|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-475 |
0e+00 |
|
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: 760.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 6 SLIDGQWAGGAGDSENINPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHI 85
Cdd:cd07097 3 NYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 86 LASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALAC 165
Cdd:cd07097 83 LTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 166 GNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQ 245
Cdd:cd07097 163 GNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 246 MEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSN 325
Cdd:cd07097 243 LEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 326 GAQFDKDLSYIALARDE-AQRVIGGAALQRAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTE 404
Cdd:cd07097 323 ERQLEKDLRYIEIARSEgAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1837855989 405 YGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGASSYGSSEQGHYAREFFTSLKTSYI 475
Cdd:cd07097 403 FGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYGPREQGEAALEFYTTIKTVYV 473
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-476 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 545.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 2 RTITSLIDGQW--AGGAGDSENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANS 79
Cdd:COG1012 4 PEYPLFIGGEWvaAASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 80 QQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKT 159
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 160 APALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVA 239
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 240 GHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQ 319
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 320 IGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAqRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALA 398
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEgAELLTGGRRPDGE-GGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1837855989 399 IANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGASSYGsSEQGHYAREFFTSLKTSYIR 476
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIG-REGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
53-472 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 514.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSiRAGVEV 132
Cdd:pfam00171 42 FPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:pfam00171 121 YTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:pfam00171 201 VEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHES 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRaqRGYYLQPCLALDVSL 371
Cdd:pfam00171 281 IYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEgAKLLTGGEAGLD--NGYFVEPTVLANVTP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGA 451
Cdd:pfam00171 359 DMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQ 438
|
410 420
....*....|....*....|.
gi 1837855989 452 SSYGsSEQGHYAREFFTSLKT 472
Cdd:pfam00171 439 SGFG-REGGPYGLEEYTEVKT 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
53-475 |
1.87e-167 |
|
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: 479.01 E-value: 1.87e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07078 91 IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07078 171 ASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHES 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRAQRGYYLQPCLALDVSLD 372
Cdd:cd07078 251 IYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTVLTDVDPD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGAS 452
Cdd:cd07078 331 MPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFGGVKQS 410
|
410 420
....*....|....*....|...
gi 1837855989 453 SYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07078 411 GIG-REGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-475 |
5.25e-160 |
|
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: 461.82 E-value: 5.25e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 6 SLIDGQWAGGAG--DSENINPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLA 83
Cdd:cd07131 1 NYIGGEWVDSASgeTFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 84 HILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPAL 163
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 164 ACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKK 243
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 244 LQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPV 323
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 324 SNGAQFDKDLSYIALARDEAQRV-IGGAALQR--AQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIA 400
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLlLGGERLTGggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1837855989 401 NDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGASSYGSSEQGHYAREFFTSLKTSYI 475
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-472 |
2.28e-148 |
|
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: 431.22 E-value: 2.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07093 33 PGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDIPRAAANFRFFADYILQLDGESYPQDGGALNY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EIsREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07093 113 VL-RQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07093 192 VAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGG---AALQRAQRGYYLQPCLALDV 369
Cdd:cd07093 272 IYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGggrPELPDLEGGYFVEPTVITGL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmpTSGV-DFHVPFGG 448
Cdd:cd07093 352 DNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN--CWLVrDLRTPFGG 429
|
410 420
....*....|....*....|....
gi 1837855989 449 RGASSYGsSEQGHYAREFFTSLKT 472
Cdd:cd07093 430 VKASGIG-REGGDYSLEFYTELKN 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-475 |
4.83e-145 |
|
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: 423.51 E-value: 4.83e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 6 SLIDGQWAGGAGDS-ENINPSDLSaPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAH 84
Cdd:cd07086 1 GVIGGEWVGSGGETfTSRNPANGE-PIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 85 ILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALA 164
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 165 CGNAVVLKPSEFTPATAVMLAEIIRAA----GVPDGVFNLVLGtGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAG 240
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 241 HKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQI 320
Cdd:cd07086 239 FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 321 GPVSNGAQFDKDLSYIALARDEAQRVI-GGAALQRAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAI 399
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLtGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1837855989 400 ANDTEYGLSAGICTQSLKHATHFRRHVQS--GLAMVNMPTSGVDFHVPFGGRGASSyGSSEQGHYAREFFTSLKTSYI 475
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNIPTSGAEIGGAFGGEKETG-GGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
53-472 |
5.12e-144 |
|
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: 419.91 E-value: 5.12e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07103 32 FKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRIYGRTIPSPAPGKRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07103 112 LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07103 192 CASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALqrAQRGYYLQPCLALDVSL 371
Cdd:cd07103 272 IYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKgAKVLTGGKRL--GLGGYFYEPTVLTDVTD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGvDFHVPFGGRGA 451
Cdd:cd07103 350 DMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLIS-DAEAPFGGVKE 428
|
410 420
....*....|....*....|.
gi 1837855989 452 SSYGsSEQGHYAREFFTSLKT 472
Cdd:cd07103 429 SGLG-REGGKEGLEEYLETKY 448
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
53-475 |
7.47e-144 |
|
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: 419.65 E-value: 7.47e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07114 34 GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07114 114 FTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07114 194 VEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRA--QRGYYLQPCLALDV 369
Cdd:cd07114 274 IYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEgARVLTGGERPSGAdlGAGYFFEPTILADV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSgVDFHVPFGGR 449
Cdd:cd07114 354 TNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRA-LSPSSPFGGF 432
|
410 420
....*....|....*....|....*.
gi 1837855989 450 GASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07114 433 KDSGIG-RENGIEAIREYTQTKSVWI 457
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
53-471 |
2.61e-136 |
|
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: 399.60 E-value: 2.61e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPAT-AVMLAEIIRAAGVPDGVFNLVLGTGADVGQV 211
Cdd:cd07104 93 MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 212 LTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTP 291
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQraqrGYYLQPCLALDVSL 371
Cdd:cd07104 253 SVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE----GLFYQPTVLSDVTP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGA 451
Cdd:cd07104 329 DMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEPHVPFGGVKA 408
|
410 420
....*....|....*....|
gi 1837855989 452 SSyGSSEQGHYAREFFTSLK 471
Cdd:cd07104 409 SG-GGRFGGPASLEEFTEWQ 427
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
53-476 |
6.49e-135 |
|
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: 397.06 E-value: 6.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPsIRAGVEV 132
Cdd:cd07090 32 QKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTLSGEHVP-LPGGSFA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGtGADVGQVL 212
Cdd:cd07090 111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07090 190 CEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAALQ---RAQRGYYLQPCLALD 368
Cdd:cd07090 270 IKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLcGGERVVpedGLENGFYVSPCVLTD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN----MPTSgvdfhV 444
Cdd:cd07090 350 CTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINtyniSPVE-----V 424
|
410 420 430
....*....|....*....|....*....|..
gi 1837855989 445 PFGGRGASSYGsSEQGHYAREFFTSLKTSYIR 476
Cdd:cd07090 425 PFGGYKQSGFG-RENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
53-475 |
2.78e-132 |
|
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: 391.29 E-value: 2.78e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSiRAGVEV 132
Cdd:cd07119 50 SGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV-PPHVIS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07119 129 RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAEL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07119 209 AESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEES 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRA--QRGYYLQPCLALDV 369
Cdd:cd07119 289 IHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEgARLVCGGKRPTGDelAKGYFVEPTIFDDV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptsgvDFHV----- 444
Cdd:cd07119 369 DRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN------DYHPyfaea 442
|
410 420 430
....*....|....*....|....*....|.
gi 1837855989 445 PFGGRGASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07119 443 PWGGYKQSGIG-RELGPTGLEEYQETKHINI 472
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
53-472 |
9.04e-131 |
|
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: 383.12 E-value: 9.04e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd06534 87 YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd06534 167 LSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAqrvmalnvghaldersqigpvsngaqfdkdlsyialardeaqrviggaalqraqrgyylqpCLALDVSLD 372
Cdd:cd06534 247 IYDEFVEKLV-------------------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGAS 452
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNS 345
|
410 420
....*....|....*....|
gi 1837855989 453 SYGsSEQGHYAREFFTSLKT 472
Cdd:cd06534 346 GIG-REGGPYGLEEYTRTKT 364
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
54-471 |
6.14e-130 |
|
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: 383.99 E-value: 6.14e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVE 133
Cdd:cd07150 35 PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRGETLPSDSPGTVSM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLT 213
Cdd:cd07150 115 SVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 GHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGI 293
Cdd:cd07150 195 DDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 HDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAalqrAQRGYYLQPCLALDVSLDA 373
Cdd:cd07150 275 YDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGG----KYDGNFYQPTVLTDVTPDM 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 374 RIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGASS 453
Cdd:cd07150 351 RIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASG 430
|
410
....*....|....*...
gi 1837855989 454 YGsSEQGHYAREFFTSLK 471
Cdd:cd07150 431 FG-REGGEWSMEEFTELK 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
56-475 |
1.43e-127 |
|
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: 378.22 E-value: 1.43e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEIS 135
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 136 REPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGH 215
Cdd:cd07118 117 REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 216 PAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHD 295
Cdd:cd07118 197 PDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 296 RFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQrGYYLQPCLALDVSLDAR 374
Cdd:cd07118 277 AFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEgATLLLGGERLASAA-GLFYQPTIFTDVTPDMA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 375 IAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDfHVPFGGRGASSY 454
Cdd:cd07118 356 IAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP-ELPFGGFKQSGI 434
|
410 420
....*....|....*....|.
gi 1837855989 455 GsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07118 435 G-RELGRYGVEEYTELKTVHL 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
54-475 |
2.13e-127 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 377.55 E-value: 2.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARG-EVQRAADIFDYYAGEVFRLGGEMFPsIRAGVEV 132
Cdd:cd07115 33 EAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPRAADTFRYYAGWADKIEGEVIP-VRGPFLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07115 192 VEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAAlQRAQRGYYLQPCLALDVSLD 372
Cdd:cd07115 272 IYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGK-RPGARGFFVEPTIFAAVPPE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPFGGRGAS 452
Cdd:cd07115 351 MRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT-YNRFDPGSPFGGYKQS 429
|
410 420
....*....|....*....|...
gi 1837855989 453 SYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07115 430 GFG-REMGREALDEYTEVKSVWV 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
53-472 |
6.18e-125 |
|
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: 372.23 E-value: 6.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07085 51 FPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGtGADVGQVL 212
Cdd:cd07085 131 YSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07085 210 LDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI--G-GAALQRAQRGYYLQPCLALDV 369
Cdd:cd07085 290 EADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVldGrGVKVPGYENGNFVGPTILDNV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTS-GVDFHvPFGG 448
Cdd:cd07085 370 TPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPvPLAFF-SFGG 448
|
410 420
....*....|....*....|....*
gi 1837855989 449 RGASSYGSSE-QGHYAREFFTSLKT 472
Cdd:cd07085 449 WKGSFFGDLHfYGKDGVRFYTQTKT 473
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-462 |
1.72e-124 |
|
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: 372.33 E-value: 1.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 2 RTITSLIDGQWAGGAGDSENINPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQ 81
Cdd:cd07124 31 REYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 82 LAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGemFPSIRAGVEVEISR-EPLGVVALITPWNFPIAIPAWKTA 160
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRG--FPVEMVPGEDNRYVyRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 161 PALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAG 240
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 241 H------KKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHAL 314
Cdd:cd07124 269 QpgqkwlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 315 DERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYE 394
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 395 HALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSG--VDFHvPFGGRGASSYGSSEQGHY 462
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGalVGRQ-PFGGFKMSGTGSKAGGPD 497
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
54-471 |
1.11e-123 |
|
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: 368.22 E-value: 1.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRL---GGEMFPSIRAGV 130
Cdd:cd07110 33 PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLdakAERAVPLPSEDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 EVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQ 210
Cdd:cd07110 113 KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 211 VLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVT 290
Cdd:cd07110 193 PLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVH 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 291 PGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQRGYYLQPCLALDV 369
Cdd:cd07110 273 ESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEgARLLCGGRRPAHLEKGYFIAPTVFADV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSgVDFHVPFGGR 449
Cdd:cd07110 353 PTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQP-CFPQAPWGGY 431
|
410 420
....*....|....*....|..
gi 1837855989 450 GASSYGsSEQGHYAREFFTSLK 471
Cdd:cd07110 432 KRSGIG-RELGEWGLDNYLEVK 452
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
56-475 |
5.61e-123 |
|
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: 367.30 E-value: 5.61e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPE-ARGEVQRAADIFDYYAGEVFRLGGEMFPsIRAGVEVEI 134
Cdd:cd07091 59 WRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIP-IDGNFLAYT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 135 SREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTG 214
Cdd:cd07091 138 RREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 215 HPAVAGVSFTGSSATGRKIA-ASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGI 293
Cdd:cd07091 218 HMDVDKIAFTGSTAVGRTIMeAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 HDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAalQRAQRGYYLQPCLALDVSLD 372
Cdd:cd07091 298 YDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEgATLLTGGE--RHGSKGYFIQPTVFTDVKDD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptSGVDFH--VPFGGRG 450
Cdd:cd07091 376 MKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDaaVPFGGFK 452
|
410 420
....*....|....*....|....*
gi 1837855989 451 ASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07091 453 QSGFG-RELGEEGLEEYTQVKAVTI 476
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
53-471 |
2.32e-122 |
|
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: 365.29 E-value: 2.32e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMFPSiRAGVE 131
Cdd:TIGR01804 48 QGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPL-GGPSF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQV 211
Cdd:TIGR01804 127 AYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 212 LTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTP 291
Cdd:TIGR01804 207 LVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRV-IGGAALQRA--QRGYYLQPCLALD 368
Cdd:TIGR01804 287 KIKERFLARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLaTGGGRPENVglQNGFFVEPTVFAD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptsgvDFH----- 443
Cdd:TIGR01804 367 CTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWIN------TYNlypae 440
|
410 420
....*....|....*....|....*...
gi 1837855989 444 VPFGGRGASSYGsSEQGHYAREFFTSLK 471
Cdd:TIGR01804 441 APFGGYKQSGIG-RENGKAALAHYTEVK 467
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
8-475 |
2.28e-121 |
|
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: 362.74 E-value: 2.28e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 8 IDGQWAGGAGDS--ENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHI 85
Cdd:cd07088 2 INGEFVPSSSGEtiDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 86 LASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALAC 165
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 166 GNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQ 245
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 246 MEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSN 325
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 326 GAQFDKDLSYIALARDE-AQRVIGGAALQRaQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTE 404
Cdd:cd07088 321 EAALDKVEEMVERAVEAgATLLTGGKRPEG-EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1837855989 405 YGLSAGICTQSLKHATHFRRHVQSGLAMVNM----PTSGvdFHvpfGGRGASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINRenfeAMQG--FH---AGWKKSGLG-GADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
8-472 |
4.17e-121 |
|
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: 361.82 E-value: 4.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 8 IDGQW--AGGAGDSENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHI 85
Cdd:cd07138 3 IDGAWvaPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 86 LASEQGKTLPEARG-EVQRAADIFDYYAGEVfrlggEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALA 164
Cdd:cd07138 82 ITLEMGAPITLARAaQVGLGIGHLRAAADAL-----KDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 165 CGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKL 244
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 245 QMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVS 324
Cdd:cd07138 237 ALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 325 NGAQFDKDLSYIALARDE-AQRVIGGAAL-QRAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIAND 402
Cdd:cd07138 317 SAAQFDRVQGYIQKGIEEgARLVAGGPGRpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIAND 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 403 TEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPtsGVDFHVPFGGRGASSYGsSEQGHYAREFFTSLKT 472
Cdd:cd07138 397 TPYGLAGYVWSADPERARAVARRLRAGQVHINGA--AFNPGAPFGGYKQSGNG-REWGRYGLEEFLEVKS 463
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
53-475 |
1.67e-120 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 361.12 E-value: 1.67e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILK---DIGRgivANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMFPsIRA 128
Cdd:PRK13252 57 QKIWAAMTAMERSRILRravDILR---ERNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIP-LRG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 129 GVEVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGaDV 208
Cdd:PRK13252 133 GSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLI 288
Cdd:PRK13252 212 GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 289 VTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQR-VIGGAALQR--AQRGYYLQPCL 365
Cdd:PRK13252 292 VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARlLCGGERLTEggFANGAFVAPTV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 366 ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmpTSGV-DFHV 444
Cdd:PRK13252 372 FTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN--TWGEsPAEM 449
|
410 420 430
....*....|....*....|....*....|.
gi 1837855989 445 PFGGRGASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:PRK13252 450 PVGGYKQSGIG-RENGIATLEHYTQIKSVQV 479
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
55-472 |
3.09e-119 |
|
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: 356.93 E-value: 3.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 55 GWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPsIRAGVEVEI 134
Cdd:cd07109 35 GWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLHGETIP-LGPGYFVYT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 135 SREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTG 214
Cdd:cd07109 114 VREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 215 HPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIH 294
Cdd:cd07109 194 HPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 295 DRFVQELAQRVMALNVGHALDERSqIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAALQ-RAQRGYYLQPCLALDVSLD 372
Cdd:cd07109 274 DEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGFVARARARGARIVaGGRIAEgAPAGGYFVAPTLLDDVPPD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGAS 452
Cdd:cd07109 353 SRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKS 432
|
410 420
....*....|....*....|
gi 1837855989 453 SYGsSEQGHYAREFFTSLKT 472
Cdd:cd07109 433 GHG-REKGLEALYNYTQTKT 451
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
53-475 |
9.99e-119 |
|
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: 355.30 E-value: 9.99e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAG-----EVFRLGgemfpsir 127
Cdd:cd07106 32 FPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASldlpdEVIEDD-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 128 AGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGtGAD 207
Cdd:cd07106 104 DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 208 VGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRL 287
Cdd:cd07106 182 LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 288 IVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAALQRaqRGYYLQPCLA 366
Cdd:cd07106 262 YVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLaGGEPLDG--PGYFIPPTIV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 367 LDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTsGVDFHVPF 446
Cdd:cd07106 340 DDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHG-ALDPDAPF 418
|
410 420
....*....|....*....|....*....
gi 1837855989 447 GGRGASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07106 419 GGHKQSGIG-VEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
53-472 |
6.51e-118 |
|
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: 353.59 E-value: 6.51e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTL-PEARGEVQRAADIFDYYAGEVFRLGGEMFPsIRAGVE 131
Cdd:cd07108 32 FPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGGLAGELKGETLP-FGPDVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIrAAGVPDGVFNLVLGTGADVGQV 211
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEIL-AQVLPAGVLNVITGYGEECGAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 212 LTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGA-FHATGQRCTASSRLIVT 290
Cdd:cd07108 190 LVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 291 PGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQ-RVIGGAALQRAQR---GYYLQPCLA 366
Cdd:cd07108 270 EDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTSGaTVLRGGPLPGEGPladGFFVQPTIF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 367 LDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPF 446
Cdd:cd07108 350 SGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ-GGGQQPGQSY 428
|
410 420
....*....|....*....|....*.
gi 1837855989 447 GGRGASSYGSSEQGHYAREFFTSLKT 472
Cdd:cd07108 429 GGFKQSGLGREASLEGMLEHFTQKKT 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
53-471 |
7.90e-118 |
|
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: 353.17 E-value: 7.90e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVE 131
Cdd:cd07092 32 FPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPGAVDNFRFFAGAARTLEGPAAGEYLPGHT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIrAAGVPDGVFNLVLGTGADVGQV 211
Cdd:cd07092 112 SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELA-AEVLPPGVVNVVCGGGASAGDA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 212 LTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTP 291
Cdd:cd07092 191 LVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRaqRGYYLQPCLALDVSL 371
Cdd:cd07092 271 SVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTGGRRAEG--PGYFYEPTVVAGVAQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN---MPTSgvdfHVPFGG 448
Cdd:cd07092 349 DDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNthiPLAA----EMPHGG 424
|
410 420
....*....|....*....|...
gi 1837855989 449 RGASSYGsSEQGHYAREFFTSLK 471
Cdd:cd07092 425 FKQSGYG-KDLSIYALEDYTRIK 446
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
56-475 |
1.16e-117 |
|
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: 353.06 E-value: 1.16e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMFPSiRAGVEVEI 134
Cdd:cd07112 42 WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALaVDVPSAANTFRWYAEAIDKVYGEVAPT-GPDALALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 135 SREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTG 214
Cdd:cd07112 121 TREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 215 HPAVAGVSFTGSSATGRK-IAASAVAGHKKLQMEMGGKNPLVVLDDA-DLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07112 201 HMDVDALAFTGSTEVGRRfLEYSGQSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHES 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQRGYYLQPCLALDVSL 371
Cdd:cd07112 281 IKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEgARLVAGGKRVLTETGGFFVEPTVFDGVTP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPFGGRGA 451
Cdd:cd07112 361 DMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNC-FDEGDITTPFGGFKQ 439
|
410 420
....*....|....*....|....
gi 1837855989 452 SSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07112 440 SGNG-RDKSLHALDKYTELKTTWI 462
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
56-455 |
8.69e-117 |
|
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: 351.11 E-value: 8.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGevfrLGGEM-FPSIRAGV--- 130
Cdd:cd07139 54 WPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrAQGPGPAALLRYYAA----LARDFpFEERRPGSggg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 EVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGtGADVGQ 210
Cdd:cd07139 130 HVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 211 VLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVT 290
Cdd:cd07139 209 YLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 291 PGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQRGYYLQPCLALDV 369
Cdd:cd07139 289 RSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEgARLVTGGGRPAGLDRGWFVEPTLFADV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTsgVDFHVPFGGR 449
Cdd:cd07139 369 DNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR--LDFGAPFGGF 446
|
....*.
gi 1837855989 450 GASSYG 455
Cdd:cd07139 447 KQSGIG 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
53-471 |
1.51e-115 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 348.99 E-value: 1.51e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:PLN02278 75 FPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:PLN02278 155 LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDAL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:PLN02278 235 LASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAqrGYYLQPCLALDVSL 371
Cdd:PLN02278 315 IYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKgAKVLLGGKRHSLG--GTFYEPTVLGDVTE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMptsGVDFHV--PFGGR 449
Cdd:PLN02278 393 DMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNE---GLISTEvaPFGGV 469
|
410 420
....*....|....*....|..
gi 1837855989 450 GASSYGsSEQGHYAREFFTSLK 471
Cdd:PLN02278 470 KQSGLG-REGSKYGIDEYLEIK 490
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
56-476 |
4.85e-115 |
|
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: 346.74 E-value: 4.85e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARG-EVQRAADIFDYYAGEVFRLGGE-MFPSIRAGVEVE 133
Cdd:cd07113 54 WAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGEtLAPSIPSMQGER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 IS----REPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGaDVG 209
Cdd:cd07113 134 YTaftrREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 210 QVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIV 289
Cdd:cd07113 213 AQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 290 TPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAALqrAQRGYYLQPCLALD 368
Cdd:cd07113 293 HRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVrGGEAL--AGEGYFVQPTLVLA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSgVDFHVPFGG 448
Cdd:cd07113 371 RSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTF-LDPAVPFGG 449
|
410 420 430
....*....|....*....|....*....|.
gi 1837855989 449 RGASSYGSSeqghYAREF---FTSLKTSYIR 476
Cdd:cd07113 450 MKQSGIGRE----FGSAFiddYTELKSVMIR 476
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
56-472 |
5.52e-114 |
|
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: 343.56 E-value: 5.52e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSirAGVE---- 131
Cdd:cd07145 37 MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRGETIPV--DAYEyner 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 --VEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVG 209
Cdd:cd07145 115 riAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 210 QVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIV 289
Cdd:cd07145 195 DEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 290 TPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAalqRAQRGYYLQPCLALDV 369
Cdd:cd07145 275 EEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGG---KRDEGSFFPPTVLEND 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGR 449
Cdd:cd07145 352 TPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGF 431
|
410 420
....*....|....*....|...
gi 1837855989 450 GASSYGsSEQGHYAREFFTSLKT 472
Cdd:cd07145 432 KKSGIG-REGVRYTMLEMTEEKT 453
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
56-477 |
6.81e-114 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 344.79 E-value: 6.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVE---V 132
Cdd:PLN02467 66 WARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMEtfkG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:PLN02467 146 YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:PLN02467 226 ASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHER 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQRGYYLQPCLALDVSL 371
Cdd:PLN02467 306 IASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEgATILCGGKRPEHLKKGFFIEPTIITDVTT 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmpTSGVDF-HVPFGGRG 450
Cdd:PLN02467 386 SMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFcQAPWGGIK 463
|
410 420
....*....|....*....|....*....
gi 1837855989 451 ASSYGsSEQGHYAREFFTSLK--TSYIRP 477
Cdd:PLN02467 464 RSGFG-RELGEWGLENYLSVKqvTKYISD 491
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-456 |
1.59e-113 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 343.04 E-value: 1.59e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 7 LIDGQWAGGAGDSENI-NPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHI 85
Cdd:PRK13473 6 LINGELVAGEGEKQPVyNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 86 LASEQGKTLPEARG-EVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALA 164
Cdd:PRK13473 85 ESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 165 CGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKL 244
Cdd:PRK13473 165 AGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 245 QMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVS 324
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 325 NGAQFDKDLSYIALARDE--AQRVIGGAALQRAqrGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIAND 402
Cdd:PRK13473 324 SAAHRDRVAGFVERAKALghIRVVTGGEAPDGK--GYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAND 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1837855989 403 TEYGLSAGICTQSLKHATHFRRHVQSGLAMVN---MPTSgvdfHVPFGGRGASSYGS 456
Cdd:PRK13473 402 SDYGLASSVWTRDVGRAHRVSARLQYGCTWVNthfMLVS----EMPHGGQKQSGYGK 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
58-472 |
3.06e-113 |
|
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: 341.53 E-value: 3.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 58 ATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR--------GEVQRAADIFDYYAGEvFRLGGEMFPSIRAG 129
Cdd:cd07089 38 STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARamqvdgpiGHLRYFADLADSFPWE-FDLPVPALRGGPGR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 130 VEVEisREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVG 209
Cdd:cd07089 117 RVVR--REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 210 QVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIV 289
Cdd:cd07089 195 EALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 290 TPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQRGYYLQPCLALD 368
Cdd:cd07089 275 PRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEgARLVTGGGRPAGLDKGFYVEPTLFAD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmPTSGVDFHVPFGG 448
Cdd:cd07089 355 VDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-GGGGYGPDAPFGG 433
|
410 420
....*....|....*....|....
gi 1837855989 449 RGASSYGsSEQGHYAREFFTSLKT 472
Cdd:cd07089 434 YKQSGLG-RENGIEGLEEFLETKS 456
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
10-471 |
7.44e-113 |
|
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: 340.82 E-value: 7.44e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 10 GQWAGGAG--DSENINPSD----LSAPvclvaQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLA 83
Cdd:cd07151 1 GEWRDGTSerTIDVLNPYTgetlAEIP-----AASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 84 HILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPAL 163
Cdd:cd07151 76 EWLIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 164 ACGNAVVLKPSEFTPATA-VMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHK 242
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 243 KLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGP 322
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 323 VSNGAQFDKDLSYIALARDE-AQRVIGGAAlqraqRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIAN 401
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEgATLLVGGEA-----EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 402 DTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGASSYGSSeQGHYAREFFTSLK 471
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRF-NGEWALEEFTTDK 459
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
53-466 |
2.58e-110 |
|
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: 332.89 E-value: 2.58e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYA--GEVFrLGGEMFPSirAGV 130
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenAEAF-LADEPIET--DAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 EVEISREPLGVVALITPWNFPIaipaWKT----APALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGA 206
Cdd:cd07100 89 KAYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 207 DVGQVLtGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSR 286
Cdd:cd07100 165 QVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 287 LIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAqrGYYLQPCL 365
Cdd:cd07100 244 FIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAgATLLLGGKRPDGP--GAFYPPTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 366 ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTsGVDFHVP 445
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMV-KSDPRLP 400
|
410 420
....*....|....*....|..
gi 1837855989 446 FGGRGASSYGsSEQGHYA-REF 466
Cdd:cd07100 401 FGGVKRSGYG-RELGRFGiREF 421
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
8-475 |
1.44e-109 |
|
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: 333.22 E-value: 1.44e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 8 IDGQWAGGAGDS--ENINPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHI 85
Cdd:cd07144 12 INNEFVKSSDGEtiKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 86 LASEQGKTL-PEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEIsREPLGVVALITPWNFPIAIPAWKTAPALA 164
Cdd:cd07144 92 EALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTL-HEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 165 CGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKL 244
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 245 QMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVM-ALNVGHALDERSQIGPV 323
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 324 SNGAQFDKDLSYIALARDEAQRVI--GGAALQRAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIAN 401
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVygGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKAN 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1837855989 402 DTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGvDFHVPFGGRGASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07144 411 DTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDS-DVGVPFGGFKMSGIG-RELGEYGLETYTQTKAVHI 482
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
54-471 |
6.87e-107 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 325.15 E-value: 6.87e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVE 133
Cdd:TIGR01780 33 KTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEILYAASFLEWFAEEAKRVYGDTIPSPQSDKRLI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGA-DVGQVL 212
Cdd:TIGR01780 113 VIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSALALARLAEQAGIPKGVLNVITGSRAkEVGNVL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:TIGR01780 193 TTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAalQRAQRG-YYLQPCLALDVSL 371
Cdd:TIGR01780 273 IYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAVEKGAKVVTGG--KRHELGgNFFEPTVLSNVTA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN--MPTSGVdfhVPFGGR 449
Cdd:TIGR01780 351 DMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWRVAEALEYGMVGINtgLISNVV---APFGGV 427
|
410 420
....*....|....*....|..
gi 1837855989 450 GASSYGsSEQGHYAREFFTSLK 471
Cdd:TIGR01780 428 KQSGLG-REGSKYGIEEYLETK 448
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
64-472 |
8.01e-107 |
|
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: 324.93 E-value: 8.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 64 RAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFP-SIRAGVEVEIS---REPL 139
Cdd:cd07149 45 RAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRLAGETIPfDASPGGEGRIGftiREPI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 140 GVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVA 219
Cdd:cd07149 125 GVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 220 GVSFTGSSATGRKIAASavAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQ 299
Cdd:cd07149 205 MISFTGSPAVGEAIARK--AGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 300 ELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAalQRaqRGYYLQPCLALDVSLDARIAREE 379
Cdd:cd07149 283 RFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGG--KR--DGAILEPTVLTDVPPDMKVVCEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 380 VFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN-MPTSGVDfHVPFGGRGASSYGsSE 458
Cdd:cd07149 359 VFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdSSTFRVD-HMPYGGVKESGTG-RE 436
|
410
....*....|....
gi 1837855989 459 QGHYAREFFTSLKT 472
Cdd:cd07149 437 GPRYAIEEMTEIKL 450
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
7-455 |
7.40e-106 |
|
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: 323.53 E-value: 7.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 7 LIDGQWAGGAGDS--ENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAH 84
Cdd:cd07559 4 FINGEWVAPSKGEyfDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 85 ILASEQGKTLPEARG-EVQRAADIFDYYAGevfrlggemfpSIRA--GVEVEIS--------REPLGVVALITPWNFPIA 153
Cdd:cd07559 83 AETLDNGKPIRETLAaDIPLAIDHFRYFAG-----------VIRAqeGSLSEIDedtlsyhfHEPLGVVGQIIPWNFPLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 154 IPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKI 233
Cdd:cd07559 152 MAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 234 AASAVAGHKKLQMEMGGKNPLVVLDDA-DLEIALACALDGAFHA----TGQRCTASSRLIVTPGIHDRFVQELAQRVMAL 308
Cdd:cd07559 231 MQYAAENLIPVTLELGGKSPNIFFDDAmDADDDFDDKAEEGQLGfafnQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 309 NVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQ--RGYYLQPCLALDVSLDARIAREEVFGPLA 385
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEgAEVLTGGERLTLGGldKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1837855989 386 CVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN----MPTsgvdfHVPFGGRGASSYG 455
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIG 459
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
53-472 |
5.32e-105 |
|
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: 320.15 E-value: 5.32e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPS-IRAGVE 131
Cdd:cd07094 34 AENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAERIRGEEIPLdATQGSD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEIS---REPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADV 208
Cdd:cd07094 114 NRLAwtiREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTGHPAVAGVSFTGSSATGRKIAASavAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLI 288
Cdd:cd07094 194 GDAFAADERVAMLSFTGSAAVGEALRAN--AGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 289 VTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQraqrGYYLQPCLALD 368
Cdd:cd07094 272 VHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGERD----GALFKPTVLED 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGG 448
Cdd:cd07094 348 VPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGG 427
|
410 420
....*....|....*....|....
gi 1837855989 449 RGASSYGsSEQGHYAREFFTSLKT 472
Cdd:cd07094 428 VKESGVG-REGVPYAMEEMTEEKT 450
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
53-458 |
6.19e-105 |
|
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: 320.09 E-value: 6.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07107 32 FPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EIsREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07107 112 TL-REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGA-FHATGQRCTASSRLIVTP 291
Cdd:cd07107 190 VRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI--GGAALQRA-QRGYYLQPCLALD 368
Cdd:cd07107 270 SIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVtgGGRPEGPAlEGGFYVEPTVFAD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptsGVDFH---VP 445
Cdd:cd07107 350 VTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWIN----GSSRHflgAP 425
|
410
....*....|...
gi 1837855989 446 FGGRGASSYGSSE 458
Cdd:cd07107 426 FGGVKNSGIGREE 438
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
64-472 |
1.01e-104 |
|
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: 319.30 E-value: 1.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 64 RAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPS-------IRAGVEVeisR 136
Cdd:cd07146 42 RSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCdltangkARKIFTL---R 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 137 EPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHP 216
Cdd:cd07146 119 EPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 217 AVAGVSFTGSSATGRKIAASavAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDR 296
Cdd:cd07146 199 DVDLVTFTGGVAVGKAIAAT--AGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 297 FVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAalQRaqRGYYLQPCLALDVSLDARIA 376
Cdd:cd07146 277 FVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGN--QR--QGALYAPTVLDHVPPDAELV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 377 REEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptSGVDF---HVPFGGRGASS 453
Cdd:cd07146 353 TEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPGFrseLSPFGGVKDSG 429
|
410
....*....|....*....
gi 1837855989 454 YGSSEQGHYAREFFTSLKT 472
Cdd:cd07146 430 LGGKEGVREAMKEMTNVKT 448
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
56-476 |
3.14e-103 |
|
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: 316.60 E-value: 3.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMFPSirAGVEVEI 134
Cdd:cd07141 63 WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPM--DGDFFTY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 135 SR-EPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLT 213
Cdd:cd07141 141 TRhEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAIS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 GHPAVAGVSFTGSSATGRKIA-ASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07141 221 SHPDIDKVAFTGSTEVGKLIQqAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQES 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAAlqRAQRGYYLQPCLALDVSL 371
Cdd:cd07141 301 IYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEgAKLECGGKR--HGDKGYFIQPTVFSDVTD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPtSGVDFHVPFGGRGA 451
Cdd:cd07141 379 DMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCY-NVVSPQAPFGGYKM 457
|
410 420
....*....|....*....|....*
gi 1837855989 452 SSYGsSEQGHYAREFFTSLKTSYIR 476
Cdd:cd07141 458 SGNG-RELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
53-466 |
9.79e-103 |
|
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: 314.54 E-value: 9.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYY---AGEV----FRLGGEMFPS 125
Cdd:cd07099 31 QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAarnAPRVlaprKVPTGLLMPN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 126 IRAGVEveisREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTG 205
Cdd:cd07099 111 KKATVE----YRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 206 AdVGQVLTGHPaVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASS 285
Cdd:cd07099 187 A-TGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 286 RLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYI--ALARDeAQRVIGGAalQRAQRGYYLQP 363
Cdd:cd07099 265 RVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVddAVAKG-AKALTGGA--RSNGGGPFYEP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 364 CLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN--MPTSGVd 441
Cdd:cd07099 342 TVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdvLLTAGI- 420
|
410 420
....*....|....*....|....*
gi 1837855989 442 FHVPFGGRGASSYGSSEQGHYAREF 466
Cdd:cd07099 421 PALPFGGVKDSGGGRRHGAEGLREF 445
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
56-452 |
1.02e-102 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 316.49 E-value: 1.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEIS 135
Cdd:PRK03137 89 WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 136 REPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGH 215
Cdd:PRK03137 169 YIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDH 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 216 PAVAGVSFTGSSATGRKI---AASAVAGHKKLQ---MEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIV 289
Cdd:PRK03137 249 PKTRFITFTGSREVGLRIyerAAKVQPGQIWLKrviAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 290 TPGIHDRFVQELAQRVMALNVGHAlDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRaqRGYYLQPCLALDV 369
Cdd:PRK03137 329 HEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDS--KGYFIQPTIFADV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSG--VDFHvPFG 447
Cdd:PRK03137 406 DPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGaiVGYH-PFG 484
|
....*
gi 1837855989 448 GRGAS 452
Cdd:PRK03137 485 GFNMS 489
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
7-472 |
3.07e-102 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 315.27 E-value: 3.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 7 LIDGQWAGGAGDSENINPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHIL 86
Cdd:TIGR01237 36 VINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 87 ASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALACG 166
Cdd:TIGR01237 116 VKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 167 NAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKI---AASAVAGHKK 243
Cdd:TIGR01237 196 NCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIferAAKVQPGQKH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 244 LQ---MEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQI 320
Cdd:TIGR01237 276 LKrviAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 321 GPVSNGAQFDKDLSYIALARDEAQRVIGGAAlqRAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIA 400
Cdd:TIGR01237 356 GPVIDQKSFNKIMEYIEIGKAEGRLVSGGCG--DDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIA 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1837855989 401 NDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSG--VDFHvPFGGRGASSYGSSEQGHYAREFFTSLKT 472
Cdd:TIGR01237 434 NNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGaiVGYQ-PFGGFKMSGTDSKAGGPDYLALFMQAKT 506
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
53-468 |
2.19e-101 |
|
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: 310.76 E-value: 2.19e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07152 26 QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 eISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATA-VMLAEIIRAAGVPDGVFNlVLGTGADVGQV 211
Cdd:cd07152 106 -ARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLH-VLPGGADAGEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 212 LTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTP 291
Cdd:cd07152 184 LVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQraqrGYYLQPCLALDVSL 371
Cdd:cd07152 264 SVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYD----GLFYRPTVLSGVKP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGA 451
Cdd:cd07152 340 GMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGGMGA 419
|
410
....*....|....*..
gi 1837855989 452 SSYGSSEQGHYAREFFT 468
Cdd:cd07152 420 SGNGSRFGGPANWEEFT 436
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
62-476 |
7.02e-101 |
|
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: 310.61 E-value: 7.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 62 AARAQILKDIGRGIVANSQQLAHILASEQGKTLPE-ARGEVQRAADIFDYYAGEVFRLGGEMfpsiragVEVEISR---- 136
Cdd:cd07143 68 SKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKRVDVQASADTFRYYGGWADKIHGQV-------IETDIKKltyt 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 137 --EPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTG 214
Cdd:cd07143 141 rhEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 215 HPAVAGVSFTGSSATGRKI-AASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGI 293
Cdd:cd07143 221 HMDIDKVAFTGSTLVGRKVmEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 HDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAAlQRAQRGYYLQPCLALDVSLDA 373
Cdd:cd07143 301 YDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGK-RHGNEGYFIEPTIFTDVTEDM 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 374 RIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSgVDFHVPFGGRGASS 453
Cdd:cd07143 380 KIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNL-LHHQVPFGGYKQSG 458
|
410 420
....*....|....*....|...
gi 1837855989 454 YGsSEQGHYAREFFTSLKTSYIR 476
Cdd:cd07143 459 IG-RELGEYALENYTQIKAVHIN 480
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
4-477 |
1.74e-100 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 309.73 E-value: 1.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 4 ITSLIDGQWAGGAGDSENINPSD--LSAPVClvAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQ 81
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANINPVDgrVIARVH--EAGAAEVDAAVAAARAALKGPWGKMTVAERADLLYAVADEIERRFDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 82 LAHILASEQGKTLPEARG-EVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEIS---REPLGVVALITPWNFPIAIPAW 157
Cdd:TIGR03216 79 FLAAEVADTGKPRSLASHlDIPRGAANFRVFADVVKNAPTECFEMATPDGKGALNyavRKPLGVVGVISPWNLPLLLMTW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 158 KTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGAD-VGQVLTGHPAVAGVSFTGSSATGRKIAAS 236
Cdd:TIGR03216 159 KVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPDsAGEFLTRHPGVDAITFTGETRTGSAIMKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 237 AVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDE 316
Cdd:TIGR03216 239 AADGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 317 RSQIGPVSNGAQFDKDLSYIALARDEAQRVI--GGAALQRAQR--GYYLQPCLALDVSLDARIAREEVFGPLACVLRAQD 392
Cdd:TIGR03216 319 ATNMGPLISAEHRDKVLSYYALAVEEGATVVtgGGVPDFGDALagGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 393 YEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptSGV--DFHVPFGGRGASSYGsSEQGHYAREFFTSL 470
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVN---SWFlrDLRTPFGGSKLSGIG-REGGVHSLEFYTEL 474
|
....*..
gi 1837855989 471 KTSYIRP 477
Cdd:TIGR03216 475 TNVCIKL 481
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
7-472 |
1.89e-99 |
|
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: 306.81 E-value: 1.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 7 LIDGQWAGGAGDSENI-NPSDL----SAPVClvaqaSAQQAAQAVEAARRAQPGWAAT-GLAARAQILKDIGRGIVANSQ 80
Cdd:cd07082 5 LINGEWKESSGKTIEVySPIDGevigSVPAL-----SALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 81 QLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRA----GVEVEISREPLGVVALITPWNFPIAIPA 156
Cdd:cd07082 80 EVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFpgtkGKIAQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 157 WKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAAS 236
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 237 avAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDE 316
Cdd:cd07082 240 --HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 317 RSQIGPV--SNGAQFDKDLSYIALARDeAQRVIGGaalqRAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYE 394
Cdd:cd07082 318 GVDITPLidPKSADFVEGLIDDAVAKG-ATVLNGG----GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 395 HALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN-MPTSGVDfHVPFGGRGASSYGSseQG-HYAREFFTSLKT 472
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINsKCQRGPD-HFPFLGRKDSGIGT--QGiGDALRSMTRRKG 469
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
62-434 |
6.03e-97 |
|
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: 299.64 E-value: 6.03e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 62 AARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFpSIRAGVEVEISREPLGV 141
Cdd:cd07120 42 RLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMI-EPEPGSFSLVLREPMGV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 142 VALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAA-GVPDGVFNLVLGTGADVGQVLTGHPAVAG 220
Cdd:cd07120 121 AGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 221 VSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQE 300
Cdd:cd07120 201 ISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 301 LAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI--GGAALQRAQRGYYLQPCLALDVSLDARIARE 378
Cdd:cd07120 281 LAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVlrGGPVTEGLAKGAFLRPTLLEVDDPDADIVQE 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1837855989 379 EVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN 434
Cdd:cd07120 361 EIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIN 416
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
53-452 |
1.83e-96 |
|
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: 297.65 E-value: 1.83e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAA---DI----FDYYAGEVFRlggEMfps 125
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAgkiDIsikaYHERTGERAT---PM--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 126 irAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGtG 205
Cdd:cd07095 87 --AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-G 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 206 ADVGQVLTGHPAVAGVSFTGSSATGRKIaASAVAGH--KKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTA 283
Cdd:cd07095 164 RETGEALAAHEGIDGLLFTGSAATGLLL-HRQFAGRpgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 284 SSRLIVTPG-IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKdlsyiALARDEAQRVIGGAALQRAQR----G 358
Cdd:cd07095 243 ARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR-----YLLAQQDLLALGGEPLLAMERlvagT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 359 YYLQPCLaLDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTS 438
Cdd:cd07095 318 AFLSPGI-IDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT 396
|
410
....*....|....
gi 1837855989 439 GVDFHVPFGGRGAS 452
Cdd:cd07095 397 GASSTAPFGGVGLS 410
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
68-434 |
8.37e-96 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 295.11 E-value: 8.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 68 LKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITP 147
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 148 WNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSS 227
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 228 ATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMA 307
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 308 LNVGHALdERSQI--GPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRaQRGYYLQPCLALDVSLDARIAREEVFGPLA 385
Cdd:PRK10090 241 VQFGNPA-ERNDIamGPLINAAALERVEQKVARAVEEGARVALGGKAVE-GKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1837855989 386 CVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN 434
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
64-474 |
1.21e-94 |
|
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: 294.40 E-value: 1.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 64 RAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMFPSiRAGVEVEISREPLGVV 142
Cdd:cd07142 67 RSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPA-DGPHHVYTLHEPIGVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 143 ALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVS 222
Cdd:cd07142 146 GQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 223 FTGSSATGRKIAASAVAGH-KKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQEL 301
Cdd:cd07142 226 FTGSTEVGKIIMQLAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 302 AQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAALqrAQRGYYLQPCLALDVSLDARIAREEV 380
Cdd:cd07142 306 KARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLItGGDRI--GSKGYYIQPTIFSDVKDDMKIARDEI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 381 FGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPFGGRGASSYGsSEQG 460
Cdd:cd07142 384 FGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIG-REKG 461
|
410
....*....|....
gi 1837855989 461 HYAREFFTSLKTSY 474
Cdd:cd07142 462 IYALNNYLQVKAVV 475
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
56-472 |
3.31e-94 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 294.04 E-value: 3.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARG-EVQRAADIFDYYAGEVFRLGGEMFPSIRAgVEVEI 134
Cdd:PLN02766 76 WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGYT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 135 SREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTG 214
Cdd:PLN02766 155 LKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIAS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 215 HPAVAGVSFTGSSATGRKI-AASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGI 293
Cdd:PLN02766 235 HMDVDKVSFTGSTEVGRKImQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 HDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALqrAQRGYYLQPCLALDVSLD 372
Cdd:PLN02766 315 YDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREgATLLTGGKPC--GDKGYYIEPTIFTDVTED 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPFGGRGAS 452
Cdd:PLN02766 393 MKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNC-YFAFDPDCPFGGYKMS 471
|
410 420
....*....|....*....|
gi 1837855989 453 SYGsSEQGHYAREFFTSLKT 472
Cdd:PLN02766 472 GFG-RDQGMDALDKYLQVKS 490
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
56-475 |
3.79e-93 |
|
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: 290.51 E-value: 3.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARG-EVQRAADIFDYYAGeVFRLGGEMFPSIRAGVEVEI 134
Cdd:cd07117 54 WRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFAG-VIRAEEGSANMIDEDTLSIV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 135 SREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGTGADVGQVLTG 214
Cdd:cd07117 133 LREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 215 HPAVAGVSFTGSSATGRKIAASAVaghKKL---QMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTP 291
Cdd:cd07117 212 HPGLDKLAFTGSTEVGRDVAIAAA---KKLipaTLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQ--RGYYLQPCLALD 368
Cdd:cd07117 289 GIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEgAKILTGGHRLTENGldKGFFIEPTLIVN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPFGG 448
Cdd:cd07117 369 VTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNT-YNQIPAGAPFGG 447
|
410 420
....*....|....*....|....*..
gi 1837855989 449 RGASSYGsSEQGHYAREFFTSLKTSYI 475
Cdd:cd07117 448 YKKSGIG-RETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
54-455 |
6.49e-93 |
|
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: 290.07 E-value: 6.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEVFRLGGEMfpsirAGvev 132
Cdd:cd07111 73 ESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLDTEL-----AG--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 eisREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGAdVGQVL 212
Cdd:cd07111 145 ---WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSAL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07111 221 ANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQES 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALqrAQRGYYLQPCLALDVSL 371
Cdd:cd07111 301 VAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEgADVFQPGADL--PSKGPFYPPTLFTNVPP 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmPTSGVDFHVPFGGRGA 451
Cdd:cd07111 379 ASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN-GHNLFDAAAGFGGYRE 457
|
....
gi 1837855989 452 SSYG 455
Cdd:cd07111 458 SGFG 461
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
54-472 |
1.24e-92 |
|
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: 287.55 E-value: 1.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVE 133
Cdd:cd07105 14 PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQV-- 211
Cdd:cd07105 94 VVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEDAPEVve 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 212 -LTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVT 290
Cdd:cd07105 174 aLIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 291 PGIHDRFVQELAQRVMALNVGHAldersQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRAQRGYYLQPCLALDVS 370
Cdd:cd07105 254 ESIADEFVEKLKAAAEKLFAGPV-----VLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPPTILDNVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 371 LDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRG 450
Cdd:cd07105 329 PDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEPTLPHGGVK 408
|
410 420
....*....|....*....|..
gi 1837855989 451 ASSYGSSeQGHYAREFFTSLKT 472
Cdd:cd07105 409 SSGYGRF-NGKWGIDEFTETKW 429
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
54-471 |
3.28e-92 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 288.34 E-value: 3.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVE 133
Cdd:PRK11241 62 PAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLT 213
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 GHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGI 293
Cdd:PRK11241 222 SNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 HDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQrAQRGYYLQPCLALDVSLDA 373
Cdd:PRK11241 302 YDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAH-ELGGNFFQPTILVDVPANA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 374 RIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHAthFRRHVQSGLAMVNMPTSGVDFHV-PFGGRGAS 452
Cdd:PRK11241 381 KVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRV--FRVGEALEYGIVGINTGIISNEVaPFGGIKAS 458
|
410
....*....|....*....
gi 1837855989 453 SYGsSEQGHYAREFFTSLK 471
Cdd:PRK11241 459 GLG-REGSKYGIEDYLEIK 476
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
9-448 |
2.93e-91 |
|
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: 285.64 E-value: 2.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 9 DGQWAGGAGDSENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHILAS 88
Cdd:cd07130 4 DGEWGGGGGVVTSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 89 EQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNA 168
Cdd:cd07130 83 EMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 169 VVLKPSEFTPATAV----MLAEIIRAAGVPDGVFNLVLGtGADVGQVLTGHPAVAGVSFTGSSATGRKIaASAVAGH--K 242
Cdd:cd07130 163 VVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV-GQAVAARfgR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 243 KLqMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGP 322
Cdd:cd07130 241 SL-LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 323 VSNGAQFDKDLSYIALARDEAQRVI-GGAALQRAqrGYYLQPCLAlDVSLDARIAREEVFGPLACVLRAQDYEHALAIAN 401
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLfGGKVIDGP--GNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1837855989 402 DTEYGLSAGICTQSLKHATHFRRHVQS--GLAMVNMPTSGVDFHVPFGG 448
Cdd:cd07130 397 EVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIGTSGAEIGGAFGG 445
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
53-471 |
3.11e-89 |
|
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: 279.52 E-value: 3.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07102 31 QKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGFER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07102 111 YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 tGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07102 191 -ADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHES 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRA-QRGYYLQPCLALDVS 370
Cdd:cd07102 270 IYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKgARALIDGALFPEDkAGGAYLAPTVLTNVD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 371 LDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmPTSGVDFHVPFGGRG 450
Cdd:cd07102 350 HSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN-RCDYLDPALAWTGVK 428
|
410 420
....*....|....*....|.
gi 1837855989 451 ASSYGSSeQGHYAREFFTSLK 471
Cdd:cd07102 429 DSGRGVT-LSRLGYDQLTRPK 448
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-471 |
4.54e-89 |
|
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: 279.13 E-value: 4.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 57 AATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFP---SIRA-GVEV 132
Cdd:cd07147 38 RALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLPldiSARGeGRQG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNlVLGTGADVGQVL 212
Cdd:cd07147 118 LVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFS-VLPCSRDDADLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIaaSAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:cd07147 197 VTDERIKLLSFTGSPAVGWDL--KARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALqraqRGYYLQPCLALDVSLD 372
Cdd:cd07147 275 VYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR----DGALLEPTILEDVPPD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN-MPTSGVDfHVPFGGRGA 451
Cdd:cd07147 351 MEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVPTFRVD-HMPYGGVKD 429
|
410 420
....*....|....*....|
gi 1837855989 452 SSYGsSEQGHYAREFFTSLK 471
Cdd:cd07147 430 SGIG-REGVRYAIEEMTEPR 448
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
22-455 |
8.19e-87 |
|
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: 275.23 E-value: 8.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 22 INPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEV 101
Cdd:cd07125 51 IDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 102 QRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATA 181
Cdd:cd07125 131 REAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 182 VMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIaASAVAGHK----KLQMEMGGKNPLVVL 257
Cdd:cd07125 211 ARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLI-NRALAERDgpilPLIAETGGKNAMIVD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 258 DDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIA 337
Cdd:cd07125 290 STALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 338 LARDEAqRVIGGAALQrAQRGYYLQPCLALDVSLDARiaREEVFGPLACVLRA--QDYEHALAIANDTEYGLSAGIctQS 415
Cdd:cd07125 370 LMRGEA-WLIAPAPLD-DGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFkaEDLDEAIEDINATGYGLTLGI--HS 443
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1837855989 416 L--KHATHFRRHVQSGLAMVNMPTSGVDFHV-PFGGRGASSYG 455
Cdd:cd07125 444 RdeREIEYWRERVEAGNLYINRNITGAIVGRqPFGGWGLSGTG 486
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
54-472 |
5.38e-85 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 269.44 E-value: 5.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVE 133
Cdd:TIGR01722 52 LTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLT 213
Cdd:TIGR01722 132 SIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 gHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTpGI 293
Cdd:TIGR01722 212 -HPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 HDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI---GGAALQRAQRGYYLQPCLALDVS 370
Cdd:TIGR01722 290 ADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLldgRGYKVDGYEEGNWVGPTLLERVP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 371 LDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTS-GVDFHvPFGGR 449
Cdd:TIGR01722 370 PTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPvPLPYF-SFTGW 448
|
410 420
....*....|....*....|....
gi 1837855989 450 GASSYGSSE-QGHYAREFFTSLKT 472
Cdd:TIGR01722 449 KDSFFGDHHiYGKQGTHFYTRGKT 472
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
5-452 |
4.68e-84 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 267.21 E-value: 4.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 5 TSLIDGQWAGGAGDS-ENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLA 83
Cdd:PRK09457 2 TLWINGDWIAGQGEAfESRNPVS-GEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 84 HILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVeISREPLGVVALITPWNFPIAIPAWKTAPAL 163
Cdd:PRK09457 81 EVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAV-LRHRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 164 ACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGtGADVGQVLTGHPAVAGVSFTGSSATGRKIAASaVAGH-- 241
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQ-FAGQpe 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 242 KKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIH-DRFVQELAQRVMALNVGHaLDERSQ- 319
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR-WDAEPQp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 320 -IGPV-SNGAqfdkdlsyiALARDEAQRVI---GGAAL----QRAQRGYYLQPCLaLDVSLDARIAREEVFGPLACVLRA 390
Cdd:PRK09457 317 fMGAViSEQA---------AQGLVAAQAQLlalGGKSLlemtQLQAGTGLLTPGI-IDVTGVAELPDEEYFGPLLQVVRY 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1837855989 391 QDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGAS 452
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGAS 448
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
8-455 |
5.02e-84 |
|
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: 267.05 E-value: 5.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 8 IDGQWAGGAGDS--ENINPSDLSAPVCLVAQASAQQAAQAVEAARRAQPG-WAATGLAARAQILKDIGRGIVANSQQLAH 84
Cdd:cd07140 10 INGEFVDAEGGKtyNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGeWGKMNARDRGRLMYRLADLMEEHQEELAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 85 ILASEQGKTLPEA-RGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEIS---REPLGVVALITPWNFPIAIPAWKTA 160
Cdd:cd07140 90 IESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTltkREPIGVCGIVIPWNYPLMMLAWKMA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 161 PALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAAS-AVA 239
Cdd:cd07140 170 ACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKScAVS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 240 GHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQ 319
Cdd:cd07140 250 NLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 320 IGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAqrGYYLQPCLALDVSLDARIAREEVFGPLACVLRAQ--DYEHA 396
Cdd:cd07140 330 HGPQNHKAHLDKLVEYCERGVKEgATLVYGGKQVDRP--GFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDVDGV 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1837855989 397 LAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPFGGRGASSYG 455
Cdd:cd07140 408 LQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFG 465
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
56-475 |
3.43e-82 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 262.91 E-value: 3.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEA-RGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVeI 134
Cdd:PRK09847 75 WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAM-I 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 135 SREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTG 214
Cdd:PRK09847 154 VREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 215 HPAVAGVSFTGSSATGRKIAASA-VAGHKKLQMEMGGKNPLVVLDDA-DLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:PRK09847 234 HNDIDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGaalQRAQRGYYLQPCLALDVSLD 372
Cdd:PRK09847 314 IADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG---RNAGLAAAIGPTIFVDVDPN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGvDFHVPFGGRGAS 452
Cdd:PRK09847 391 ASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDG-DMTVPFGGYKQS 469
|
410 420
....*....|....*....|...
gi 1837855989 453 SYGSSEQGHyAREFFTSLKTSYI 475
Cdd:PRK09847 470 GNGRDKSLH-ALEKFTELKTIWI 491
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
8-455 |
1.42e-81 |
|
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: 260.46 E-value: 1.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 8 IDGQWAGGAGDS--ENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLAHI 85
Cdd:cd07116 5 IGGEWVAPVKGEyfDNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 86 LASEQGKTLPEARG-EVQRAADIFDYYAGevfrlggemfpSIRA--GVEVEISR--------EPLGVVALITPWNFPIAI 154
Cdd:cd07116 84 ETWDNGKPVRETLAaDIPLAIDHFRYFAG-----------CIRAqeGSISEIDEntvayhfhEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 155 PAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIA 234
Cdd:cd07116 153 ATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 235 ASAVAGHKKLQMEMGGKNPLVVL------DDADLEIALACALDGAFHaTGQRCTASSRLIVTPGIHDRFVQELAQRVMAL 308
Cdd:cd07116 232 QYASENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 309 NVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQR---AQRGYYLQPCLALDVSLdaRIAREEVFGPL 384
Cdd:cd07116 311 KQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEgAEVLTGGERNELgglLGGGYYVPTTFKGGNKM--RIFQEEIFGPV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1837855989 385 ACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN----MPTsgvdfHVPFGGRGASSYG 455
Cdd:cd07116 389 LAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIG 458
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
53-434 |
1.06e-79 |
|
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: 254.93 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLggeMFPSIRAGV-- 130
Cdd:cd07101 31 QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERL---LKPRRRRGAip 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 ---EVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGAD 207
Cdd:cd07101 108 vltRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 208 VGQVLTGHpaVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRL 287
Cdd:cd07101 188 VGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 288 IVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAAlqRAQRG-YYLQPCL 365
Cdd:cd07101 266 YVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLaGGRA--RPDLGpYFYEPTV 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1837855989 366 ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN 434
Cdd:cd07101 344 LTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVN 412
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
64-471 |
1.20e-78 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 254.73 E-value: 1.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 64 RAQILKDIGRGIVANSQQLAHILASEQGKTLPEARG-EVQRAADIFDYYAGEVFRLGGEMFPSiRAGVEVEISREPLGVV 142
Cdd:PLN02466 121 RSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPA-DGPHHVQTLHEPIGVA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 143 ALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVS 222
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 223 FTGSSATGRKI-AASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQEL 301
Cdd:PLN02466 280 FTGSTDTGKIVlELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 302 AQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALqrAQRGYYLQPCLALDVSLDARIAREEV 380
Cdd:PLN02466 360 KARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESgATLECGGDRF--GSKGYYIQPTVFSNVQDDMLIAQDEI 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 381 FGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMpTSGVDFHVPFGGRGASSYGsSEQG 460
Cdd:PLN02466 438 FGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMSGIG-REKG 515
|
410
....*....|.
gi 1837855989 461 HYAREFFTSLK 471
Cdd:PLN02466 516 IYSLNNYLQVK 526
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
56-472 |
3.21e-77 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 249.01 E-value: 3.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEvfrlGGEMF---PSIRAGVEV 132
Cdd:PRK13968 45 WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEH----GPAMLkaePTLVENQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:PRK13968 121 VIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TgHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPG 292
Cdd:PRK13968 201 N-DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 293 IHDRFVQELAQRVMALNVGHALDERSQIGPVsngAQFDkdlsyialARDE------------AQRVIGGAALqrAQRGYY 360
Cdd:PRK13968 280 IASAFTERFVAAAAALKMGDPRDEENALGPM---ARFD--------LRDElhhqveatlaegARLLLGGEKI--AGAGNY 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 361 LQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmPTSGV 440
Cdd:PRK13968 347 YAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN-GYCAS 425
|
410 420 430
....*....|....*....|....*....|..
gi 1837855989 441 DFHVPFGGRGASSYGsSEQGHYAREFFTSLKT 472
Cdd:PRK13968 426 DARVAFGGVKKSGFG-RELSHFGLHEFCNIQT 456
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
53-455 |
7.42e-76 |
|
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: 245.29 E-value: 7.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEAR-GEVQRAADIFDYYAGEvfrlgGE--MFPSIRAG 129
Cdd:cd07098 31 QREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEILVTCEKIRWTLKH-----GEkaLRPESRPG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 130 --------VEVEIsrEPLGVVALITPWNFP---IAIPAwktAPALACGNAVVLKPSEFTPATAVMLAEIIRAA----GVP 194
Cdd:cd07098 106 gllmfykrARVEY--EPLGVVGAIVSWNYPfhnLLGPI---IAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 195 DGVFNLVLGTGaDVGQVLTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAF 274
Cdd:cd07098 181 PDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 275 HATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAalQR 354
Cdd:cd07098 260 QSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGG--KR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 355 AQR-----GYYLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSG 429
Cdd:cd07098 338 YPHpeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETG 417
|
410 420
....*....|....*....|....*....
gi 1837855989 430 laMVNMPTSGVDFHV---PFGGRGASSYG 455
Cdd:cd07098 418 --MVAINDFGVNYYVqqlPFGGVKGSGFG 444
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
53-455 |
1.19e-75 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 246.33 E-value: 1.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLggeMFPSIRAGV-- 130
Cdd:PRK09407 67 QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKL---LAPRRRAGAlp 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 ---EVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGAD 207
Cdd:PRK09407 144 vltKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 208 VGQVLTGHpaVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRL 287
Cdd:PRK09407 224 VGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 288 IVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAAlqRAQRG-YYLQPCL 365
Cdd:PRK09407 302 YVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLaGGKA--RPDLGpLFYEPTV 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 366 ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN---MPTSG-VD 441
Cdd:PRK09407 380 LTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyAAAWGsVD 459
|
410
....*....|....
gi 1837855989 442 fhVPFGGRGASSYG 455
Cdd:PRK09407 460 --APMGGMKDSGLG 471
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
56-475 |
9.39e-75 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 242.34 E-value: 9.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 56 WAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYA--GEVFrLGGEmfPSIRAGV--- 130
Cdd:PRK09406 39 YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAehAEAL-LADE--PADAAAVgas 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 EVEISREPLGVVALITPWNFPIaipaWKT----APALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVF-NLVLGTG 205
Cdd:PRK09406 116 RAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFqTLLVGSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 206 AdVGQVLTgHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASS 285
Cdd:PRK09406 192 A-VEAILR-DPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 286 RLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRaqRGYYLQPC 364
Cdd:PRK09406 270 RFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAgATILCGGKRPDG--PGWFYPPT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 365 LALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN-MPTSGVDFh 443
Cdd:PRK09406 348 VITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINgMTVSYPEL- 426
|
410 420 430
....*....|....*....|....*....|..
gi 1837855989 444 vPFGGRGASSYGSSEQGHYAREfFTSLKTSYI 475
Cdd:PRK09406 427 -PFGGVKRSGYGRELSAHGIRE-FCNIKTVWI 456
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-468 |
2.52e-73 |
|
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: 239.79 E-value: 2.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 1 MRTITSLIDGQWAGGAGDSENINPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQ 80
Cdd:cd07083 16 GRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 81 QLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEmfPSIRAGVEVEISR---EPLGVVALITPWNFPIAIPAW 157
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYP--AVEVVPYPGEDNEsfyVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 158 KTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKI---- 233
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeaa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 234 AASAVAGH--KKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVG 311
Cdd:cd07083 254 ARLAPGQTwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 312 HALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALqrAQRGYYLQPCLALDVSLDARIAREEVFGPLACVLR-- 389
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRL--EGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRyk 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 390 AQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHV-PFGGRGASSYGSSEQG-HYAREFF 467
Cdd:cd07083 412 DDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVqPFGGFKLSGTNAKTGGpHYLRRFL 491
|
.
gi 1837855989 468 T 468
Cdd:cd07083 492 E 492
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
7-460 |
1.97e-68 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 226.95 E-value: 1.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 7 LIDGQW-AGGAGDS-ENINPSDLSAP----VClvaqaSAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQ 80
Cdd:PLN00412 19 YADGEWrTSSSGKSvAITNPSTRKTQykvqAC-----TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 81 QLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGE-------MFPSIRAGVEVEISREPLGVVALITPWNFPIA 153
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 154 IPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSaTGrkI 233
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TG--I 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 234 AASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHA 313
Cdd:PLN00412 251 AISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 314 LDErSQIGPV--SNGAQFDKDLSYIALARdeaqrviGGAALQRAQR-GYYLQPCLALDVSLDARIAREEVFGPLACVLRA 390
Cdd:PLN00412 331 EDD-CDITPVvsESSANFIEGLVMDAKEK-------GATFCQEWKReGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1837855989 391 QDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN-MPTSGVDfHVPFGGRGASSYGSseQG 460
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINsAPARGPD-HFPFQGLKDSGIGS--QG 470
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
54-472 |
5.55e-68 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 228.48 E-value: 5.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVE 133
Cdd:PLN02419 165 PLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGaDVGQVLT 213
Cdd:PLN02419 245 SIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN-DTVNAIC 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 GHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTpGI 293
Cdd:PLN02419 324 DDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFV-GD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 HDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGA---ALQRAQRGYYLQPCLALDVS 370
Cdd:PLN02419 403 AKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGrdiVVPGYEKGNFIGPTILSGVT 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 371 LDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRG 450
Cdd:PLN02419 483 PDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNK 562
|
410 420
....*....|....*....|...
gi 1837855989 451 ASSYGS-SEQGHYAREFFTSLKT 472
Cdd:PLN02419 563 ASFAGDlNFYGKAGVDFFTQIKL 585
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
133-455 |
1.88e-67 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 223.88 E-value: 1.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEII-RAAGVPDGVFNLVLGTGADVGQV 211
Cdd:TIGR04284 136 TLRREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVTSSDHRLGAL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 212 LTGHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALA-CALDGAFHAtGQRCTASSRLIVT 290
Cdd:TIGR04284 216 LAKDPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSmAAFTVCMHA-GQGCAITTRLVVP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 291 PGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQR-VIGGAALQRAQRGYYLQPCLALDV 369
Cdd:TIGR04284 295 RARYDEAVAAAAATMGSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRfACGGGRPADRDRGFFVEPTVIAGL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 370 SLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptSGVDF--HVPFG 447
Cdd:TIGR04284 375 DNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN---GGVWYsaDAPFG 451
|
....*...
gi 1837855989 448 GRGASSYG 455
Cdd:TIGR04284 452 GYKQSGIG 459
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
2-460 |
4.16e-66 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 220.86 E-value: 4.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 2 RTITSLIDGQWAGGAGDSENINPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQ 81
Cdd:PLN02315 19 RNLGCYVGGEWRANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 82 LAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFPSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKTAP 161
Cdd:PLN02315 98 LGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 162 ALACGNAVVLKPSEFTP----ATAVMLAEIIRAAGVPDGVFNLVLGtGADVGQVLTGHPAVAGVSFTGSSATGRKIAASA 237
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 238 VAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDER 317
Cdd:PLN02315 257 NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 318 SQIGPVSNGAQFDKDLSYIALARDEAQRVI-GGAALQRaqRGYYLQPCLaLDVSLDARIAREEVFGPLACVLRAQDYEHA 396
Cdd:PLN02315 337 TLLGPLHTPESKKNFEKGIEIIKSQGGKILtGGSAIES--EGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEA 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1837855989 397 LAIANDTEYGLSAGICTQslKHATHFR----RHVQSGLAMVNMPTSGVDFHVPFGGRGASSyGSSEQG 460
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTR--NPETIFKwigpLGSDCGIVNVNIPTNGAEIGGAFGGEKATG-GGREAG 478
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
63-465 |
1.51e-62 |
|
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: 210.35 E-value: 1.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 63 ARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMFP----SIRAGVEVEISREP 138
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 139 LGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLgTGADVGQVLTGHPAV 218
Cdd:cd07148 125 IGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 219 AGVSFTGSSATGRKIAASAVAGhKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRFV 298
Cdd:cd07148 204 AFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 299 QELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDE-AQRVIGGAALQRAQrgyyLQPCLALDVSLDARIAR 377
Cdd:cd07148 283 QRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAgARLLCGGKRLSDTT----YAPTVLLDPPRDAKVST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 378 EEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTS-GVDFhVPFGGRGASSYGS 456
Cdd:cd07148 359 QEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAfRVDW-MPFAGRRQSGYGT 437
|
....*....
gi 1837855989 457 SEQGHYARE 465
Cdd:cd07148 438 GGIPYTMHD 446
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
4-452 |
3.19e-60 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 213.14 E-value: 3.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 4 ITSLIDGQWA-----GGAGDSENI-NPSDLSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVA 77
Cdd:PRK11904 543 IAAFLEKQWQagpiiNGEGEARPVvSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 78 NSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRL--GGEMFPSIrAGVEVEISREPLGVVALITPWNFPIAIP 155
Cdd:PRK11904 623 NRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLfgAPEKLPGP-TGESNELRLHGRGVFVCISPWNFPLAIF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 156 AWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIaA 235
Cdd:PRK11904 702 LGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARII-N 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 236 SAVAGHK----KLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVTPGIHDRfVQELAQRVMA-LNV 310
Cdd:PRK11904 781 RTLAARDgpivPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADR-VIEMLKGAMAeLKV 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 311 GHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRAQRGYYLQPCLA-LDvslDARIAREEVFGPLACVLR 389
Cdd:PRK11904 860 GDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFeID---SISQLEREVFGPILHVIR 936
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1837855989 390 --AQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHV-PFGGRGAS 452
Cdd:PRK11904 937 ykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVqPFGGQGLS 1002
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
54-469 |
4.88e-56 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 193.97 E-value: 4.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVfrlgGEMFPsiragvevE 133
Cdd:TIGR01238 88 PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQV----RDVLG--------E 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLT 213
Cdd:TIGR01238 156 FSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 GHPAVAGVSFTGSSATGRKIA---ASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVT 290
Cdd:TIGR01238 236 SDPRIAGVAFTGSTEVAQLINqtlAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 291 PGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRV--IGGAALQRAQRGYYLQPCLALD 368
Cdd:TIGR01238 316 EDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqLTLDDSRACQHGTFVAPTLFEL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDAriAREEVFGPLACVLR--AQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHV-P 445
Cdd:TIGR01238 396 DDIAE--LSEEVFGPVLHVVRykARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVqP 473
|
410 420
....*....|....*....|....*
gi 1837855989 446 FGGRGASSYGSSEQG-HYAREFFTS 469
Cdd:TIGR01238 474 FGGQGLSGTGPKAGGpHYLYRLTQV 498
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
53-452 |
7.00e-55 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 197.85 E-value: 7.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEmfpsiragvev 132
Cdd:COG4230 606 FPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAA----------- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:COG4230 675 PTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAAL 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIAAsAVAGHK----KLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTAsSRLI 288
Cdd:COG4230 755 VADPRIAGVAFTGSTETARLINR-TLAARDgpivPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSA-LRVL 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 289 vtpgihdrFVQE-LAQRV-------MA-LNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRAQRGY 359
Cdd:COG4230 833 --------CVQEdIADRVlemlkgaMAeLRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGT 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 360 YLQPCLaldVSLDaRIAR--EEVFGPLACVLR--AQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN- 434
Cdd:COG4230 905 FVAPTL---IEID-SISDleREVFGPVLHVVRykADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNr 980
|
410 420
....*....|....*....|.
gi 1837855989 435 -M--PTSGVDfhvPFGGRGAS 452
Cdd:COG4230 981 nIigAVVGVQ---PFGGEGLS 998
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
61-475 |
1.30e-53 |
|
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: 185.81 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 61 LAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEA--------RGEVQRAADIFD-YYAGEVFRLGGEMFPSiRAGVE 131
Cdd:cd07087 19 LEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHALKHLKkWMKPRRVSVPLLLQPA-KAYVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 veisREPLGVVALITPWNFPIA---IPAwktAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVfnLVLGTGADV 208
Cdd:cd07087 98 ----PEPLGVVLIIGPWNYPLQlalAPL---IGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAV--AVVEGGVEV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTGHPaVAGVSFTGSSATGRKIAASAVaghKKLQ---MEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASS 285
Cdd:cd07087 169 ATALLAEP-FDHIFFTGSPAVGKIVMEAAA---KHLTpvtLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 286 RLIVTPGIHDRFVQELAQRVMALnVGHALDERSQIGPVSNGAQFDKDLSYIalarDEAQRVIGGaalQRAQRGYYLQPCL 365
Cdd:cd07087 245 YVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLL----DDGKVVIGG---QVDKEERYIAPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 366 ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptsGVDFHV- 444
Cdd:cd07087 317 LDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN----DVLLHAa 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1837855989 445 ----PFGGRGASSYGSSeQGHYAREFFTSLKTSYI 475
Cdd:cd07087 393 ipnlPFGGVGNSGMGAY-HGKAGFDTFSHLKSVLK 426
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
53-455 |
1.77e-53 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 193.93 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLggemfpsiragvEV 132
Cdd:PRK11905 603 FPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRL------------LN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:PRK11905 671 GPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATGRKIA---ASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIV 289
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVARLIQrtlAKRSGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCL 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 290 TPGIHDRFVQELAQRVMALNVGHALDERSQIGPV-SNGAQfDKDLSYIALARDEAQRVIGGAALQRAQRGYYLQPCLald 368
Cdd:PRK11905 831 QEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPViDAEAQ-ANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTL--- 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 369 VSLDA-RIAREEVFGPLACVLR--AQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFHV- 444
Cdd:PRK11905 907 IEIDSiSDLEREVFGPVLHVVRfkADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVq 986
|
410
....*....|.
gi 1837855989 445 PFGGRGASSYG 455
Cdd:PRK11905 987 PFGGEGLSGTG 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
54-455 |
5.78e-51 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 186.72 E-value: 5.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAGEVfrlggemfpsiRAGVEVE 133
Cdd:PRK11809 696 PIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQV-----------RDDFDND 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISRePLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLT 213
Cdd:PRK11809 765 THR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALV 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 GHPAVAGVSFTGSSATGRKIAASaVAGHKKLQ-------MEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSR 286
Cdd:PRK11809 844 ADARVRGVMFTGSTEVARLLQRN-LAGRLDPQgrpipliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRV 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 287 LIVTPGIHDRFVQELAQRVMALNVGHAldER--SQIGPVSNGAQFDKDLSYIALARDEAQRV--IGGAALQRAQRGYYLQ 362
Cdd:PRK11809 923 LCLQDDVADRTLKMLRGAMAECRMGNP--DRlsTDIGPVIDAEAKANIERHIQAMRAKGRPVfqAARENSEDWQSGTFVP 1000
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 363 PCLaldVSLDaRIAR--EEVFGPLACVLR--AQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTS 438
Cdd:PRK11809 1001 PTL---IELD-SFDElkREVFGPVLHVVRynRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMV 1076
|
410
....*....|....*...
gi 1837855989 439 GVDFHV-PFGGRGASSYG 455
Cdd:PRK11809 1077 GAVVGVqPFGGEGLSGTG 1094
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
134-472 |
2.23e-48 |
|
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: 172.02 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGTGADVGQVLT 213
Cdd:cd07135 104 IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 214 ---GHpavagVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRLIVT 290
Cdd:cd07135 183 qkfDK-----IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 291 PGIHDRFVQELaQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYiaLARDEAQRVIGGAAlQRAQRgyYLQPCLALDVS 370
Cdd:cd07135 258 PSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSL--LDTTKGKVVIGGEM-DEATR--FIPPTIVSDVS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 371 LDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptsGVDFHV-----P 445
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIN----DTLIHVgvdnaP 407
|
330 340
....*....|....*....|....*..
gi 1837855989 446 FGGRGASSYGsSEQGHYAREFFTSLKT 472
Cdd:cd07135 408 FGGVGDSGYG-AYHGKYGFDTFTHERT 433
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
53-452 |
1.09e-46 |
|
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: 169.30 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKdigrgivansqQLAHILASE------------QGKTLPEArgEVQRAADIFD------YYAGE 114
Cdd:cd07123 82 RKEWARMPFEDRAAIFL-----------KAADLLSGKyryelnaatmlgQGKNVWQA--EIDAACELIDflrfnvKYAEE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 115 VFrlgGEMFPSIRAGVEVEISREPL-GVVALITPWNFpIAIPA-WKTAPALAcGNAVVLKPSEftpaTAV----MLAEII 188
Cdd:cd07123 149 LY---AQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNF-TAIGGnLAGAPALM-GNVVLWKPSD----TAVlsnyLVYKIL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 189 RAAGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKI---AASAVAGHK---KLQMEMGGKNPLVVLDDADL 262
Cdd:cd07123 220 EEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLwkqIGENLDRYRtypRIVGETGGKNFHLVHPSADV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 263 EIALACALDGAFHATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALAR-- 340
Cdd:cd07123 300 DSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsd 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 341 DEAQRVIGGAALQRaqRGYYLQPCLALDVSLDARIAREEVFGPLACVL--RAQDYEHALAIANDT-EYGLSAGI---CTQ 414
Cdd:cd07123 380 PEAEIIAGGKCDDS--VGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTTsPYALTGAIfaqDRK 457
|
410 420 430
....*....|....*....|....*....|....*...
gi 1837855989 415 SLKHATHFRRHVQSGLAMVNMPTSGVDFHVPFGGRGAS 452
Cdd:cd07123 458 AIREATDALRNAAGNFYINDKPTGAVVGQQPFGGARAS 495
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
132-462 |
1.23e-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: 167.28 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEISREPLGVVALITPWNFPIAI---PAwktAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVfNLVLGtGADV 208
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLalgPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTG-GADV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTG----HpavagVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTAS 284
Cdd:cd07133 170 AAAFSSlpfdH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 285 SRLIVTPGIHDRFVQELAQRV--MALNVGHALDERSQIgpvsNGAQFDKDLSYIALARDEAQRVI----GGAALQRAQRg 358
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVakMYPTLADNPDYTSII----NERHYARLQGLLEDARAKGARVIelnpAGEDFAATRK- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 359 yyLQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmpts 438
Cdd:cd07133 320 --LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN---- 393
|
330 340
....*....|....*....|....*....
gi 1837855989 439 GVDFHV-----PFGGRGASSYgsseqGHY 462
Cdd:cd07133 394 DTLLHVaqddlPFGGVGASGM-----GAY 417
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
61-471 |
1.08e-45 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 165.97 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 61 LAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEA--------RGEVQRA-ADIFDYYAGEVFRLGGEMFPSiragvE 131
Cdd:PTZ00381 28 LEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEHLlKHLDEYLKPEKVDTVGVFGPG-----K 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEISREPLGVVALITPWNFPI---AIPAwktAPALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGtGADV 208
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLnltLIPL---AGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTGHPaVAGVSFTGSSATGrKIAASAVAghKKL---QMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASS 285
Cdd:PTZ00381 178 TTELLKEP-FDHIFFTGSPRVG-KLVMQAAA--ENLtpcTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 286 RLIVTPGIHDRFVQELAQrVMALNVGHALDERSQIGPVSNGAQFDKDLSYIalARDEAQRVIGGAAlQRAQRgyYLQPCL 365
Cdd:PTZ00381 254 YVLVHRSIKDKFIEALKE-AIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI--KDHGGKVVYGGEV-DIENK--YVAPTI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 366 ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptsGVDFHV- 444
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN----DCVFHLl 403
|
410 420 430
....*....|....*....|....*....|.
gi 1837855989 445 ----PFGGRGASSYGSSeQGHYAREFFTSLK 471
Cdd:PTZ00381 404 npnlPFGGVGNSGMGAY-HGKYGFDTFSHPK 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
128-466 |
1.57e-44 |
|
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: 161.63 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 128 AGVEVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFnLVLGtGAD 207
Cdd:cd07134 90 FGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 208 VGQVLTGHPaVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIAlACALD-GAFHATGQRCTASSR 286
Cdd:cd07134 168 VAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKA-AKKIAwGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 287 LIVTPGIHDRFVQELaQRVMALNVG--HALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAALQRAQRgyYLQPC 364
Cdd:cd07134 246 VFVHESVKDAFVEHL-KAEIEKFYGkdAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR--YIAPT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 365 LALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNmptsGVDFHV 444
Cdd:cd07134 323 VLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN----DVVLHF 398
|
330 340
....*....|....*....|....*...
gi 1837855989 445 -----PFGGRGASSYGSSeQGHYA-REF 466
Cdd:cd07134 399 lnpnlPFGGVNNSGIGSY-HGVYGfKAF 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
134-456 |
7.35e-40 |
|
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: 149.19 E-value: 7.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 134 ISREPLGVVALITPWNFPI--AIpawktAP---ALACGNAVVLKPSEFTPATAVMLAEIIRAAgVPDGVFNLVLGtGADV 208
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFqlAL-----APligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTGHPaVAGVSFTGSSATGRKIAASAvAGH-KKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSRL 287
Cdd:cd07136 169 NQELLDQK-FDYIFFTGSVRVGKIVMEAA-AKHlTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 288 IVTPGIHDRFVQELAQRVMALNVGHALdERSQIGPVSNGAQFDKDLSYIalarDEAQRVIGGAAlQRAQRgyYLQPCLAL 367
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFYGEDPL-ESPDYGRIINEKHFDRLAGLL----DNGKIVFGGNT-DRETL--YIEPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 368 DVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN-----MPTSgvdf 442
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimhLANP---- 394
|
330
....*....|....
gi 1837855989 443 HVPFGGRGASSYGS 456
Cdd:cd07136 395 YLPFGGVGNSGMGS 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
123-471 |
4.70e-38 |
|
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: 143.71 E-value: 4.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 123 FPSiragvEVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVfnLVL 202
Cdd:cd07137 91 FPA-----KAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI--KVI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 203 GTGADVGQVLTGHpAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHA-TGQRC 281
Cdd:cd07137 164 EGGVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQAC 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 282 TASSRLIVTPGIHDRFVQELaQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGaalQRAQRGYYL 361
Cdd:cd07137 243 IAPDYVLVEESFAPTLIDAL-KNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG---ERDEKNLYI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 362 QPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN--MPTSG 439
Cdd:cd07137 319 EPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtVVQYA 398
|
330 340 350
....*....|....*....|....*....|..
gi 1837855989 440 VDfHVPFGGRGASSYGSSeQGHYAREFFTSLK 471
Cdd:cd07137 399 ID-TLPFGGVGESGFGAY-HGKFSFDAFSHKK 428
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
54-411 |
1.54e-35 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 137.29 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGktLPEAR--GEVQRAADIFDYYAGEVfRLGGEMFPSI-RAGV 130
Cdd:cd07129 13 ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARlqGELGRTTGQLRLFADLV-REGSWLDARIdPADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 E------VEISRE--PLGVVALITPWNFPIA--IPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAA----GVPDG 196
Cdd:cd07129 90 DrqplprPDLRRMlvPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 197 VFNLVLGTGADVGQVLTGHPAVAGVSFTGSSATGRKIAASAVA--------GhkklqmEMGGKNPLVVLDDAdlEIALAC 268
Cdd:cd07129 170 VFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpepipfyA------ELGSVNPVFILPGA--LAERGE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 269 ALDGAFHA-----TGQRCTASSRLIVTPGIH-DRFVQELAQRVMALNVGHALDERSQigpvsngAQFDKDLSYIAlARDE 342
Cdd:cd07129 242 AIAQGFVGsltlgAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTMLTPGIA-------EAYRQGVEALA-AAPG 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1837855989 343 AQRVIGGAAlqrAQRGYYLQPCLALdVSLDARIA----REEVFGPLACVLRAQDYEHALAIANDTEYGLSAGI 411
Cdd:cd07129 314 VRVLAGGAA---AEGGNQAAPTLFK-VDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATI 382
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
131-476 |
1.16e-34 |
|
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: 134.66 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 EVEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDgVFNLVLGTGADVGQ 210
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKE-CYPVVLGGVEETTE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 211 VLT---GHpavagVSFTGSSATGRKIAASAvAGH-KKLQMEMGGKNPLVVLDDADLEIALACALDGAFHATGQRCTASSR 286
Cdd:cd07132 172 LLKqrfDY-----IFYTGSTSVGKIVMQAA-AKHlTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 287 LIVTPGIHDRFVQELaQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIalardEAQRV-IGGaalQRAQRGYYLQPCL 365
Cdd:cd07132 246 VLCTPEVQEKFVEAL-KKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVaIGG---QTDEKERYIAPTV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 366 ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN--MPTSGVDfH 443
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtIMHYTLD-S 395
|
330 340 350
....*....|....*....|....*....|...
gi 1837855989 444 VPFGGRGASSYGSSeQGHYAREFFTSLKTSYIR 476
Cdd:cd07132 396 LPFGGVGNSGMGAY-HGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
54-400 |
5.66e-32 |
|
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: 126.97 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 54 PGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEArGEVQRAADIFDYYA--GEVFRLGGEMFPSIRAGVE 131
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAfvIYSYRIPHEPGNHLGQGLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEISRE--PLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAG-VPDGVFNLVLGTGaDV 208
Cdd:cd07084 92 QQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDG-KT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTGHPAVAGVSFTGSSATGRKIAASAVAGhkKLQMEMGGKNPLVVLDDADLEIALACALDGAFHA-TGQRCTASSRL 287
Cdd:cd07084 171 MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTAcSGQKCTAQSML 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 288 IVTPGIHDRFVQELAQRVMAlnvgHALDERSQIGPVsngaQFDKDLSYIALARDEAQRVI--GGAALQRAQRGYYLQPCL 365
Cdd:cd07084 249 FVPENWSKTPLVEKLKALLA----RRKLEDLLLGPV----QTFTTLAMIAHMENLLGSVLlfSGKELKNHSIPSIYGACV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1837855989 366 --ALDVSLDARIAR-----EEVFGPLACVLRAQDYEHALAIA 400
Cdd:cd07084 321 asALFVPIDEILKTyelvtEEIFGPFAIVVEYKKDQLALVLE 362
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
133-476 |
7.31e-32 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 127.47 E-value: 7.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVfNLVLGTGADVGQVL 212
Cdd:PLN02174 107 EIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAV-RVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 tgHPAVAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVVLDDADLEIALACALDGAFHA-TGQRCTASSRLIVTP 291
Cdd:PLN02174 186 --EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALnVGHALDERSQIGPVSNGAQFDKdLSYIALARDEAQRVIGGAalQRAQRGYYLQPCLALDVSL 371
Cdd:PLN02174 264 EYAPKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGG--EKDRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVNMPTSGVDFH-VPFGGRG 450
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGVG 419
|
330 340
....*....|....*....|....*.
gi 1837855989 451 ASSYGSSeQGHYAREFFTSLKTSYIR 476
Cdd:PLN02174 420 ESGMGAY-HGKFSFDAFSHKKAVLYR 444
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
137-471 |
8.87e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 124.45 E-value: 8.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 137 EPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEII------RAAGVPDGvfnlvlgtGADVGQ 210
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIpkyldsKAVKVIEG--------GPAVGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 211 VLTGHPAvAGVSFTGSSATGRKIAASAVAGHKKLQMEMGGKNPLVV--LDDA-DLEIALACALDGAFHA-TGQRCTASSR 286
Cdd:PLN02203 179 QLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 287 LIVtpgiHDRFVQ---ELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGGAAlqrAQRGYYLQP 363
Cdd:PLN02203 258 VLV----EERFAPiliELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSI---DEKKLFIEP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 364 CLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHFRRHVQSGLAMVN--MPTSGVD 441
Cdd:PLN02203 331 TILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaIIQYACD 410
|
330 340 350
....*....|....*....|....*....|
gi 1837855989 442 fHVPFGGRGASSYGSSeQGHYAREFFTSLK 471
Cdd:PLN02203 411 -SLPFGGVGESGFGRY-HGKYSFDTFSHEK 438
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
58-400 |
1.35e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 103.63 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 58 ATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADIFDYYAgevfRLGGEMFPS--IRAGVEVEIS 135
Cdd:PRK11903 59 ALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYA----KLGAALGDArlLRDGEAVQLG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 136 REPL-----------GVVALITPWNFPiaipAW----KTAPALACGNAVVLKPSEFTP-ATAVMLAEIIRAAGVPDGVFN 199
Cdd:PRK11903 135 KDPAfqgqhvlvptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAwLTQRMVKDVVAAGILPAGALS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 200 LVLGTGADVGQVLTGHPAVagvSFTGSSATGRKIAASA--VAGHKKLQMEMGGKNPLVVLDDADleiALACALDGAFH-- 275
Cdd:PRK11903 211 VVCGSSAGLLDHLQPFDVV---SFTGSAETAAVLRSHPavVQRSVRVNVEADSLNSALLGPDAA---PGSEAFDLFVKev 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 276 ------ATGQRCTASSRLIVTPGIHDRFVQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGG 349
Cdd:PRK11903 285 vremtvKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDG 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1837855989 350 AALQ----RAQRGYYLQPCL--ALDVSLDARIAREEVFGPLACVLRAQDYEHALAIA 400
Cdd:PRK11903 365 GGFAlvdaDPAVAACVGPTLlgASDPDAATAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
6-422 |
1.67e-21 |
|
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: 97.34 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 6 SLIDGQWAGGAGDSENI-NPSDlSAPVCLVAQASAQQAAQAVEAARRAQPGWAATGLAARAQILKDIGRGIVANSQQLaH 84
Cdd:cd07128 3 SYVAGQWHAGTGDGRTLhDAVT-GEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDL-Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 85 ILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGgEMFPSIRAGVEVEISRE----------PLGVVAL-ITPWNFPIA 153
Cdd:cd07128 81 ALSAATGATRRDSWIDIDGGIGTLFAYASLGRREL-PNAHFLVEGDVEPLSKDgtfvgqhiltPRRGVAVhINAFNFPVW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 154 IPAWKTAPALACGNAVVLKPSeftPATA----VMLAEIIRAAGVPDGVFNLVLGTGADVGQVLTGHPAVAgvsFTGSSAT 229
Cdd:cd07128 160 GMLEKFAPALLAGVPVIVKPA---TATAylteAVVKDIVESGLLPEGALQLICGSVGDLLDHLGEQDVVA---FTGSAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 230 GRKIAASA--VAGHKKLQMEMGGKNPLVVLDDA-------DL---EIALACALDgafhaTGQRCTASSRLIVTPGIHDRF 297
Cdd:cd07128 234 AAKLRAHPniVARSIRFNAEADSLNAAILGPDAtpgtpefDLfvkEVAREMTVK-----AGQKCTAIRRAFVPEARVDAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 298 VQELAQRVMALNVGHALDERSQIGPVSNGAQFDKDLSYIALARDEAQRVIGG-----AALQRAQRGYYLQPCLAL-DVSL 371
Cdd:cd07128 309 IEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGpdrfeVVGADAEKGAFFPPTLLLcDDPD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1837855989 372 DARIARE-EVFGPLACVLRAQDYEHALAIANDTEYGLSAGICTQSLKHATHF 422
Cdd:cd07128 389 AATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
82-428 |
7.19e-14 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 73.68 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 82 LAHILASEQGKTLPEARGEVQRAADIFDYYAGEVFRLGGEMF--PSIRAGVEVEISREPLGVVALITPWNFPIAIPAWKT 159
Cdd:cd07126 84 FARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFnvPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 160 APALACGNAVVLKPSEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVLT-GHPAVagVSFTGSSatgrKIAasav 238
Cdd:cd07126 164 MGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPRM--TLFTGSS----KVA---- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 239 aghKKLQMEMGGKnplVVLDDADLE-------------IALACALDgAFHATGQRCTASSRLIVtpgiHDRFVQE-LAQR 304
Cdd:cd07126 234 ---ERLALELHGK---VKLEDAGFDwkilgpdvsdvdyVAWQCDQD-AYACSGQKCSAQSILFA----HENWVQAgILDK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 305 VMALNVGHALDERSqIGPV---SNGAQFDKDLSYIALArdEAQRVIGGAALQR----AQRGYYLQ-----PCLALDVSLD 372
Cdd:cd07126 303 LKALAEQRKLEDLT-IGPVltwTTERILDHVDKLLAIP--GAKVLFGGKPLTNhsipSIYGAYEPtavfvPLEEIAIEEN 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1837855989 373 ARIAREEVFGPLACVLRAQDYE--HALAIANDTEYGLSAGICTQSLkhatHFRRHVQS 428
Cdd:cd07126 380 FELVTTEVFGPFQVVTEYKDEQlpLVLEALERMHAHLTAAVVSNDI----RFLQEVLA 433
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
53-454 |
4.69e-11 |
|
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: 64.57 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGKTLPEARGEVQRAADifdYYAGEVFRLGGEMFPSIRAGVEV 132
Cdd:cd07121 17 QKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAA---EKTPGTEDLTTTAWSGDNGLTLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 133 EISrePLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKP---SEFTPATAV-MLAEIIRAAGVPDGVFNLVLGTGADV 208
Cdd:cd07121 94 EYA--PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVeLINKAIAEAGGPDNLVVTVEEPTIET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 209 GQVLTGHPAVAGVSFTGssatGRKIAASAVAGHKKLqMEMGGKNPLVVLD-DADLEIALACALDGAFHATGQRCTASSRL 287
Cdd:cd07121 172 TNELMAHPDINLLVVTG----GPAVVKAALSSGKKA-IGAGAGNPPVVVDeTADIEKAARDIVQGASFDNNLPCIAEKEV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 288 IVTPGIHDRFVQELaQRVMALNVGH--ALDERSQIGPVSNGAQFDKDL-----SYIALArdeaqrvIGGAALQRAqrgyy 360
Cdd:cd07121 247 IAVDSVADYLIAAM-QRNGAYVLNDeqAEQLLEVVLLTNKGATPNKKWvgkdaSKILKA-------AGIEVPADI----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 361 lqPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGL--SAGICTQSLKHATHFRRHVQSGLAMVNMPT- 437
Cdd:cd07121 314 --RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQTTIFVKNGPSy 391
|
410
....*....|....*..
gi 1837855989 438 SGVDfhvpFGGRGASSY 454
Cdd:cd07121 392 AGLG----VGGEGYTTF 404
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
132-452 |
3.46e-10 |
|
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: 61.74 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 VEISrEPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKPSEFTPATAVMLAEIIR----AAGVPDGVFNLVLGTGAD 207
Cdd:cd07122 90 VEIA-EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMReaavAAGAPEGLIQWIEEPSIE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 208 VGQVLTGHPAVAGVSFTGSSATgrkIAASAVAGHKKLqmemG---GKNPLVVLDDADLEIALACALDG-AF-HATGqrCT 282
Cdd:cd07122 169 LTQELMKHPDVDLILATGGPGM---VKAAYSSGKPAI----GvgpGNVPAYIDETADIKRAVKDIILSkTFdNGTI--CA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 283 ASSRLIVTPGIHDRFVQELAQRvmalnvghaldersqigpvsnGAQF--DKDLSYI--ALARDEAQR---VIGGAALQRA 355
Cdd:cd07122 240 SEQSVIVDDEIYDEVRAELKRR---------------------GAYFlnEEEKEKLekALFDDGGTLnpdIVGKSAQKIA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 356 QRgyylqpcLALDVSLDAR--IAREEVFGP--------LACVL---RAQDYEHALAIAND-TEY---GLSAGICTQSLKH 418
Cdd:cd07122 299 EL-------AGIEVPEDTKvlVAEETGVGPeeplsrekLSPVLafyRAEDFEEALEKARElLEYggaGHTAVIHSNDEEV 371
|
330 340 350
....*....|....*....|....*....|....
gi 1837855989 419 ATHFRRHVQSGLAMVNMPTSgvdfhvpFGGRGAS 452
Cdd:cd07122 372 IEEFALRMPVSRILVNTPSS-------LGGIGDT 398
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
137-438 |
5.53e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 61.13 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 137 EPLGVVALITPWNFPIAIPAWKTAPALACGNAVVLKP----SEFTPATAVMLAEIIRAAGVPDGVFNLVLGTGADVGQVL 212
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 213 TGHPAVAGVSFTGSSATgrkiaASAVAGHKKLQMEMGGKNPLVVLDD-ADLEIALACALDGAFHATGQRCTASSRLIVTP 291
Cdd:cd07081 174 MKFPGIGLLLATGGPAV-----VKAAYSSGKPAIGVGAGNTPVVIDEtADIKRAVQSIVKSKTFDNGVICASEQSVIVVD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 292 GIHDRFVQELAQRVMALNVGHALDersQIGPVSngaqfdkdLSYIALARDeaqrVIGgaalqraQRGYYLQPCLALDVSL 371
Cdd:cd07081 249 SVYDEVMRLFEGQGAYKLTAEELQ---QVQPVI--------LKNGDVNRD----IVG-------QDAYKIAAAAGLKVPQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 372 DARI-------------AREEVFGPLACVLRAQDYEHALAIA----NDTEYGLSAGICTQSLK---HATHFRRHVQSGLA 431
Cdd:cd07081 307 ETRIligevtslaehepFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRF 386
|
....*..
gi 1837855989 432 MVNMPTS 438
Cdd:cd07081 387 VKNGPCS 393
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
53-454 |
1.52e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 59.92 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 53 QPGWAATGLAARAQILKDIGRGIVANSQQLAHILASEQGktlpeargeVQRAADIFdyyagEVFRLGGEMFPsiraGVE- 131
Cdd:PRK15398 49 QQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG---------MGRVEDKI-----AKNVAAAEKTP----GVEd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 132 ------------VEISREPLGVVALITPWNFPIAIPAWKTAPALACGNAVVlkpseFTP---ATAV------MLAEIIRA 190
Cdd:PRK15398 111 lttealtgdnglTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVV-----FSPhpgAKKVslraieLLNEAIVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 191 AGVPDGVFNLVLGTGADVGQVLTGHPAVAGVSFTGssatGRKIAASAVAGHKKLqMEMGGKNPLVVLDD-ADLEIALACA 269
Cdd:PRK15398 186 AGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMKSGKKA-IGAGAGNPPVVVDEtADIEKAARDI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 270 LDGAFHATGQRCTASSRLIVTPGIHDRFVQELaQRVMALNVGHALDERSQIGPVSNGAQFDKDLsyiaLARDeAQRVIGG 349
Cdd:PRK15398 261 VKGASFDNNLPCIAEKEVIVVDSVADELMRLM-EKNGAVLLTAEQAEKLQKVVLKNGGTVNKKW----VGKD-AAKILEA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 350 AALQRAQRgyylQPCLALDVSLDARIAREEVFGPLACVLRAQDYEHALAIANDTEYGL--SAGICTQSLKHATHFRRHVQ 427
Cdd:PRK15398 335 AGINVPKD----TRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
410 420
....*....|....*....|....*...
gi 1837855989 428 SGLAMVNMPT-SGVDfhvpFGGRGASSY 454
Cdd:PRK15398 411 TSIFVKNGPSyAGLG----LGGEGFTTF 434
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
155-444 |
4.78e-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: 58.64 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 155 PAWKTAPA----LACGNAVVLKPSeftPATAVMLA-------EIIRAAGV-PDGVFNLVLGTGADVGQVLTGHPAVAGVS 222
Cdd:cd07127 206 PTWNGYPGlfasLATGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIID 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 223 FTGSSATGRKIAASavAGHKKLQMEMGGKNPLVVLDDADLE-----IALACALdgafhATGQRCTASSRLIV-TPGI--- 293
Cdd:cd07127 283 FTGSNAFGDWLEAN--ARQAQVYTEKAGVNTVVVDSTDDLKamlrnLAFSLSL-----YSGQMCTTPQNIYVpRDGIqtd 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 294 -----HDRFVQELAQRVMALnvgHALDERSQ--IGPVSNGAqfdkdlsyiALARDEAQRVIGGAALQRAQRGYYLQP--- 363
Cdd:cd07127 356 dgrksFDEVAADLAAAIDGL---LADPARAAalLGAIQSPD---------TLARIAEARQLGEVLLASEAVAHPEFPdar 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 364 -----CLALDVSLDARIArEEVFGPLACVLRAQDYEHALAIANDT--EYG-LSAGICTQS---LKHATHFRRHVQSGLAM 432
Cdd:cd07127 424 vrtplLLKLDASDEAAYA-EERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDpevVERVQEAALDAGVALSI 502
|
330
....*....|....*....
gi 1837855989 433 -------VNMPTSGVDFHV 444
Cdd:cd07127 503 nltggvfVNQSAAFSDFHG 521
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
131-310 |
7.88e-09 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 57.62 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 131 EVEISREPLGVVALITPWNFPIAIPAwKTAPALACGNAVVLKPSEFTPATA---VMLAEIIRAAGVPDGVFNLVLGTGAD 207
Cdd:cd07077 93 ETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNralALLFQAADAAHGPKILVLYVPHPSDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837855989 208 VGQVLTGHPAVAGVSFTGSSATGRkiAASAVAGHKKLqMEMGGKNPLVVLDD-ADLEIALACALDGAFHaTGQRCTASSR 286
Cdd:cd07077 172 LAEELLSHPKIDLIVATGGRDAVD--AAVKHSPHIPV-IGFGAGNSPVVVDEtADEERASGSVHDSKFF-DQNACASEQN 247
|
170 180
....*....|....*....|....*.
gi 1837855989 287 LIVTPGIHDRFVQELAQ--RVMALNV 310
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLklVVEGLKV 273
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