRI 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 480 ANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07144 385 VKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWIN 443
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
91-545 |
6.52e-50 |
|
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: 180.58 E-value: 6.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 91 EIIDPSQPNIIqSHCPATGQhlssylpkynEDIDEMVTIAQNA--QEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTC 168
Cdd:cd07119 16 DIINPANGEVI-ATVPEGTA----------EDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 169 RDTGKTmldasLGEIMATIDKLNWIIRYGPKHL-QPSARSGTTNYFMEWYrgtEVHyEPLGVVSSIISWNYPFYNVISPI 247
Cdd:cd07119 85 LNTGKT-----LRESEIDIDDVANCFRYYAGLAtKETGEVYDVPPHVISR---TVR-EPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 248 ISAIFTGNAIIVKCSEQVIWSS-EFFisivrKCLEVCNEDPDLVQLCyCLPKSDkynATNYFISHPGFKHITFIGRKTVA 326
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTiALF-----ELIEEAGLPAGVVNLV-TGSGAT---VGAELAESPDVDLVSFTGGTATG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 327 NKILNCAAESLTPVVVELCGKDSYIVLeSQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLttQP 406
Cdd:cd07119 227 RSIMRAAAGNVKKVALELGGKNPNIVF-ADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERA--KK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 407 LRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFG 486
Cdd:cd07119 304 IKLGNGLD--ADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFG 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 487 PILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYV 545
Cdd:cd07119 382 PVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFA 440
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
122-538 |
6.96e-50 |
|
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: 179.31 E-value: 6.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 122 DIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTM------LDASLGEIMATIDKLNWIIr 195
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAawagfnVDLAAGMLREAASLITQII- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 196 ygpKHLQPSARSGTTNYFMEwyrgtevhyEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISI 275
Cdd:cd07105 80 ---GGSIPSDKPGTLAMVVK---------EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 276 VRK------CLEVCNEDPDlvqlcyclpksDKYNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDS 349
Cdd:cd07105 148 FHEaglpkgVLNVVTHSPE-----------DAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 350 YIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDmdhleniDVGAMISPKT 429
Cdd:cd07105 217 AIVLED-ADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAA--AEKLFAGPV-------VLGSLVSAAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 430 FDSLEELIKDAVESGATLICGGSRynhPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPY 509
Cdd:cd07105 287 ADRVKELVDDALSKGAKLVVGGLA---DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEY 363
|
410 420
....*....|....*....|....*....
gi 156847713 510 AVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07105 364 GLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
87-543 |
8.83e-50 |
|
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: 180.10 E-value: 8.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 87 LVNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEE--WAKADLDRRLKVLHTLHEYIINNQEIIA 164
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 165 RVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKhLQPSARSGTTNYFmewyrgTEVHYEPLGVVSSIISWNYPFYNVI 244
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAGWADK-IQGKTIPIDGNFL------AYTRREPIGVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 245 SPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCL---EVCNedpdlvqlcyCLPKSDKYnATNYFISHPGFKHITFIG 321
Cdd:cd07091 160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGfppGVVN----------IVPGFGPT-AGAAISSHMDVDKIAFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 322 RKTVANKILNCAAES-LTPVVVELCGKDSYIVLES---QKDVSSVSSLIlrttFQSSGQSCIGIERIIVSSKRYKQTVQL 397
Cdd:cd07091 229 STAVGRTIMEAAAKSnLKKVTLELGGKSPNIVFDDadlDKAVEWAAFGI----FFNQGQCCCAGSRIFVQESIYDEFVEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 398 LKDRltTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNypQGHYFQPTLLVDVTSDM 477
Cdd:cd07091 305 FKAR--AEKRVVGDPFD--PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGER--HGS--KGYFIQPTVFTDVKDDM 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156847713 478 KIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTF 543
Cdd:cd07091 377 KIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVF 442
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
106-539 |
4.89e-49 |
|
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: 177.52 E-value: 4.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMA 185
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDKlnwiIRY--GPKHLQPSARSGttnyfmEWYRGTE--VHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKC 261
Cdd:cd07092 84 AVDN----FRFfaGAARTLEGPAAG------EYLPGHTsmIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 262 SEQVIWSSEFFISIVRKCLevcnedPDLVQLCYClpkSDKYNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVV 341
Cdd:cd07092 154 SETTPLTTLLLAELAAEVL------PPGVVNVVC---GGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 342 VELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhlENIDV 421
Cdd:cd07092 225 LELGGKAPVIVFDD-ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSA--IRVGDPDD--EDTEM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 422 GAMISPKTFDSLEELIKDAVEsGATLICGGSRYNHPnypqGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCI 501
Cdd:cd07092 300 GPLNSAAQRERVAGFVERAPA-HARVLTGGRRAEGP----GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAI 374
|
410 420 430
....*....|....*....|....*....|....*...
gi 156847713 502 TIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:cd07092 375 ELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT 412
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
104-554 |
1.26e-48 |
|
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: 176.47 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 104 HCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEI 183
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 184 MATIDKLN----WIIRYGPKHLQPSARSGTTNyfmewyRGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIV 259
Cdd:cd07094 83 DRAIDTLRlaaeEAERIRGEEIPLDATQGSDN------RLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 260 KCSEQVIWSSEFFISIVRKClevcNEDPDLVQLcycLPKSDKYNATNyFISHPGFKHITFIGRKTVANKIlnCAAESLTP 339
Cdd:cd07094 157 KPASKTPLSALELAKILVEA----GVPEGVLQV---VTGEREVLGDA-FAADERVAMLSFTGSAAVGEAL--RANAGGKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 340 VVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENI 419
Cdd:cd07094 227 IALELGGNAPVIVDRD-ADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAA--VKKLKVGDPLD--EDT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 420 DVGAMISPKTFDSLEELIKDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDED 499
Cdd:cd07094 302 DVGPLISEEAAERVERWVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEE 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 156847713 500 CITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVRQTPFGGIS 554
Cdd:cd07094 375 AIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVK 429
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
104-540 |
1.93e-48 |
|
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: 175.99 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 104 HCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEE--WAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTmLDASLG 181
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKP-ISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 182 EIMATIDklnwIIRYGPK-----HLQPSARSGTTNYFMewyrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNA 256
Cdd:cd07118 81 EIEGAAD----LWRYAASlartlHGDSYNNLGDDMLGL-------VLREPIGVVGIITPWNFPFLILSQKLPFALAAGCT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 257 IIVKCSEqviWSSEFFISIVRKCLE------VCNedpdlVQLCYCLPksdkynATNYFISHPGFKHITFIGRKTVANKIL 330
Cdd:cd07118 150 VVVKPSE---FTSGTTLMLAELLIEaglpagVVN-----IVTGYGAT------VGQAMTEHPDVDMVSFTGSTRVGKAIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 331 NCAAESLTPVVVELCGKDSYIVLeSQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLG 410
Cdd:cd07118 216 AAAARNLKKVSLELGGKNPQIVF-ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVAR--SRKVRVG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 411 SDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNypqGHYFQPTLLVDVTSDMKIANSDLFGPILL 490
Cdd:cd07118 293 DPLD--PETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAA---GLFYQPTIFTDVTPDMAIAREEIFGPVLS 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 156847713 491 VMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:cd07118 368 VLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTF 417
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
106-540 |
3.51e-48 |
|
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: 175.48 E-value: 3.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEE--WAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEI 183
Cdd:cd07112 9 PATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 184 MATIDKLNW---II--RYGpkHLQPSARSGTTnyfmewyrgtEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:cd07112 89 PSAANTFRWyaeAIdkVYG--EVAPTGPDALA----------LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEQviwSSeffISIVRkclevcnedpdLVQLCY--CLPKSdKYNATnyfishPGFKH--------------ITFIGR 322
Cdd:cd07112 157 LKPAEQ---SP---LTALR-----------LAELALeaGLPAG-VLNVV------PGFGHtagealglhmdvdaLAFTGS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 323 KTVANKILNCAAES-LTPVVVELCGKDSYIVLESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDR 401
Cdd:cd07112 213 TEVGRRFLEYSGQSnLKRVWLECGGKSPNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 402 LTTqpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNYPQGHYFQPTLLVDVTSDMKIAN 481
Cdd:cd07112 293 ARE--WKPGDPLD--PATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKR--VLTETGGFFVEPTVFDGVTPDMRIAR 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 482 SDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:cd07112 367 EEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCF 425
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
101-544 |
9.52e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 171.07 E-value: 9.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 101 IQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTmLDASL 180
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 181 GEIMATIDKLNWIIRYGPKHLQP----SARSGTTNYFmewyrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNA 256
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADepadAAAVGASRAY--------VRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 257 IIVKCSEQVIWSSEFFISIVRK------CLEVCnedpdlvqlcycLPKSDkynATNYFISHPGFKHITFIGRKTVANKIL 330
Cdd:PRK09406 154 GLLKHASNVPQTALYLADLFRRagfpdgCFQTL------------LVGSG---AVEAILRDPRVAAATLTGSEPAGRAVA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 331 NCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLG 410
Cdd:PRK09406 219 AIAGDEIKKTVLELGGSDPFIVMPS-ADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAA--LRVG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 411 SDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnypqGHYFQPTLLVDVTSDMKIANSDLFGPILL 490
Cdd:PRK09406 296 DPTD--PDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGP----GWFYPPTVITDITPDMRLYTEEVFGPVAS 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 156847713 491 VMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFY 544
Cdd:PRK09406 370 LYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSY 423
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
87-538 |
1.41e-46 |
|
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: 171.38 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 87 LVNTEIIDPSQPNIIQSHCPATG-QHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIAR 165
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 166 VTCRDTGKTmLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTNYFMEWYRgtevhyEPLGVVSSIISWNYPFYNVIS 245
Cdd:cd07131 82 LVTREMGKP-LAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRR------QPIGVVALITPWNFPVAIPSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 246 PIISAIFTGNAIIVKCSEQVIWSSEFFIsivrKCLEVCNEDPDLVQLC--YCLPKSDKynatnyFISHPGFKHITFIGRK 323
Cdd:cd07131 155 KIFPALVCGNTVVFKPAEDTPACALKLV----ELFAEAGLPPGVVNVVhgRGEEVGEA------LVEHPDVDVVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 324 TVANKILNCAAESLTPVVVELCGKDSYIVLESQKDVSSVSSLILrTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRlt 403
Cdd:cd07131 225 EVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALW-SAFGTTGQRCTATSRLIVHESVYDEFLKRFVER-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 404 TQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSD 483
Cdd:cd07131 302 AKRLRVGDGLD--EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 156847713 484 LFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07131 380 IFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN 434
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
140-547 |
2.17e-46 |
|
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: 169.59 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 140 ADLDRRLKVLHTLHEYIINNQEIIARVTCRDTG-KTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGttnyfMEWYR 218
Cdd:cd07133 17 PSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHV-----GLLFL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 219 G--TEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCL---EVC--NEDPDLVQ 291
Cdd:cd07133 92 PakAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFdedEVAvvTGGADVAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 292 lcyclpksdkynatnYFISHPgFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESQKDVSSVSSLILRTTF 371
Cdd:cd07133 172 ---------------AFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 372 qSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTQ-PlrlgsdmDHLENIDVGAMISPKTFDSLEELIKDAVESGATLI-C 449
Cdd:cd07133 236 -NAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyP-------TLADNPDYTSIINERHYARLQGLLEDARAKGARVIeL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 450 GGsryNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKK 529
Cdd:cd07133 308 NP---AGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRR 384
|
410
....*....|....*...
gi 156847713 530 LKTTDVTINDfTTFYVRQ 547
Cdd:cd07133 385 THSGGVTIND-TLLHVAQ 401
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
83-539 |
5.69e-45 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 167.17 E-value: 5.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 83 KSKRLVNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEI 162
Cdd:PLN02278 24 RTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 163 IARVTCRDTGKTMLDAsLGEIMATIDKLNWI----IR-YGPKHLQPSARsgttnyfmewyRGTEVHYEPLGVVSSIISWN 237
Cdd:PLN02278 104 LAQLMTLEQGKPLKEA-IGEVAYGASFLEYFaeeaKRvYGDIIPSPFPD-----------RRLLVLKQPVGVVGAITPWN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 238 YPFYNVISPIISAIFTGNAIIVKCSEQViwsseffiSIVRKCLEVCNED---PDLVqLCYCLPKSDKYNATnyFISHPGF 314
Cdd:PLN02278 172 FPLAMITRKVGPALAAGCTVVVKPSELT--------PLTALAAAELALQagiPPGV-LNVVMGDAPEIGDA--LLASPKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 315 KHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQT 394
Cdd:PLN02278 241 RKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDD-ADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 395 VQLLKDRLttQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNhpnyPQGHYFQPTLLVDVT 474
Cdd:PLN02278 320 AEAFSKAV--QKLVVGDGFE--EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156847713 475 SDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:PLN02278 392 EDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNE 456
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
84-543 |
6.32e-45 |
|
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: 166.52 E-value: 6.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 84 SKRLVNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEE--WAKADLDRRLKVLHTLHEYIINNQE 161
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 162 IIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPK-HlqpsarsGTTNYFMEWYRGTEVHyEPLGVVSSIISWNYPF 240
Cdd:cd07142 84 ELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKiH-------GMTLPADGPHHVYTLH-EPIGVVGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 241 YNVISPIISAIFTGNAIIVKCSEQVIWSSEFfisIVRKCLEVcnEDPDLVqlcycLPKSDKYNATN--YFISHPGFKHIT 318
Cdd:cd07142 156 LMFAWKVGPALACGNTIVLKPAEQTPLSALL---AAKLAAEA--GLPDGV-----LNIVTGFGPTAgaAIASHMDVDKVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 319 FIGRKTVANKILNCAAES-LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQL 397
Cdd:cd07142 226 FTGSTEVGKIIMQLAAKSnLKPVTLELGGKSPFIVCED-ADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 398 LK----DRLTTQPLRLGsdmdhlenIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHpnypQGHYFQPTLLVDV 473
Cdd:cd07142 305 AKaralKRVVGDPFRKG--------VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGS----KGYYIQPTIFSDV 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 474 TSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTF 543
Cdd:cd07142 373 KDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVF 442
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
106-538 |
2.70e-44 |
|
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: 164.45 E-value: 2.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAS--LGEI 183
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 184 MATIDklnwiiRYGPKHLQPSARSGTT-NYFMEWYRGtEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCS 262
Cdd:cd07110 84 AGCFE------YYADLAEQLDAKAERAvPLPSEDFKA-RVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 263 EQVIWSSEFFISIvrkCLEVCNedPDLVqLCYCLPKSDKYNATnyFISHPGFKHITFIGRKTVANKILNCAAESLTPVVV 342
Cdd:cd07110 157 ELTSLTELELAEI---AAEAGL--PPGV-LNVVTGTGDEAGAP--LAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 343 ELCGKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhlENIDVG 422
Cdd:cd07110 229 ELGGKSPIIVFDDA-DLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEA--IRVGDPLE--EGVRLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 423 AMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnyPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCIT 502
Cdd:cd07110 304 PLVSQAQYEKVLSFIARGKEEGARLLCGGRRPAHL--EKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIA 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 156847713 503 IANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07110 382 LANDSEYGLAAAVISRDAERCDRVAEALEAGIVWIN 417
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
141-539 |
3.11e-44 |
|
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: 163.47 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 141 DLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSaRSGTTnyFMEWYRGT 220
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPR-RVSVP--LLLQPAKA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 221 EVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcneDPDLVQLCyclpKSD 300
Cdd:cd07087 95 YVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYF-----DPEAVAVV----EGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 301 KYNATNyFISHPgFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIG 380
Cdd:cd07087 166 VEVATA-LLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKD-ANLEVAARRIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 381 IERIIVSSKRYKQTVQLLKDRLTTQplrLGSDMdhLENIDVGAMISPKTFDSLEELIKDavesgATLICGGSRynhpnYP 460
Cdd:cd07087 243 PDYVLVHESIKDELIEELKKAIKEF---YGEDP--KESPDYGRIINERHFDRLASLLDD-----GKVVIGGQV-----DK 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 461 QGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:cd07087 308 EERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVND 386
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
121-549 |
9.78e-44 |
|
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: 162.80 E-value: 9.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASlGEIMATIDKLNWIIrygpkh 200
Cdd:cd07147 21 DDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GEVARAIDTFRIAA------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 201 lQPSARSGTTNYFMEWYRGTE-----VHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISI 275
Cdd:cd07147 94 -EEATRIYGEVLPLDISARGEgrqglVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 276 VRKC---------LEVCNEDPDlvqlcyclpksdkynatnYFISHPGFKHITFIGRKTVANKILNCAAESltPVVVELCG 346
Cdd:cd07147 173 LAETglpkgafsvLPCSRDDAD------------------LLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 347 KDSYIVlESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENIDVGAMIS 426
Cdd:cd07147 233 NAAVIV-DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVAR--VKALKTGDPKD--DATDVGPMIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 427 PKTFDSLEELIKDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANA 506
Cdd:cd07147 308 ESEAERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVND 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 156847713 507 APYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVRQTP 549
Cdd:cd07147 381 SKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVDHMP 423
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
121-540 |
2.01e-43 |
|
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: 161.62 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKH 200
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 201 LQPSARSGTTNYFMEWyrGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCL 280
Cdd:cd07135 85 AKDEKVKDGPLAFMFG--KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 281 evcneDPDLVQLCYCLPKSdkynaTNYFISHpGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVS 360
Cdd:cd07135 163 -----DPDAFQVVQGGVPE-----TTALLEQ-KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKN-ADLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 361 SVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKdrlTTQPLRLGSDMDHLEniDVGAMISPKTFDSLEELIKda 440
Cdd:cd07135 231 LAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELK---KVLDEFYPGGANASP--DYTRIVNPRHFNRLKSLLD-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 441 vESGATLICGGSRynhpnYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNV 520
Cdd:cd07135 304 -TTKGKVVIGGEM-----DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDK 377
|
410 420
....*....|....*....|
gi 156847713 521 KQCRYVAKKLKTTDVTINDF 540
Cdd:cd07135 378 SEIDHILTRTRSGGVVINDT 397
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
106-549 |
5.37e-42 |
|
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: 158.67 E-value: 5.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQE---EWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGE 182
Cdd:cd07141 29 PATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 183 IMATIDKLNWIIRYGPKHLqpsarsGTT-----NYFmewyrgTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAI 257
Cdd:cd07141 109 LPGAIKVLRYYAGWADKIH------GKTipmdgDFF------TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 258 IVKCSEQVIWSSEFFISIVRKClevcNEDPDLVQLcycLPKsdkYNAT--NYFISHPGFKHITFIGRKTVANKILNCAAE 335
Cdd:cd07141 177 VLKPAEQTPLTALYLASLIKEA----GFPPGVVNV---VPG---YGPTagAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 336 S-LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRY----KQTVQLLKDRLTTQPLRLG 410
Cdd:cd07141 247 SnLKRVTLELGGKSPNIVFAD-ADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYdefvKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 411 SDMdhlenidvGAMISPKTFDSLEELIKDAVESGATLICGGSRynHPNypQGHYFQPTLLVDVTSDMKIANSDLFGPILL 490
Cdd:cd07141 326 TEQ--------GPQIDEEQFKKILELIESGKKEGAKLECGGKR--HGD--KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 491 VMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVrQTP 549
Cdd:cd07141 394 IFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSP-QAP 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
106-539 |
7.41e-42 |
|
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: 157.51 E-value: 7.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEE--WAKaDLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASlGEI 183
Cdd:cd07120 4 PATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-FEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 184 MATIDKLNW---IIRYGPKHLqpsarsgttnyfMEWYRGT--EVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:cd07120 82 SGAISELRYyagLARTEAGRM------------IEPEPGSfsLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEQviwsSEFFISIVRKCLEVCNEDPDLVQLCYCLPKSDkynATNYFISHPGFKHITFIGRKTVANKILNCAAESLT 338
Cdd:cd07120 150 VKPAGQ----TAQINAAIIRILAEIPSLPAGVVNLFTESGSE---GAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 339 PVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhlEN 418
Cdd:cd07120 223 RLGLELGGKTPCIVFDD-ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAA--VKVGPGLD--PA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 419 IDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHpNYPQGHYFQPTLLVDVTSDMKIANSDLFGPIlLVMKANSDE 498
Cdd:cd07120 298 SDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTE-GLAKGAFLRPTLLEVDDPDADIVQEEIFGPV-LTLETFDDE 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 156847713 499 D-CITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:cd07120 376 AeAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND 417
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
101-522 |
8.66e-42 |
|
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: 157.73 E-value: 8.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 101 IQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsL 180
Cdd:cd07086 15 FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEG-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 181 GEIMATIDKLNWII---R--YGpkHLQPSARSGTTNYfMEWyrgtevhyEPLGVVSSIISWNYPF-----YNVIspiisA 250
Cdd:cd07086 94 GEVQEMIDICDYAVglsRmlYG--LTIPSERPGHRLM-EQW--------NPLGVVGVITAFNFPVavpgwNAAI-----A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 251 IFTGNAIIVKCSEQVIWSSEFFISIVRKCLEVCNEDPDLVQLCYClpKSDKYNATnyfISHPGFKHITFIGRKTVANKIL 330
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTG--GGDGGELL---VHDPRVPLVSFTGSTEVGRRVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 331 NCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLG 410
Cdd:cd07086 233 ETVARRFGRVLLELGGNNAIIVMDD-ADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKA--YKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 411 SDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnyPQGHYFQPTLLVDVTSDMKIANSDLFGPILL 490
Cdd:cd07086 310 DPLD--EGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGG--EPGNYVEPTIVTGVTDDARIVQEETFAPILY 385
|
410 420 430
....*....|....*....|....*....|..
gi 156847713 491 VMKANSDEDCITIANAAPYAVGTCVFGKNVKQ 522
Cdd:cd07086 386 VIKFDSLEEAIAINNDVPQGLSSSIFTEDLRE 417
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
84-543 |
1.53e-41 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 158.43 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 84 SKRLVNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEE--WAKADLDRRLKVLHTLHEYIINNQE 161
Cdd:PLN02466 58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 162 IIARVTCRDTGKTMLDASLGEIMATIDklnwIIRY----------------GPKHLQpsarsgttnyfmewyrgteVHYE 225
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKAELPMFAR----LFRYyagwadkihgltvpadGPHHVQ-------------------TLHE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 226 PLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFfisiVRKCLEVCNEDPDLVQLCyclpksDKYNAT 305
Cdd:PLN02466 195 PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALY----AAKLLHEAGLPPGVLNVV------SGFGPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 306 N--YFISHPGFKHITFIGRKTVANKILNCAAES-LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIE 382
Cdd:PLN02466 265 AgaALASHMDVDKLAFTGSTDTGKIVLELAAKSnLKPVTLELGGKSPFIVCED-ADVDKAVELAHFALFFNQGQCCCAGS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 383 RIIVSSKRYKQTVQLLK----DRLTTQPLRLGsdmdhlenIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNhpn 458
Cdd:PLN02466 344 RTFVHERVYDEFVEKAKaralKRVVGDPFKKG--------VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG--- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 459 yPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:PLN02466 413 -SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN 491
|
....*
gi 156847713 539 DFTTF 543
Cdd:PLN02466 492 CFDVF 496
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
121-541 |
1.60e-40 |
|
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: 153.60 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIMATIDKLNWIIRYGPK- 199
Cdd:cd07152 13 ADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA-GFEVGAAIGELHEAAGLPTQp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 200 --HLQPSARsGTTNYfmeWYRgtevhyEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVr 277
Cdd:cd07152 92 qgEILPSAP-GRLSL---ARR------VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 278 kcLEVCNEDPDLVQLcycLPKSDkyNATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqK 357
Cdd:cd07152 161 --FEEAGLPAGVLHV---LPGGA--DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDD-A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 358 DVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELI 437
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAK--AKHLPVGDPAT--GQVALGPLINARQLDRVHAIV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 438 KDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFG 517
Cdd:cd07152 309 DDSVAAGARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIIS 381
|
410 420
....*....|....*....|....
gi 156847713 518 KNVKQCRYVAKKLKTTDVTINDFT 541
Cdd:cd07152 382 RDVGRAMALADRLRTGMLHINDQT 405
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
91-519 |
4.23e-40 |
|
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: 153.53 E-value: 4.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 91 EIIDPSQPN-IIQSHCPATGqhlssylpkynEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEyIINNQ--EIIARVT 167
Cdd:cd07124 49 ESRNPADPSeVLGTVQKATK-----------EEAEAAVQAARAAFPTWRRTPPEERARLLLRAAA-LLRRRrfELAAWMV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 168 cRDTGKTMLDAsLGEIMATIDKLNW----IIRYGPKHLQPsaRSGTTNyfmewyrgtEVHYEPLGVVSSIISWNYPFYNV 243
Cdd:cd07124 117 -LEVGKNWAEA-DADVAEAIDFLEYyareMLRLRGFPVEM--VPGEDN---------RYVYRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 244 ISPIISAIFTGNAIIVKCSEQVIWSSEFFIsivrKCLEVCNEDPDLVQLcycLPKSDKyNATNYFISHPGFKHITFIGRK 323
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLV----EILEEAGLPPGVVNF---LPGPGE-EVGDYLVEHPDVRFIAFTGSR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 324 TVANKILNCAAES------LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQL 397
Cdd:cd07124 256 EVGLRIYERAAKVqpgqkwLKRVIAEMGGKNAIIVDED-ADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLER 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 398 LKDRltTQPLRLGsDMDHLENiDVGAMISPKTFDSLEELIKDAVESGaTLICGGSRYNHPNypQGHYFQPTLLVDVTSDM 477
Cdd:cd07124 335 LVER--TKALKVG-DPEDPEV-YMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAA--EGYFVQPTIFADVPPDH 407
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 156847713 478 KIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKN 519
Cdd:cd07124 408 RLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRS 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
141-539 |
1.30e-39 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 152.11 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 141 DLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPsaRSGTTNyFMEWYRGT 220
Cdd:PTZ00381 27 PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKP--EKVDTV-GVFGPGKS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 221 EVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcneDPDLVQLCyclpkSD 300
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL-----DPSYVRVI-----EG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 301 KYNATNYFISHPgFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVlESQKDVSSVSSLILRTTFQSSGQSCIG 380
Cdd:PTZ00381 174 GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIV-DKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 381 IERIIVSSKRYKQTVQLLKDRLTTQplrLGSDMdhLENIDVGAMISPKTFDSLEELIKDaveSGATLICGGsRYNHPNyp 460
Cdd:PTZ00381 252 PDYVLVHRSIKDKFIEALKEAIKEF---FGEDP--KKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGG-EVDIEN-- 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 461 qgHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:PTZ00381 321 --KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIND 397
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
149-538 |
2.06e-39 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 149.50 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 149 LHTLHEYIINNQEIIARVTCRDTGKTMLDASLgEIMATIDKLN----WIIRYGPKHLQpSARSGTTNYfmewyrgteVHY 224
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDymaeWARRYEGEIIQ-SDRPGENIL---------LFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 225 EPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKClevcnedpdlvqlcyCLPKS----- 299
Cdd:PRK10090 70 RALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI---------------GLPKGvfnlv 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 300 DKYNAT--NYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQS 377
Cdd:PRK10090 135 LGRGETvgQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDD-ADLDLAVKAIVDSRVINSGQV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 378 CIGIERIIVSSKRYKQTVqllkDRLTT--QPLRLGSDMDHlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYN 455
Cdd:PRK10090 214 CNCAERVYVQKGIYDQFV----NRLGEamQAVQFGNPAER-NDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 456 HpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDV 535
Cdd:PRK10090 289 G----KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGET 364
|
...
gi 156847713 536 TIN 538
Cdd:PRK10090 365 YIN 367
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
141-539 |
3.59e-39 |
|
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: 149.96 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 141 DLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQP-SARSGTTNYFMEWYrg 219
Cdd:cd07136 18 DVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPkRVKTPLLNFPSKSY-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 220 teVHYEPLGVVSsIIS-WNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcneDPDLVqlcyCLPK 298
Cdd:cd07136 96 --IYYEPYGVVL-IIApWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETF-----DEEYV----AVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 299 SDKynATNYFISHPGFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSC 378
Cdd:cd07136 164 GGV--EENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDED-ANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 379 IGIERIIVSSKRYKQTVQLLKDRLTTQplrLGSDMdhLENIDVGAMISPKTFDSLEELIKDavesgATLICGGsRYNhpn 458
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKF---YGEDP--LESPDYGRIINEKHFDRLAGLLDN-----GKIVFGG-NTD--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 459 yPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07136 307 -RETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN 385
|
.
gi 156847713 539 D 539
Cdd:cd07136 386 D 386
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
88-543 |
5.09e-39 |
|
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: 149.85 E-value: 5.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 88 VNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVT 167
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 168 CRDTGKTMLDASLGEIMATIDKLnwIIRYGPKHLQPSARSGttnyfmewyrgtevhYEPLGVVSSIISWNYPFYNVISPI 247
Cdd:cd07111 106 SLDNGKPIRESRDCDIPLVARHF--YHHAGWAQLLDTELAG---------------WKPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 248 ISAIFTGNAIIVKCSEQVIWSSEFFIsivrkclEVCNE---DPDLVQLCyclpkSDKYNATNYFISHPGFKHITFIGRKT 324
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFA-------EICAEaglPPGVLNIV-----TGNGSFGSALANHPGVDKVAFTGSTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 325 VANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTT 404
Cdd:cd07111 237 VGRALRRATAGTGKKLSLELGGKSPFIVFDD-ADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 405 qpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSryNHPNypQGHYFQPTLLVDVTSDMKIANSDL 484
Cdd:cd07111 316 --LRVGDPLD--KAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGA--DLPS--KGPFYPPTLFTNVPPASRIAQEEI 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 485 FGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTF 543
Cdd:cd07111 388 FGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLF 446
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
106-528 |
3.47e-38 |
|
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: 147.59 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNA-QEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIM 184
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 185 ATIDKLN----WIIRYGPKHLQPSARSGTTNYFMEWYRgtevhYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVK 260
Cdd:cd07113 102 QSANFLRyfagWATKINGETLAPSIPSMQGERYTAFTR-----REPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 261 cseqviwSSEFFISIVRKCLEVCNED--PDLVqlcyclpksdkYNATN-------YFISHPGFKHITFIGRKTVANKILN 331
Cdd:cd07113 177 -------PSEFTPLTLLRVAELAKEAgiPDGV-----------LNVVNgkgavgaQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 332 CAAESLTPVVVELCGKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLttQPLRLGS 411
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDA-DIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQAL--SSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 412 DMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnypqGHYFQPTLLVDVTSDMKIANSDLFGPILLV 491
Cdd:cd07113 316 PMD--ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE----GYFVQPTLVLARSADSRLMREETFGPVVSF 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 156847713 492 MKANSDEDCITIANAAPYAVGTCVFGKNVKQC-RYVAK 528
Cdd:cd07113 390 VPYEDEEELIQLINDTPFGLTASVWTNNLSKAlRYIPR 427
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
61-543 |
1.02e-37 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 146.89 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 61 SSLKVKPINFTleipdaaknnwksKRLVNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQE--EWA 138
Cdd:PLN02766 11 SGVKVPEIKFT-------------KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 139 KADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPK-HlqpsarsGTTNYFMEWY 217
Cdd:PLN02766 78 RMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKiH-------GETLKMSRQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 218 RGTEVHyEPLGVVSSIISWNYP---FYNVISPIISAiftGNAIIVKCSEQVIWSSEFFISIVRKClevcnEDPDLVqlcy 294
Cdd:PLN02766 151 QGYTLK-EPIGVVGHIIPWNFPstmFFMKVAPALAA---GCTMVVKPAEQTPLSALFYAHLAKLA-----GVPDGV---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 295 cLPKSDKYNATN--YFISHPGFKHITFIGRKTVANKILNCAAES-LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTF 371
Cdd:PLN02766 218 -INVVTGFGPTAgaAIASHMDVDKVSFTGSTEVGRKIMQAAATSnLKQVSLELGGKSPLLIFDD-ADVDMAVDLALLGIF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 372 QSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDHLENIdvGAMISPKTFDSLEELIKDAVESGATLICGG 451
Cdd:PLN02766 296 YNKGEICVASSRVYVQEGIYDEFVKKLVEK--AKDWVVGDPFDPRARQ--GPQVDKQQFEKILSYIEHGKREGATLLTGG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 452 SrynhPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLK 531
Cdd:PLN02766 372 K----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIR 447
|
490
....*....|..
gi 156847713 532 TTDVTINDFTTF 543
Cdd:PLN02766 448 AGTIWVNCYFAF 459
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
101-530 |
3.37e-37 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 145.02 E-value: 3.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 101 IQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHT----LHEyiiNNQEIiARVTCRDTGKTML 176
Cdd:PRK13252 24 FEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRavdiLRE---RNDEL-AALETLDTGKPIQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 177 DASLGEIMATIDKLNWiirYGpkHLQPSArSGTTNYFmewyRGTEVHY---EPLGVVSSIISWNYPFYnvispiIS---- 249
Cdd:PRK13252 100 ETSVVDIVTGADVLEY---YA--GLAPAL-EGEQIPL----RGGSFVYtrrEPLGVCAGIGAWNYPIQ------IAcwks 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 250 --AIFTGNAIIVKCSEQVIWSSeffisivRKCLEVCNED--PDLVqlcyclpksdkYNATN-------YFISHPGFKHIT 318
Cdd:PRK13252 164 apALAAGNAMIFKPSEVTPLTA-------LKLAEIYTEAglPDGV-----------FNVVQgdgrvgaWLTEHPDIAKVS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 319 FIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLL 398
Cdd:PRK13252 226 FTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDD-ADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 399 KDRltTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMK 478
Cdd:PRK13252 305 LER--VERIRIGDPMD--PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMT 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 156847713 479 IANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKL 530
Cdd:PRK13252 381 IVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQL 432
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
106-554 |
1.40e-36 |
|
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: 142.50 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADldrRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIMA 185
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAASYRSTLTRYQ---RSAILNKAAALLEARREEFARLITLESGLCLKDT-RYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDKLNWIIRYGPKHLQPSARSGTTNYFMEwyRGTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQV 265
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTANGKA--RKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 266 IWSSEFFISIVRKClevcNEDPDLVQLCYCLPkSDKYNAtnyFISHPGFKHITFIGRKTVANKIlnCAAESLTPVVVELC 345
Cdd:cd07146 160 PLSAIYLADLLYEA----GLPPDMLSVVTGEP-GEIGDE---LITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 346 GKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENIDVGAMI 425
Cdd:cd07146 230 GNDPLIVMDD-ADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEK--SAALVVGDPMD--PATDMGTVI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 426 SPKTFDSLEELIKDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIAN 505
Cdd:cd07146 305 DEEAAIQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISN 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 156847713 506 AAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVRQTPFGGIS 554
Cdd:cd07146 378 STAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSELSPFGGVK 426
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
121-538 |
4.94e-36 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 141.82 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIMATIDKLNWIIRYGPKH 200
Cdd:PLN00412 53 EEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSGDLISYTAEEGVRI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 201 LqpsarsGTTNYFM-EWYRGTE------VHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFI 273
Cdd:PLN00412 132 L------GEGKFLVsDSFPGNErnkyclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 274 SivrkCLEVCNEDPDLVQlCYCLPKSDkynATNYFISHPGFKHITFIGRKTvanKILNCAAESLTPVVVELCGKDSYIVL 353
Cdd:PLN00412 206 H----CFHLAGFPKGLIS-CVTGKGSE---IGDFLTMHPGVNCISFTGGDT---GIAISKKAGMVPLQMELGGKDACIVL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 354 ESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhleNIDVGAMISPKTFDSL 433
Cdd:PLN00412 275 ED-ADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAK--LTVGPPED---DCDITPVVSESSANFI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 434 EELIKDAVESGATLICGGSRynhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGT 513
Cdd:PLN00412 349 EGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQG 421
|
410 420
....*....|....*....|....*
gi 156847713 514 CVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:PLN00412 422 CVFTRDINKAILISDAMETGTVQIN 446
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
106-541 |
1.19e-35 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 140.00 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASlGEIMA 185
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDKLNWIIRYGPKHLQPSARSGTTNYFMewyrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQV 265
Cdd:PRK13968 93 SANLCDWYAEHGPAMLKAEPTLVENQQAV-------IEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 266 IWSSEFFISIVrkclevcnEDPDLVQLCYclpksDKYNATN----YFISHPGFKHITFIGRKTVANKILNCAAESLTPVV 341
Cdd:PRK13968 166 MGCAQLIAQVF--------KDAGIPQGVY-----GWLNADNdgvsQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 342 VELCGKDSYIVL-ESQKDVSSVSSLILRttFQSSGQSCIGIERIIVSskryKQTVQLLKDRLT--TQPLRLGSDMDhlEN 418
Cdd:PRK13968 233 LELGGSDPFIVLnDADLELAVKAAVAGR--YQNTGQVCAAAKRFIIE----EGIASAFTERFVaaAAALKMGDPRD--EE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 419 IDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDE 498
Cdd:PRK13968 305 NALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAG----AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAE 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 156847713 499 DCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFT 541
Cdd:PRK13968 381 HALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYC 423
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
121-554 |
2.23e-35 |
|
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: 139.09 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNA---QEEWAKADldRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLgEIMATIDKLNWII--- 194
Cdd:cd07148 21 AAIDKALDTAHALfldRNNWLPAH--ERIAILERLADLMEERADELALLIAREGGKPLVDAKV-EVTRAIDGVELAAdel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 195 -----RYGPKHLQPsARSGTTNYFMEwyrgtevhyEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSS 269
Cdd:cd07148 98 gqlggREIPMGLTP-ASAGRIAFTTR---------EPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 270 EFFISIVRKClevcNEDPDLVQLCYClpksdKYNATNYFISHPGFKHITFIGRKTVA----NKI---LNCAAE--SLTPV 340
Cdd:cd07148 168 LAFVDLLHEA----GLPEGWCQAVPC-----ENAVAEKLVTDPRVAFFSFIGSARVGwmlrSKLapgTRCALEhgGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 341 VVELCGkdsyivlesqkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSDMDhlENID 420
Cdd:cd07148 239 IVDRSA-----------DLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAA--AEKLVVGDPTD--PDTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 421 VGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYpqghyfQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDC 500
Cdd:cd07148 304 VGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 156847713 501 ITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTTFYVRQTPFGGIS 554
Cdd:cd07148 378 IAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRR 431
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
106-539 |
4.69e-35 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 138.50 E-value: 4.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMA 185
Cdd:PRK13473 24 PATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEIPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 186 TIDklnwIIRY---GPKHLQPSArSGttnyfmEWYRG--TEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVK 260
Cdd:PRK13473 104 IVD----VFRFfagAARCLEGKA-AG------EYLEGhtSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 261 CSEQVIWSSEFFISIVRKCLE------VCNEDPDlvqlcyclpksdkynATNYFISHPGFKHITFIGRKTVANKILNCAA 334
Cdd:PRK13473 173 PSEITPLTALKLAELAADILPpgvlnvVTGRGAT---------------VGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 335 ESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMD 414
Cdd:PRK13473 238 DSVKRTHLELGGKAPVIVFDD-ADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT--LKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 415 hlENIDVGAMISPKTFDSLEELIKDAVESG-ATLICGGSRYNHPnypqGHYFQPTLLVDVTSDMKIANSDLFGPILLVMK 493
Cdd:PRK13473 315 --EDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGK----GYYYEPTLLAGARQDDEIVQREVFGPVVSVTP 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 156847713 494 ANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:PRK13473 389 FDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT 434
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
101-519 |
2.54e-33 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 133.91 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 101 IQSHCPATGQHLSSYLPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAS 179
Cdd:PRK03137 52 IVSINPANKSEVVGRVSKATkELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 180 lGEIMATIDklnwiirygpkHLQPSARSgttnyFMEWYRGTEV----------HYEPLGVVSSIISWNYPFYNVISPIIS 249
Cdd:PRK03137 132 -ADTAEAID-----------FLEYYARQ-----MLKLADGKPVesrpgehnryFYIPLGVGVVISPWNFPFAIMAGMTLA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 250 AIFTGNAIIVKCSEQVIWSSEFFISIvrkcLEVCNEDPDLVQLCyclPKSDKyNATNYFISHPGFKHITFIGRKTVANKI 329
Cdd:PRK03137 195 AIVAGNTVLLKPASDTPVIAAKFVEV----LEEAGLPAGVVNFV---PGSGS-EVGDYLVDHPKTRFITFTGSREVGLRI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 330 LNCAAES------LTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRlt 403
Cdd:PRK03137 267 YERAAKVqpgqiwLKRVIAEMGGKDAIVVDED-ADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVEL-- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 404 TQPLRLGsdmDHLENIDVGAMISPKTFDSleelIKDAVESG---ATLICGGSRynhpNYPQGHYFQPTLLVDVTSDMKIA 480
Cdd:PRK03137 344 TKELTVG---NPEDNAYMGPVINQASFDK----IMSYIEIGkeeGRLVLGGEG----DDSKGYFIQPTIFADVDPKARIM 412
|
410 420 430
....*....|....*....|....*....|....*....
gi 156847713 481 NSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKN 519
Cdd:PRK03137 413 QEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNN 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
82-538 |
4.59e-33 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 132.72 E-value: 4.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 82 WKSKRLVNTEIIDPSQPNIIQSHCPATGQHLSSyLPKYN-EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQ 160
Cdd:PRK11241 9 FRQQALINGEWLDANNGEVIDVTNPANGDKLGS-VPKMGaDETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 161 EIIARVTCRDTGKTMLDASlGEIMATIDKLNWIIR-----YG---PKHlQPSARsgttnyfmewyrgTEVHYEPLGVVSS 232
Cdd:PRK11241 88 DDLARLMTLEQGKPLAEAK-GEISYAASFIEWFAEegkriYGdtiPGH-QADKR-------------LIVIKQPIGVTAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 233 IISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKClevcnedpDLVQLCYCLPKSDKYNATNYFISHP 312
Cdd:PRK11241 153 ITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRA--------GIPAGVFNVVTGSAGAVGGELTSNP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 313 GFKHITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYK 392
Cdd:PRK11241 225 LVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD-ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 393 QTVQLLKDRLTTqpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSrynhPNYPQGHYFQPTLLVD 472
Cdd:PRK11241 304 RFAEKLQQAVSK--LHIGDGLE--KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGK----AHELGGNFFQPTILVD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156847713 473 VTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:PRK11241 376 VPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN 441
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
106-538 |
2.23e-32 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 131.01 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 106 PATGQHLSSYLPKYNEDIDEMVTIAQNA-----QEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTmLDASL 180
Cdd:PLN02467 30 PATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP-LDEAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 181 GEImatiDKLNWIIRYGPKHLQP--SARSGTTNYFMEWYRGTeVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:PLN02467 109 WDM----DDVAGCFEYYADLAEAldAKQKAPVSLPMETFKGY-VLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEqviwssefFISIVrkCLE---VCNE---DPDLVQLCYCLPKsdkyNATNYFISHPGFKHITFIGRKTVANKILNC 332
Cdd:PLN02467 184 LKPSE--------LASVT--CLEladICREvglPPGVLNVVTGLGT----EAGAPLASHPGVDKIAFTGSTATGRKIMTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 333 AAESLTPVVVELCGKDSYIVLESQkDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRltTQPLRLGSD 412
Cdd:PLN02467 250 AAQMVKPVSLELGGKSPIIVFDDV-DLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKW--AKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 413 MDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVM 492
Cdd:PLN02467 327 LE--EGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLK--KGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 156847713 493 KANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
136-539 |
2.90e-31 |
|
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: 126.76 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 136 EWAKADLDRRLKVLHtlheyiiNNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTNYFME 215
Cdd:cd07137 21 EWRKSQLKGLLRLVD-------ENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLTTFPA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 216 WyrgTEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcneDPDLVQLCYC 295
Cdd:cd07137 94 K---AEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYL-----DTKAIKVIEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 296 LPksdkyNATNYFISHPGFKhITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVlESQKDVSSVSSLILRTTFQS-S 374
Cdd:cd07137 166 GV-----PETTALLEQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIV-DSTVDLKVAVRRIAGGKWGCnN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 375 GQSCIGIERIIVSSKRYKQTVQLLKDRLTTqplRLGSDmdHLENIDVGAMISPKTFDSLEELIKDAVESgATLICGGSRY 454
Cdd:cd07137 239 GQACIAPDYVLVEESFAPTLIDALKNTLEK---FFGEN--PKESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 455 NhpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTD 534
Cdd:cd07137 313 E-----KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGG 387
|
....*
gi 156847713 535 VTIND 539
Cdd:cd07137 388 VTFND 392
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
88-540 |
3.86e-31 |
|
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: 127.23 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 88 VNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQE--EWAKADLDRRLKVLHTLHEYIINNQEIIAR 165
Cdd:cd07140 10 INGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 166 VTCRDTGKTMLDASLGEIMATIDklnwiirygpkhlqpsarsgTTNYFMEW---YRG--------------TEVHYEPLG 228
Cdd:cd07140 90 IESLDSGAVYTLALKTHVGMSIQ--------------------TFRYFAGWcdkIQGktipinqarpnrnlTLTKREPIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 229 VVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKClevcNEDPDLVQLcycLPKSDKyNATNYF 308
Cdd:cd07140 150 VCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKA----GFPKGVINI---LPGSGS-LVGQRL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 309 ISHPGFKHITFIGRKTVANKIL-NCAAESLTPVVVELCGKDSYIVLeSQKDVSSVSSLILRTTFQSSGQSCIGIERIIVS 387
Cdd:cd07140 222 SDHPDVRKLGFTGSTPIGKHIMkSCAVSNLKKVSLELGGKSPLIIF-ADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 388 SKRYKQTVQLLKDRLTTqpLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnypqGHYFQP 467
Cdd:cd07140 301 ESIHDEFVRRVVEEVKK--MKIGDPLD--RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP----GFFFEP 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156847713 468 TLLVDVTSDMKIANSDLFGPILLVMKANSD--EDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:cd07140 373 TVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTY 447
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
88-538 |
7.90e-31 |
|
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: 126.41 E-value: 7.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 88 VNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVT 167
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 168 CRDTGKTMLDASLGEIMATIDKLNW---IIRygpkhlqpsARSGTTNYFMEWYRGTEVHyEPLGVVSSIISWNYPFYNVI 244
Cdd:cd07116 85 TWDNGKPVRETLAADIPLAIDHFRYfagCIR---------AQEGSISEIDENTVAYHFH-EPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 245 SPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRkclevcnedpDLvqlcycLPKSdKYNATN--------YFISHPGFKH 316
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMELIG----------DL------LPPG-VVNVVNgfgleagkPLASSKRIAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 317 ITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIVLESQKDV------SSVSSLILRTTFQssGQSCIGIERIIVSSKR 390
Cdd:cd07116 218 VAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVMDAddaffdKALEGFVMFALNQ--GEVCTCPSRALIQESI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 391 YKQTVQLLKDRltTQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTlL 470
Cdd:cd07116 296 YDRFMERALER--VKAIKQGNPLD--TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPT-T 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156847713 471 VDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:cd07116 371 FKGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
76-540 |
1.32e-30 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 125.78 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 76 DAAKNNWKSKRL-VNTEIIDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQE--EWAKADLDRRLKVLHTL 152
Cdd:PRK09847 11 DKALSLAIENRLfINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 153 HEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTNYFMewyrgteVHYEPLGVVSS 232
Cdd:PRK09847 91 ADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAM-------IVREPVGVIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 233 IISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKClevcnEDPDLVqlcYCLPKSDKYNATNYFISHP 312
Cdd:PRK09847 164 IVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEA-----GLPDGV---LNVVTGFGHEAGQALSRHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 313 GFKHITFIGRKTVANKILNCAAES-LTPVVVELCGKDSYIVLESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRY 391
Cdd:PRK09847 236 DIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 392 KQTVQLLKDRLTT-QPlrlGSDMDhlENIDVGAMISPKTFDSLEELIKDAvESGATLICGGSRYNHPNYpqghyFQPTLL 470
Cdd:PRK09847 316 DEFLALLKQQAQNwQP---GHPLD--PATTMGTLIDCAHADSVHSFIREG-ESKGQLLLDGRNAGLAAA-----IGPTIF 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 471 VDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTINDF 540
Cdd:PRK09847 385 VDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNY 454
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-538 |
1.79e-29 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 123.70 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 24 KTLLSRAESQQNQRLIATTTLFATLFLFYVS----------YKLLFTSSLKVKPINFTL-EIPDAAKNnwkskrLVNTEI 92
Cdd:PLN02419 49 RRLYKEADDNTKLRSSSSTTTTTTTMLLRISgnnlrplrpqFLALRSSWLSTSPEQSTQpQMPPRVPN------LIGGSF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 93 IDPSQPNIIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTG 172
Cdd:PLN02419 123 VESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 173 KTMLDaSLGEIMATIDKLNWIIryGPKHLQ-----PSARSGTTNYFMEwyrgtevhyEPLGVVSSIISWNYPFYNVISPI 247
Cdd:PLN02419 203 KTLKD-SHGDIFRGLEVVEHAC--GMATLQmgeylPNVSNGVDTYSIR---------EPLGVCAGICPFNFPAMIPLWMF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 248 ISAIFTGNAIIVKCSEQviwssEFFISIVRKCLEVCNEDPDLVqLCYCLPKSDKYNAtnyFISHPGFKHITFIGRKTVAN 327
Cdd:PLN02419 271 PVAVTCGNTFILKPSEK-----DPGASVILAELAMEAGLPDGV-LNIVHGTNDTVNA---ICDDEDIRAVSFVGSNTAGM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 328 KILNCAAESLTPVVVELCGKDSYIVLeSQKDVSSVSSLILRTTFQSSGQSCIGIERIIV--SSKRYKQTvqlLKDRLTTQ 405
Cdd:PLN02419 342 HIYARAAAKGKRIQSNMGAKNHGLVL-PDANIDATLNALLAAGFGAAGQRCMALSTVVFvgDAKSWEDK---LVERAKAL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 406 PLRLGSDMDhlenIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLF 485
Cdd:PLN02419 418 KVTCGSEPD----ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIF 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 156847713 486 GPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:PLN02419 494 GPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
123-542 |
1.79e-29 |
|
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: 122.69 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 123 IDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASlGEIMATIDKLNWIIRY-----G 197
Cdd:cd07083 57 AEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAalrlrY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 198 PKHLQPSArSGTTNyfmewyrgtEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVR 277
Cdd:cd07083 136 PAVEVVPY-PGEDN---------ESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 278 KclevCNEDPDLVQLcycLPkSDKYNATNYFISHPGFKHITFIGRKTVANKILNCAAESLT------PVVVELCGKDSYI 351
Cdd:cd07083 206 E----AGFPPGVVQF---LP-GVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAII 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 352 VLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQtvqlLKDRLTTQPLRLGSDMDHLENIDVGAMISPKTFD 431
Cdd:cd07083 278 VDET-ADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEP----VLERLLKRAERLSVGPPEENGTDLGPVIDAEQEA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 432 SLEELIKDAVESGaTLICGGSRYNHpnypQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDE--DCITIANAAPY 509
Cdd:cd07083 353 KVLSYIEHGKNEG-QLVLGGKRLEG----EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPY 427
|
410 420 430
....*....|....*....|....*....|...
gi 156847713 510 AVGTCVFGKNVKQCRYVAKKLKTTDVTINDFTT 542
Cdd:cd07083 428 GLTGGVYSRKREHLEEARREFHVGNLYINRKIT 460
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
129-539 |
4.27e-29 |
|
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: 120.40 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 129 IAQNAQEEWAK---ADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSA 205
Cdd:cd07132 3 AVRRAREAFSSgktRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 206 RSGT-TNYFMEWYrgteVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcn 284
Cdd:cd07132 83 VKKNlATLLDDVY----IYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYL---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 285 eDPDLVQLcYCLPKSDkynaTNYFISHPgFKHITFIGRKTVANKILNCAAESLTPVVVELCGKdSYIVLESQKDVSSVSS 364
Cdd:cd07132 155 -DKECYPV-VLGGVEE----TTELLKQR-FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGK-SPCYVDKSCDIDVAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 365 LILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqplRLGSDMDhlENIDVGAMISPKTFDSLEELIkdaveSG 444
Cdd:cd07132 227 RIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKE---FYGEDPK--ESPDYGRIINDRHFQRLKKLL-----SG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 445 ATLICGGsRYNhpnyPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANA--APYAVgtCVFGKNVKQ 522
Cdd:cd07132 297 GKVAIGG-QTD----EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSreKPLAL--YVFSNNKKV 369
|
410
....*....|....*..
gi 156847713 523 CRYVAKKLKTTDVTIND 539
Cdd:cd07132 370 INKILSNTSSGGVCVND 386
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
221-545 |
6.64e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 120.60 E-value: 6.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 221 EVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcneDPDLVQLCYCLPksd 300
Cdd:PLN02203 103 EVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYL-----DSKAVKVIEGGP--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 301 kyNATNYFISHPGFKhITFIGRKTVANKILNCAAESLTPVVVELCGKDSYIV--LESQKDVSSVSSLILRTTFQS-SGQS 377
Cdd:PLN02203 175 --AVGEQLLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSRDTKVAVNRIVGGKWGScAGQA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 378 CIGIERIIVSSKRYKQTVQLLKDRLTTQPLRLGSDMDHLENIdvgamISPKTFDSLEELIKD-AVEsgATLICGGSRynh 456
Cdd:PLN02203 252 CIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARI-----LNKKHFQRLSNLLKDpRVA--ASIVHGGSI--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 457 pnYPQGHYFQPTLLVDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVT 536
Cdd:PLN02203 322 --DEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVT 399
|
....*....
gi 156847713 537 INDFTTFYV 545
Cdd:PLN02203 400 FNDAIIQYA 408
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
70-538 |
1.14e-28 |
|
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: 120.38 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 70 FTLEIPDAAKNNWKSKRLVNTEIIDPSQPNI---------IQSHCpATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKA 140
Cdd:cd07125 10 FDLEVPLEALADALKAFDEKEWEAIPIINGEetetgegapVIDPA-DHERTIGEVSLADAEDVDAALAIAAAAFAGWSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 141 DLDRRLKVLHTL-HEYIINNQEIIArVTCRDTGKTMLDAsLGEIMATIDKLnwiiRYGPKhlqpSARSGTTNYFMEWYRG 219
Cdd:cd07125 89 PVEERAEILEKAaDLLEANRGELIA-LAAAEAGKTLADA-DAEVREAIDFC----RYYAA----QARELFSDPELPGPTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 220 --TEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFIsivrKCLEVCNEDPDLVQLcycLP 297
Cdd:cd07125 159 elNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAV----ELLHEAGVPRDVLQL---VP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 298 KSDKYnATNYFISHPGFKHITFIGRKTVANKILNCAAE---SLTPVVVELCGKDSYIV----LESQ--KDVssvssliLR 368
Cdd:cd07125 232 GDGEE-IGEALVAHPRIDGVIFTGSTETAKLINRALAErdgPILPLIAETGGKNAMIVdstaLPEQavKDV-------VQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 369 TTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqpLRLGSDMDhLENiDVGAMISPKTFDSLEELIKdaVESG-ATL 447
Cdd:cd07125 304 SAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMAS--LKVGDPWD-LST-DVGPLIDKPAGKLLRAHTE--LMRGeAWL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 448 ICGGsrynHPNYPQGHYFQPTLLVDVTSDmkIANSDLFGPILLVMKANSD--EDCITIANAAPYAVGTCVFGKNVKQCRY 525
Cdd:cd07125 378 IAPA----PLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEY 451
|
490
....*....|...
gi 156847713 526 VAKKLKTTDVTIN 538
Cdd:cd07125 452 WRERVEAGNLYIN 464
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
101-522 |
3.31e-28 |
|
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: 118.46 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 101 IQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsL 180
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEG-L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 181 GEIMATID------KLNWIIrYGPkhLQPSARSGttNYFMEwyrgtevHYEPLGVVSSIISWNYPF----YNVIspiISA 250
Cdd:cd07130 93 GEVQEMIDicdfavGLSRQL-YGL--TIPSERPG--HRMME-------QWNPLGVVGVITAFNFPVavwgWNAA---IAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 251 IfTGNAIIVKCSEQVIWSSEFFISIVRKCLEVCNEDPDLVQLCYClpKSDKYNAtnyFISHPGFKHITFIGRKTVANKIL 330
Cdd:cd07130 158 V-CGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCG--GADVGEA---LVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 331 NCAAESLTPVVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQtvqlLKDRLTT--QPLR 408
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMED-ADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDE----VLERLKKayKQVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 409 LGSDMDhlENIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNHPnypqGHYFQPTLlVDVTSDMKIANSDLFGPI 488
Cdd:cd07130 307 IGDPLD--DGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP----GNYVEPTI-VEGLSDAPIVKEETFAPI 379
|
410 420 430
....*....|....*....|....*....|....
gi 156847713 489 LLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQ 522
Cdd:cd07130 380 LYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRN 413
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
170-539 |
3.28e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 109.37 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 170 DTGKTMLDASLGEIMATIDKLNWIIRYGPKHLQPSARSGTTNYFMEwyrGTEVHYEPLGVVSSIISWNYPFYNVISPIIS 249
Cdd:PLN02174 59 DLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPA---SAEIVSEPLGVVLVISAWNYPFLLSIDPVIG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 250 AIFTGNAIIVKCSEQVIWSSEFFISIVRKCLevcneDPDLVQLCyclpkSDKYNATNYFISHPgFKHITFIGRKTVANKI 329
Cdd:PLN02174 136 AISAGNAVVLKPSELAPASSALLAKLLEQYL-----DSSAVRVV-----EGAVTETTALLEQK-WDKIFYTGSSKIGRVI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 330 LNCAAESLTPVVVELCGKdSYIVLESQKDVS-SVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTVQLLKDRLTTqplr 408
Cdd:PLN02174 205 MAAAAKHLTPVVLELGGK-SPVVVDSDTDLKvTVRRIIAGKWGCNNGQACISPDYILTTKEYAPKVIDAMKKELET---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 409 lGSDMDHLENIDVGAMISPKTFDSLEELIkDAVESGATLICGGSRyNHPNYPqghyFQPTLLVDVTSDMKIANSDLFGPI 488
Cdd:PLN02174 280 -FYGKNPMESKDMSRIVNSTHFDRLSKLL-DEKEVSDKIVYGGEK-DRENLK----IAPTILLDVPLDSLIMSEEIFGPL 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 156847713 489 LLVMKANSDEDCITIANAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIND 539
Cdd:PLN02174 353 LPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVND 403
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
122-519 |
2.70e-22 |
|
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: 100.04 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 122 DIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsLGEIMATIDKLNWIIRygpkhl 201
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIK------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 202 QPSARSGTTNYFMEWYRGTeVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFIsivrKCLE 281
Cdd:cd07095 74 AYHERTGERATPMAQGRAV-LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMV----ELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 282 VCNEDPDLVQLCyclpKSDKyNATNYFISHPGFKHITFIG--------RKTVAN---KILncaaesltpvVVELCGKDSY 350
Cdd:cd07095 149 EAGLPPGVLNLV----QGGR-ETGEALAAHEGIDGLLFTGsaatglllHRQFAGrpgKIL----------ALEMGGNNPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 351 IVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSkryKQTVQLLKDRLT--TQPLRLGSDMDhlENIDVGAMISPK 428
Cdd:cd07095 214 VVWDV-ADIDAAAYLIVQSAFLTAGQRCTCARRLIVPD---GAVGDAFLERLVeaAKRLRIGAPDA--EPPFMGPLIIAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 429 TFDSLEELIKDAVESGATLICGGSRYNHpnypQGHYFQPTLLvDVTSDMKIANSDLFGPILLVMKANSDEDCITIANAAP 508
Cdd:cd07095 288 AAARYLLAQQDLLALGGEPLLAMERLVA----GTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATR 362
|
410
....*....|.
gi 156847713 509 YAVGTCVFGKN 519
Cdd:cd07095 363 FGLSAGLLSDD 373
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
100-519 |
2.55e-18 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 88.35 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 100 IIQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKtMLDAS 179
Cdd:PLN02315 35 LVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGK-ILAEG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 180 LGEIMATIDKLNWII---RYGPKHLQPSARSgttNYFMewyrgTEVhYEPLGVVSSIISWNYPfynvispiiSAIFTGNA 256
Cdd:PLN02315 114 IGEVQEIIDMCDFAVglsRQLNGSIIPSERP---NHMM-----MEV-WNPLGIVGVITAFNFP---------CAVLGWNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 257 II-VKCSEQVIWSSE-----FFISIVRKCLEVC--NEDPDLVQLCYC----LPKSDKYNATNYFISHPGFKHITFIGRKT 324
Cdd:PLN02315 176 CIaLVCGNCVVWKGApttplITIAMTKLVAEVLekNNLPGAIFTSFCggaeIGEAIAKDTRIPLVSFTGSSKVGLMVQQT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 325 VANKILNCaaesltpvVVELCGKDSYIVLESqKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRYKQTV-QLLKdrlT 403
Cdd:PLN02315 256 VNARFGKC--------LLELSGNNAIIVMDD-ADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLeQLLT---V 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 404 TQPLRLGSDMDHleNIDVGAMISPKTFDSLEELIKDAVESGATLICGGSRYNhpnyPQGHYFQPTLlVDVTSDMKIANSD 483
Cdd:PLN02315 324 YKQVKIGDPLEK--GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTI-VEISPDADVVKEE 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 156847713 484 LFGPILLVMKANSDEDCITIANAAPYAVGTCVFGKN 519
Cdd:PLN02315 397 LFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
101-509 |
1.13e-16 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 83.08 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 101 IQSHCPATGQHLSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGKTMLDAsL 180
Cdd:PRK09457 17 FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEA-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 181 GEIMATIDKLNWIIR-YgpkhlqpSARSGTTNYFMEwyRGTEV-HYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:PRK09457 96 TEVTAMINKIAISIQaY-------HERTGEKRSEMA--DGAAVlRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEQVIWSSEFFISIVRKC---LEVCNedpdLVQlcyclPKSDKYNAtnyFISHPGFKHITFIG--------RKTVAN 327
Cdd:PRK09457 167 FKPSELTPWVAELTVKLWQQAglpAGVLN----LVQ-----GGRETGKA---LAAHPDIDGLLFTGsantgyllHRQFAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 328 ---KILncAAEsltpvvvelCGKDSYIVLESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVssKRYKQTVQLLkDRLT- 403
Cdd:PRK09457 235 qpeKIL--ALE---------MGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLV--PQGAQGDAFL-ARLVa 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 404 -TQPLRLGSDMDHLENIdVGAMISPKTFDSLEELIKDAVESGATLICggsrynHPNYPQ-GHYFQPTLLVDVTSDMKIAN 481
Cdd:PRK09457 301 vAKRLTVGRWDAEPQPF-MGAVISEQAAQGLVAAQAQLLALGGKSLL------EMTQLQaGTGLLTPGIIDVTGVAELPD 373
|
410 420
....*....|....*....|....*...
gi 156847713 482 SDLFGPILLVMKANSDEDCITIANAAPY 509
Cdd:PRK09457 374 EEYFGPLLQVVRYDDFDEAIRLANNTRF 401
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
99-545 |
7.19e-16 |
|
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: 80.71 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 99 NIIQSHCPATGQH-LSSYLPKYNEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIIN--NQEIIArvtcrdtgKTM 175
Cdd:cd07123 46 NTGKQVMPHDHAHvLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGkyRYELNA--------ATM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 176 LDASLGEIMATIDKLNWII---RYGPK------HLQP-SARSGTTNyFMEwYRGTEvhyeplGVVSSIISWNYpfynvis 245
Cdd:cd07123 118 LGQGKNVWQAEIDAACELIdflRFNVKyaeelyAQQPlSSPAGVWN-RLE-YRPLE------GFVYAVSPFNF------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 246 piiSAI---------FTGNAIIVKCSEQVIWSSEFFISIvrkcLEVCNEDPDLVQLcycLPkSDKYNATNYFISHPGFKH 316
Cdd:cd07123 183 ---TAIggnlagapaLMGNVVLWKPSDTAVLSNYLVYKI----LEEAGLPPGVINF---VP-GDGPVVGDTVLASPHLAG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 317 ITFIGRKTVANKILNCAAESLT-----PVVVELCGKDSYIVLESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSSKRY 391
Cdd:cd07123 252 LHFTGSTPTFKSLWKQIGENLDryrtyPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLW 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 392 KQtvqlLKDRLTTQ--PLRLGSDMDHleNIDVGAMISPKTFDSLEELIKDAVES-GATLICGGsrynHPNYPQGHYFQPT 468
Cdd:cd07123 332 PE----VKERLLEElkEIKMGDPDDF--SNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGG----KCDDSVGYFVEPT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 469 LLVDVTSDMKIANSDLFGPILLVM---KANSDEDCITIANAAPYAVGTCVFGknvkQCRYVAKKLktTDVTINDFTTFYV 545
Cdd:cd07123 402 VIETTDPKHKLMTEEIFGPVLTVYvypDSDFEETLELVDTTSPYALTGAIFA----QDRKAIREA--TDALRNAAGNFYI 475
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
226-493 |
3.87e-15 |
|
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: 78.05 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 226 PLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQVIWSSEFFISIVRKCLEVCNEDPDLVQlcyclpkSDKyNAT 305
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLIN-------GDG-KTM 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 306 NYFISHPGFKHITFIGRKTVANKILNCAAESltPVVVELCGKDSYIVLESQKDVSSVSSLILRTTFQSSGQSCIGIERII 385
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTACSGQKCTAQSMLF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 386 VSSKRYKQ-TVQLLKDRLTTQplrlgsdmdhlenIDVGAMISP-KTFDSLEELIKDAVESGATLICGGSRYNHPNYPQ-- 461
Cdd:cd07084 250 VPENWSKTpLVEKLKALLARR-------------KLEDLLLGPvQTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSiy 316
|
250 260 270
....*....|....*....|....*....|....*
gi 156847713 462 GHYFQPTLLVDVTSDMK---IANSDLFGPILLVMK 493
Cdd:cd07084 317 GACVASALFVPIDEILKtyeLVTEEIFGPFAIVVE 351
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
122-513 |
1.70e-09 |
|
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: 60.57 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 122 DIDEMVTIAQNAQEEWAKADLDRR----LKVLHTLHEyiiNNQEIIARVtcrdtgktMLDASLGEIMAtidklnwiIRYG 197
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARagvcLEILQRLNA---RSFEMAHAV--------MHTTGQAFMMA--------FQAG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 198 PKHLQPSARSGTTNYFMEWYRGTEV-------------------HYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAII 258
Cdd:cd07127 146 GPHAQDRGLEAVAYAWREMSRIPPTaewekpqgkhdplamektfTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 259 VKCSEQVIWSSEFFISIVRKCLEVCNEDPDLVQLCYCLPKSDkynATNYFISHPGFKHITFIGRKTVANKILNCAAESLt 338
Cdd:cd07127 226 VKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAADTPEEP---IAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 339 pVVVELCGKDSYIVlESQKDVSSVSSLILRTTFQSSGQSCIGIERIIVSS---------KRYKQTVQLLKDRLTtqplRL 409
Cdd:cd07127 302 -VYTEKAGVNTVVV-DSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRdgiqtddgrKSFDEVAADLAAAID----GL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 410 GSDMDHLENIdVGAMISPKTFDSLEElikdaVESGATLICGGSRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDLFGPIL 489
Cdd:cd07127 376 LADPARAAAL-LGAIQSPDTLARIAE-----ARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIA 449
|
410 420
....*....|....*....|....
gi 156847713 490 LVMKANSDEDCITIANAAPYAVGT 513
Cdd:cd07127 450 FVVATDSTDHSIELARESVREHGA 473
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
121-259 |
9.92e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.99 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGktmldasLGEIMATIDKLNWIIRY--GP 198
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG-------MGRVEDKIAKNVAAAEKtpGV 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156847713 199 KHLQPSARSGTtnyfmewyRG-TEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIV 259
Cdd:PRK15398 109 EDLTTEALTGD--------NGlTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVF 162
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
120-538 |
3.67e-08 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 56.75 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 120 NEDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQ-EIIArVTCRDTGKTMLDAsLGEIMATIDKLnwiiRY-- 196
Cdd:PRK11904 584 AEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRaELIA-LCVREAGKTLQDA-IAEVREAVDFC----RYya 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 197 --GPKHL-QPSARSGTT---NyfmewyrgtEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQViwsse 270
Cdd:PRK11904 658 aqARRLFgAPEKLPGPTgesN---------ELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQT----- 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 271 ffiSIV-RKCLEVCNE---DPDLVQLcycLPKSDKY--NAtnyFISHPGFKHITFIGRKTVA---NKILncAAES--LTP 339
Cdd:PRK11904 724 ---PLIaAEAVKLLHEagiPKDVLQL---LPGDGATvgAA---LTADPRIAGVAFTGSTETAriiNRTL--AARDgpIVP 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 340 VVVELCGKDSYIV----LESQ--KDVssvssliLRTTFQSSGQSCigieriivSSKR--YKQ------TVQLLKDRLttQ 405
Cdd:PRK11904 793 LIAETGGQNAMIVdstaLPEQvvDDV-------VTSAFRSAGQRC--------SALRvlFVQediadrVIEMLKGAM--A 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 406 PLRLGSDMDHleNIDVGAMISPKTFDSLEELIkDAVESGATLICGGSRynhPNYPQ-GHYFQPTLL-VDVTSDMKianSD 483
Cdd:PRK11904 856 ELKVGDPRLL--STDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPL---PAGTEnGHFVAPTAFeIDSISQLE---RE 926
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 484 LFGPILLVMKANSDE-----DCItiaNAAPYAVGTCVFGKNVKQCRYVAKKLKTTDVTIN 538
Cdd:PRK11904 927 VFGPILHVIRYKASDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
121-342 |
9.94e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 54.55 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVLHTLHEYIINNQEIIARVTCRDTGktmldasLGEIMATIDKLNWIIRY--GP 198
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG-------MGRVEDKIAKNHLAAEKtpGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 199 KHLQPSARSGTtnyfmewyRG-TEVHYEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIV-------KCSEQVIwsSE 270
Cdd:cd07121 77 EDLTTTAWSGD--------NGlTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFnphpgakKVSAYAV--EL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 271 FFISIVRKC----LEVCNEDPDLvqlcyclpksdkyNATNYFISHPGFKHITFIGRKTVANKILN------CAAESLTPV 340
Cdd:cd07121 147 INKAIAEAGgpdnLVVTVEEPTI-------------ETTNELMAHPDINLLVVTGGPAVVKAALSsgkkaiGAGAGNPPV 213
|
..
gi 156847713 341 VV 342
Cdd:cd07121 214 VV 215
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
121-498 |
1.13e-07 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 55.26 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 121 EDIDEMVTIAQNAQEEWAKADLDRRLKVL---------HTlheyiinnQEIIArVTCRDTGKTMLDAsLGEIMATIDKLn 191
Cdd:PRK11905 590 EDVERALAAAQAAFPEWSATPAAERAAILeraadlmeaHM--------PELFA-LAVREAGKTLANA-IAEVREAVDFL- 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 192 wiiRY----GPKHLQPSARsgttnyfmewyrgtevhyEPLGVVSSIISWNYPFYNVISPIISAIFTGNAIIVKCSEQViw 267
Cdd:PRK11905 659 ---RYyaaqARRLLNGPGH------------------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQT-- 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 268 sseffiSIVR----KCLEVCNEDPDLVQLcycLPKS-DKYNATnyFISHPGFKHITFIGRKTVA---NKILNCAAESLTP 339
Cdd:PRK11905 716 ------PLIAaravRLLHEAGVPKDALQL---LPGDgRTVGAA--LVADPRIAGVMFTGSTEVArliQRTLAKRSGPPVP 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 340 VVVELCGKDSYIVlesqkDVSS----VSSLILRTTFQSSGQSCigieriivSSKR--YKQ------TVQLLKDRLttQPL 407
Cdd:PRK11905 785 LIAETGGQNAMIV-----DSSAlpeqVVADVIASAFDSAGQRC--------SALRvlCLQedvadrVLTMLKGAM--DEL 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 408 RLGsDMDHLeNIDVGAMISPKTFDSLEELIkDAVESGATLIcggsrYNHP---NYPQGHYFQPTLL-VDVTSDMKianSD 483
Cdd:PRK11905 850 RIG-DPWRL-STDVGPVIDAEAQANIEAHI-EAMRAAGRLV-----HQLPlpaETEKGTFVAPTLIeIDSISDLE---RE 918
|
410
....*....|....*
gi 156847713 484 LFGPILLVMKANSDE 498
Cdd:PRK11905 919 VFGPVLHVVRFKADE 933
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
372-505 |
2.38e-03 |
|
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: 40.72 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 372 QSSGQSCIGIERIIVSSKRYKQTVQLLKDRLttQPLRLGSDMDhlENIDVGAMISPKTFDSLEELIkDAVESGATLICGG 451
Cdd:cd07128 286 VKAGQKCTAIRRAFVPEARVDAVIEALKARL--AKVVVGDPRL--EGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGG 360
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 156847713 452 ---SRYNHPNYPQGHYFQPTLLVDVTSDMKIANSDL--FGPILLVMKANSDEDCITIAN 505
Cdd:cd07128 361 pdrFEVVGADAEKGAFFPPTLLLCDDPDAATAVHDVeaFGPVATLMPYDSLAEAIELAA 419
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
225-313 |
7.77e-03 |
|
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: 39.01 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156847713 225 EPLGVVSSII-SWNyPFYNVISPIISAIFTGNAII-------VKCSEQViwsseffISIVRKCLEVCNEDPDLVQlcyCL 296
Cdd:cd07122 94 EPVGVIAALIpSTN-PTSTAIFKALIALKTRNAIIfsphpraKKCSIEA-------AKIMREAAVAAGAPEGLIQ---WI 162
|
90
....*....|....*...
gi 156847713 297 PK-SDKynATNYFISHPG 313
Cdd:cd07122 163 EEpSIE--LTQELMKHPD 178
|
|
| |
