|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
59-513 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 795.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSA 218
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 219 LALGELANQAGIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFD 298
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSP---AEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 299 SANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERHIN 378
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERV-KKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 379 DAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQ 458
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 459 IWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVCF 513
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
59-509 |
0e+00 |
|
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: 769.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSA 218
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 219 LALGELANQAGIPAGVYNVVPCSRqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFD 298
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSR--AKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 299 SANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHIN 378
Cdd:TIGR01780 239 DADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKK-LKVGNGLDEGVTQGPLINEKAVEKVEKHIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 379 DAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQ 458
Cdd:TIGR01780 318 DAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1728938489 459 IWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:TIGR01780 398 IWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
37-516 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 731.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 37 ASLVRWGGLVGGRWVET--PAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVE 114
Cdd:PLN02278 20 AGLLRTQGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 115 NKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITR 194
Cdd:PLN02278 100 NKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 195 KVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVpcsRQQTSAVGEVLCTDPLVAKISFTGSTATGKILL 274
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVV---MGDAPEIGDALLASPKVRKITFTGSTAVGKKLM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 275 KHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSG 354
Cdd:PLN02278 257 AGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAV-QKLVVGDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 355 FDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEA 434
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 435 EAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVCFG 514
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
..
gi 1728938489 515 GL 516
Cdd:PLN02278 496 NM 497
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
45-513 |
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: 610.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARI 122
Cdd:COG1012 9 FIGGEWVAaaSGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 123 ITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAA 202
Cdd:COG1012 89 LTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 203 GCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVK 282
Cdd:COG1012 169 GNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGD---GSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 283 RVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQG 362
Cdd:COG1012 246 RVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA-LKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 363 PLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGK-NFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIAN 441
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 442 AADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIIS-SAECPFGGVKQSGLGREGSKYGIDEYLEIKYVCF 513
Cdd:COG1012 405 DTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
37-514 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 609.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 37 ASLVRWGGLVGGRWVETPA--VFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVE 114
Cdd:PRK11241 6 STLFRQQALINGEWLDANNgeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 115 NKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITR 194
Cdd:PRK11241 86 HQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 195 KVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILL 274
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGS---AGAVGGELTSNPLVRKLSFTGSTEIGRQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 275 KHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSG 354
Cdd:PRK11241 243 EQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK-LHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 355 FDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEA 434
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 435 EAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVCFG 514
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
50-511 |
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: 549.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 50 WVE-TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENG 128
Cdd:pfam00171 1 WVDsESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 129 KPLKEAQGEILYSASFLEWFAEEARRVYGDIIPaSAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVV 208
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETLP-SDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 209 KPAEDTPLSALALGELANQAGIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMEL 288
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSG---AEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 289 GGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEK 368
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK-LKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 369 AVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLA 448
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728938489 449 GYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAE-CPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-513 |
4.25e-180 |
|
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: 512.52 E-value: 4.25e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 89 AGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRR 168
Cdd:cd07078 10 AFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 169 MLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRqqtSAV 248
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG---DEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 249 GEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFL 328
Cdd:cd07078 167 GAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 329 VQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGK-NFFEPTLLT 407
Cdd:cd07078 247 VHESIYDEFVERLVERVKA-LKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKgYFVPPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 408 NVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIIS-SAECPFG 486
Cdd:cd07078 326 DVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEPSAPFG 405
|
410 420
....*....|....*....|....*..
gi 1728938489 487 GVKQSGLGREGSKYGIDEYLEIKYVCF 513
Cdd:cd07078 406 GVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
46-511 |
2.30e-158 |
|
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: 458.65 E-value: 2.30e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:cd07088 2 INGEFVPssSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAG 203
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 204 CTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKR 283
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVT---GRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 284 VSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGP 363
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKM-KAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 364 LINEKAVEKVERHINDAVSQGASIVTGGKRHSLGK-NFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANA 442
Cdd:cd07088 318 LVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKgYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728938489 443 ADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
61-511 |
8.96e-152 |
|
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: 441.60 E-value: 8.96e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSA 218
Cdd:cd07114 83 RYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 219 LALGELANQAGIPAGVYNVVPCSRQQTsavGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFD 298
Cdd:cd07114 163 LELAKLAEEAGFPPGVVNVVTGFGPET---GEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 299 SANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAkAIERELRVGSGFDENTTQGPLINEKAVEKVERHIN 378
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLV-ARARAIRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 379 DAVSQGASIVTGGKRHSLGKN----FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQ 454
Cdd:cd07114 319 RAREEGARVLTGGERPSGADLgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1728938489 455 DPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
59-512 |
8.57e-147 |
|
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: 428.52 E-value: 8.57e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQ-GE 137
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 138 ILYSASFLEWFAEEARRVYGDIIPaSAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLS 217
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYP-QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 218 ALALGELANQAGIPAGVYNVVpcsrQQT-SAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIV 296
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVV----HGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 297 FDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERH 376
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERA-KALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 377 INDAVSQGASIVTGGKRHSL----GKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFY 452
Cdd:cd07093 315 VELARAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 453 SQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVC 512
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
45-511 |
1.03e-139 |
|
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: 411.22 E-value: 1.03e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVetPAV----FPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDE 118
Cdd:cd07091 7 FINNEFV--DSVsgktFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 119 LARIITAENGKPLKE-AQGEILYSASFLEWFAEEARRVYGDIIPaSAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVG 197
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIP-IDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 198 AALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHA 277
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGF---GPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 278 AGT-VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFaKAIERELRVGSGFD 356
Cdd:cd07091 241 AKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKF-KARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 357 ENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEA 436
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 437 VAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
46-509 |
7.15e-138 |
|
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: 406.12 E-value: 7.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:cd07138 3 IDGAWVApaGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQ--------GEILYSASFLEWFAEEARRvygdiipasakdRRMLVLKQPVGVSAIITPWNFPSAMITRK 195
Cdd:cd07138 83 TLEMGAPITLARaaqvglgiGHLRAAADALKDFEFEERR------------GNSLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 196 VGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLK 275
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGD---GPVVGEALSAHPDVDMVSFTGSTRAGKRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 276 HAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnFAKAIERELRVGSGF 355
Cdd:cd07138 228 AAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEE-IAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 356 DENTTQGPLINEKAVEKVERHINDAVSQGASIVTGG--KRHSLGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDT 432
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEGLERGYFvKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728938489 433 EAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNeGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
57-513 |
5.98e-137 |
|
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: 403.51 E-value: 5.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 57 FPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQG 136
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 137 EILYSASFLEWFAEEARRVYGDIIP----ASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAE 212
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPfdasPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 213 DTPLSALALGELANQAGIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKIlLKHAAGtVKRVSMELGGHA 292
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSG---ETVGDALVTDPRVRMISFTGSPAVGEA-IARKAG-LKKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 293 PFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEK 372
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK-LVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 373 VERHINDAVSQGASIVTGGKRHSlgkNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFY 452
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDG---AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728938489 453 SQDPAQIWRVAEQLEVGMVGVNEgiISSAEC---PFGGVKQSGLGREGSKYGIDEYLEIKYVCF 513
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
57-511 |
4.19e-136 |
|
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: 401.32 E-value: 4.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 57 FPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQG 136
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 137 EILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPL 216
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 217 SALALGELANQAGIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIV 296
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGG---AEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 297 FDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERH 376
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASK-LKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 377 INDAVSQGASIVTGGKRHSlgkNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDP 456
Cdd:cd07150 317 VEDAVAKGAKLLTGGKYDG---NFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1728938489 457 AQIWRVAEQLEVGMVGVNEGIISS-AECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
59-509 |
1.87e-135 |
|
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: 399.70 E-value: 1.87e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWG-RLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQG- 136
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 137 EILYSASFLEWFAEEARRVYGDIIPASAKDRRM----LVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAE 212
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 213 DTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHA 292
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGS---DNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 293 PFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnFAKAIERELRVGSGFDENTTQGPLINEKAVEK 372
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVE-ALAAAFEALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 373 VERHINDAVSQGASIVTGGKR-HSLGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGY 450
Cdd:cd07089 317 VEGYIARGRDEGARLVTGGGRpAGLDKGFYvEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728938489 451 FYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
46-511 |
2.45e-134 |
|
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: 397.84 E-value: 2.45e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELAR 121
Cdd:cd07119 2 IDGEWVEaaSGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 122 IITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPAsAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALA 201
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 202 AGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTV 281
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGS---GATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 282 KRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQ 361
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKK-IKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 362 GPLINEKAVEKVERHINDAVSQGASIVTGGKRHS---LGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAV 437
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdeLAKGYFvEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728938489 438 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-511 |
1.37e-133 |
|
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: 395.18 E-value: 1.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 57 FPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQG 136
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 137 EILYSASFLEWFAEEARRVYGDIIPASAKD---RRM-LVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAE 212
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEyneRRIaFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 213 DTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHA 292
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGY---GSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 293 PFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEK 372
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKV-KKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 373 VERHINDAVSQGASIVTGGKRhsLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFY 452
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 453 SQDPAQIWRVAEQLEVGMVGVNEgiiSSA----ECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07145 395 TNDINRALKVARELEAGGVVIND---STRfrwdNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-511 |
6.78e-133 |
|
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: 392.28 E-value: 6.78e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 87 HDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKD 166
Cdd:cd07104 10 AAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 167 RRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLS-ALALGELANQAGIPAGVYNVVPCSRqqt 245
Cdd:cd07104 90 KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGG--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 246 SAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTN 325
Cdd:cd07104 167 SEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 326 RFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSlgkNFFEPTL 405
Cdd:cd07104 247 RILVHESVYDEFVEKLVAKAKA-LPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG---LFYQPTV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 406 LTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEG-IISSAECP 484
Cdd:cd07104 323 LSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQtVNDEPHVP 402
|
410 420
....*....|....*....|....*..
gi 1728938489 485 FGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07104 403 FGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
89-513 |
5.33e-132 |
|
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: 387.74 E-value: 5.33e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 89 AGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRR 168
Cdd:cd06534 6 AFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 169 MLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRqqtSAV 248
Cdd:cd06534 86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG---DEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 249 GEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFL 328
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 329 VQKGIHDKFVENFAkaierelrvgsgfdenttqgplinekavekverhindavsqgasivtggkrhslgknffepTLLTN 408
Cdd:cd06534 243 VHESIYDEFVEKLV-------------------------------------------------------------TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 409 VTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEG-IISSAECPFGG 487
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSsIGVGPEAPFGG 341
|
410 420
....*....|....*....|....*.
gi 1728938489 488 VKQSGLGREGSKYGIDEYLEIKYVCF 513
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
59-509 |
1.49e-131 |
|
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: 389.58 E-value: 1.49e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVygDIIPASAkDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSA 218
Cdd:cd07106 81 GGAVAWLRYTASLDLPD--EVIEDDD-TRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 219 LALGELANQAgIPAGVYNVVPCSRQqtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFD 298
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDE----LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 299 SANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAkAIERELRVGSGFDENTTQGPLINEKAVEKVERHIN 378
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALV-ALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 379 DAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQ 458
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1728938489 459 IWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
62-511 |
6.33e-131 |
|
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: 388.23 E-value: 6.33e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 62 PASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEIL 139
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 140 YSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSAL 219
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 220 ALGELANQAGIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDS 299
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYG---ATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 300 ANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENfAKAIERELRVGSGFDENTTQGPLINEKAVEKVERHIND 379
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAA-VVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 380 AVSQGASIVTGGKRHSLGKN-FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQ 458
Cdd:cd07118 320 GRAEGATLLLGGERLASAAGlFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 459 IWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
87-511 |
4.01e-130 |
|
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: 385.27 E-value: 4.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 87 HDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGD-IIPASAK 165
Cdd:cd07100 9 HAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADePIETDAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 166 drRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQQT 245
Cdd:cd07100 89 --KAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 246 SAVGEvlctDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTN 325
Cdd:cd07100 167 EAIIA----DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 326 RFLVQKGIHDKFVENFAKAIErELRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTL 405
Cdd:cd07100 243 RFIVHEDVYDEFLEKFVEAMA-ALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 406 LTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPF 485
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPF 401
|
410 420
....*....|....*....|....*.
gi 1728938489 486 GGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07100 402 GGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
46-511 |
1.02e-128 |
|
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: 383.08 E-value: 1.02e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELAR 121
Cdd:cd07139 3 IGGRWVApsGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 122 IITAENGKPLKEAQ-GEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAAL 200
Cdd:cd07139 83 LWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 201 AAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRqqtsAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT 280
Cdd:cd07139 163 AAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR----EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 281 VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGFDENTT 360
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVA-ALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 361 QGPLINEKAVEKVERHINDAVSQGASIVTGGKR--HSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVA 438
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 439 IANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNeGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
61-512 |
1.71e-128 |
|
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: 381.79 E-value: 1.71e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQG-EIL 139
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 140 YSASFLEWFAEEARRVYGDIIPASAkDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSAL 219
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 220 ALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDS 299
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVT---GFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 300 ANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERHIND 379
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLA-RSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 380 AVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQI 459
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 460 WRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVC 512
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
55-509 |
1.14e-127 |
|
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: 380.02 E-value: 1.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 55 AVFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLK 132
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 133 EAQ-GEILYSASFLEWFAEEARRVYGDIIPaSAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPA 211
Cdd:cd07112 82 DALaVDVPSAANTFRWYAEAIDKVYGEVAP-TGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 212 EDTPLSALALGELANQAGIPAGVYNVVPCSRQQtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT-VKRVSMELGG 290
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHT---AGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 291 HAPFIVF-DSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKA 369
Cdd:cd07112 238 KSPNIVFaDAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAA-REWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 370 VEKVERHINDAVSQGASIVTGGKRHSL--GKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGL 447
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 448 AGYFYSQDPAQIWRVAEQLEVGMVGVN---EGIISSaecPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNcfdEGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
45-511 |
1.80e-124 |
|
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: 372.45 E-value: 1.80e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVE--TPAVFPVQDPASGEEL-GRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELAR 121
Cdd:cd07131 2 YIGGEWVDsaSGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 122 IITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALA 201
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 202 AGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVpcsRQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTV 281
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVV---HGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 282 KRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAkAIERELRVGSGFDENTTQ 361
Cdd:cd07131 239 KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFV-ERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 362 GPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGK----NFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAV 437
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGyekgYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728938489 438 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGII-SSAECPFGGVKQSGLG-REGSKYGIDEYLEIKYV 511
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
59-513 |
1.13e-121 |
|
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: 364.45 E-value: 1.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIP----ASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDT 214
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPldatQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 215 PLSALALGELANQAGIPAGVYNVVPCSRQQtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAGtvKRVSMELGGHAPF 294
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREV---LGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 295 IVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVE 374
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKK-LKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 375 RHINDAVSQGASIVTGGKRHslgKNFFEPTLLTNV-TTKMLCTqEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYS 453
Cdd:cd07094 317 RWVEEAVEAGARLLCGGERD---GALFKPTVLEDVpRDTKLST-EETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1728938489 454 QDPAQIWRVAEQLEVGMVGVNEG-IISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVCF 513
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
45-511 |
1.80e-121 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 364.62 E-value: 1.80e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETP-AVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:PRK13473 6 LINGELVAGEgEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEA-QGEILYSASFLEWFAEEARRVYGdiiPASAK---DRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAA 199
Cdd:PRK13473 86 SLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEG---KAAGEyleGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 200 LAAGCTVVVKPAEDTPLSALALGELANQAgIPAGVYNVVpCSRQQTsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAG 279
Cdd:PRK13473 163 LAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVV-TGRGAT--VGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 280 TVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENT 359
Cdd:PRK13473 239 SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT-LKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 360 TQGPLINEKAVEKVERHINDAVSQG-ASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVA 438
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 439 IANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:PRK13473 398 WANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
61-511 |
3.47e-121 |
|
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: 363.08 E-value: 3.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILY 140
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 141 SASFLEWFAEEARRVYGD-IIPASA--KDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLS 217
Cdd:cd07099 82 ALEAIDWAARNAPRVLAPrKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 218 ALALGELANQAGIPAGVYNVVpcsrQQTSAVGEVLCtDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVF 297
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVV----TGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 298 DSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAkAIERELRVGSGFDENTTQGPLINEKAVEKVERHI 377
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLV-AKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 378 NDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPA 457
Cdd:cd07099 316 DDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1728938489 458 QIWRVAEQLEVGMVGVNEGIISSA--ECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07099 396 RAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
59-511 |
3.83e-121 |
|
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: 363.09 E-value: 3.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDA-GAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGE 137
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 138 ILYSASFLEWFAEEARRVYGDIIPaSAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLS 217
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 218 ALALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVF 297
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVT---GLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 298 DSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGfDENTTQGPLINEKAVEKVERHI 377
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERF-RALRVGPG-LEDPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 378 NDAVSQGASIVTGGKR---HSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQ 454
Cdd:cd07109 315 ARARARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728938489 455 DPAQIWRVAEQLEVGMVGVNE-----GIissaECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNygaggGI----ELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
44-511 |
6.61e-120 |
|
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: 360.41 E-value: 6.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 44 GLVGGRWVETPAVFPVQDPAS-GEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARI 122
Cdd:cd07097 3 NYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 123 ITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAA 202
Cdd:cd07097 83 LTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 203 GCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVK 282
Cdd:cd07097 163 GNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGS---GSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 283 RVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQG 362
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERT-KALKVGDALDEGVDIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 363 PLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKN--FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIA 440
Cdd:cd07097 319 PVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728938489 441 NAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNegiISSAE----CPFGGVKQSGLG-REGSKYGIDEYLEIKYV 511
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN---LPTAGvdyhVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
59-512 |
9.85e-120 |
|
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: 359.70 E-value: 9.85e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIPASAKD----RRmlvlkQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDT 214
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSfaytRR-----EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 215 PLSALALGELANQAGIPAGVYNVVpcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPF 294
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVV----QGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 295 IVFDSANVDCAVAGALASKYRNSGQtcVCTN--RFLVQKGIHDKFVEnfaKAIER--ELRVGSGFDENTTQGPLINEKAV 370
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQ--VCSNgtRVFVQRSIKDEFTE---RLVERtkKIRIGDPLDEDTQMGALISEEHL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 371 EKVERHINDAVSQGASIVTGGKRHSL-----GKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADV 445
Cdd:cd07090 307 EKVLGYIESAKQEGAKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTY 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728938489 446 GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVC 512
Cdd:cd07090 387 GLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
57-511 |
2.74e-119 |
|
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: 359.41 E-value: 2.74e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 57 FPVQDPASGEELGRVADCGVAEAREAVRAAHDA-GAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKE-A 134
Cdd:cd07144 25 IKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 135 QGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDT 214
Cdd:cd07144 105 LGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAY-TLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 215 PLSALALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPF 294
Cdd:cd07144 184 PLSLLYFANLVKEAGFPPGVVNIIP---GYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 295 IVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIERELRVGSGFDENTTQGPLINEKAVEKVE 374
Cdd:cd07144 261 LVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDTVVGPQVSKTQYDRVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 375 RHINDAVSQGASIVTGGKRHS--LGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYF 451
Cdd:cd07144 341 SYIEKGKKEGAKLVYGGEKAPegLGKGYFiPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAV 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 452 YSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07144 421 FTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
59-511 |
6.40e-119 |
|
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: 357.41 E-value: 6.40e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKE-AQGE 137
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 138 ILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLS 217
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 218 ALALGELAnQAGIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVF 297
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGG---ASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 298 DSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHI 377
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSA-IRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 378 nDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPA 457
Cdd:cd07092 316 -ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1728938489 458 QIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
59-511 |
9.87e-118 |
|
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: 354.35 E-value: 9.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRV---YGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTP 215
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 216 LSALALGELANQAGIPAGVYNVVpcsRQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFI 295
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVV---TGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 296 VFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVER 375
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEA-IRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 376 HINDAVSQGASIVTGGKR-HSLGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYS 453
Cdd:cd07110 317 FIARGKEEGARLLCGGRRpAHLEKGYFiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728938489 454 QDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-509 |
6.34e-117 |
|
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: 352.32 E-value: 6.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 57 FPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQG 136
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 137 EILYSASFLEWFAEEARRVYGDIIP----ASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAE 212
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 213 DTPLSALALGELANQAGIPAGVYNVVPCSRQQTSAvgevLCTDPLVAKISFTGSTATGkILLKHAAGTvKRVSMELGGHA 292
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADL----LVTDERIKLLSFTGSPAVG-WDLKARAGK-KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 293 PFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEK 372
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARV-KALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 373 VERHINDAVSQGASIVTGGKRHSlgkNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGL-AGYF 451
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKRDG---ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLqAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1728938489 452 ySQDPAQIWRVAEQLEVGMVGVNEgiISSAEC---PFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:cd07147 391 -TRDLEKALRAWDELEVGGVVIND--VPTFRVdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
45-511 |
6.82e-114 |
|
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: 345.25 E-value: 6.82e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPA--VFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELA 120
Cdd:cd07142 7 FINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 121 RIITAENGKPLKEA-QGEILYSASFLEWFAEEARRVYGDIIPASAkDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAA 199
Cdd:cd07142 87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADG-PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 200 LAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAG 279
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVT---GFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 280 T-VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnfaKAIERELR--VGSGFD 356
Cdd:cd07142 243 SnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVE---KAKARALKrvVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 357 ENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEA 436
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 437 VAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
61-512 |
3.24e-113 |
|
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: 342.79 E-value: 3.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVrLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAfdETDWAHDPRLRARV-LLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIPASAkDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSA 218
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEP-GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 219 LALGE-LANQAGIPAGVYNVVpcsRQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVF 297
Cdd:cd07120 161 AAIIRiLAEIPSLPAGVVNLF---TESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 298 DSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERHI 377
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARL-AAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 378 NDAVSQGASIVTGGKRHSLGKN---FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQ 454
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728938489 455 DPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVC 512
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
46-511 |
6.55e-113 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 343.02 E-value: 6.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:PRK13252 11 IDGAYVEatSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQ-GEILYSASFLEWFAEEARRVYGDIIPASAKD----RRmlvlkQPVGVSAIITPWNFPSAMITRKVGA 198
Cdd:PRK13252 91 TLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvytRR-----EPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 199 ALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVpcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAA 278
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVV----QGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 279 GTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQtcVCTN--RFLVQKGIHDKFVENFAKAIEReLRVGSGFD 356
Cdd:PRK13252 242 ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ--VCTNgtRVFVQKSIKAAFEARLLERVER-IRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 357 ENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKR---HSLGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDT 432
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERlteGGFANGAFvAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728938489 433 EAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
44-509 |
3.42e-112 |
|
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: 341.08 E-value: 3.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 44 GLVGGRWVE-TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARI 122
Cdd:cd07086 1 GVIGGEWVGsGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 123 ITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAA 202
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 203 GCTVVVKPAEDTPLSALALGELANQA----GIPAGVYNVVPCSRQqtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAA 278
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD----GGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 279 GTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDEN 358
Cdd:cd07086 237 RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQ-VRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 359 TTQGPLINEKAVEKVERHINDAVSQGASIVTGGKR--HSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEA 436
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728938489 437 VAIANAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVNEGiISSAEC--PFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIP-TSGAEIggAFGGEKETGGGRESGSDAWKQYMRRS 471
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-511 |
1.47e-111 |
|
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: 337.63 E-value: 1.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 87 HDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKD 166
Cdd:cd07105 10 AAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 167 RRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQQTS 246
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEDAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 247 AVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNR 326
Cdd:cd07105 170 EVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 327 FLVQKGIHDKFVENFAKAIERElrvgsgFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGK-RHSLGKNFFEPTL 405
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKL------FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPSGTSMPPTI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 406 LTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIIS-SAECP 484
Cdd:cd07105 324 LDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHdEPTLP 403
|
410 420
....*....|....*....|....*..
gi 1728938489 485 FGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07105 404 HGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
105-511 |
3.80e-110 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 333.24 E-value: 3.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 105 LRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITP 184
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 185 WNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFT 264
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGR---GETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 265 GSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKA 344
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 345 IErELRVGSGFDENTTQ-GPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGP 423
Cdd:PRK10090 238 MQ-AVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 424 LAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGID 503
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 1728938489 504 EYLEIKYV 511
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
21-507 |
4.12e-110 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 337.24 E-value: 4.12e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 21 PPGPAAARWRSSWALPASLVRwggLVGGRWVETPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKE 100
Cdd:PRK09407 1 ATTTALPMPAPSALTFERLRR---LTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 101 RSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGD-----IIPASAKDRrmlVLKQP 175
Cdd:PRK09407 78 RAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPrrragALPVLTKTT---ELRQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 176 VGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGevlctD 255
Cdd:PRK09407 155 KGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGP---GPVVG-----T 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 256 PLVAK---ISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKG 332
Cdd:PRK09407 227 ALVDNadyLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 333 IHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGK-RHSLGKNFFEPTLLTNVTT 411
Cdd:PRK09407 307 IYDEFVRAFVAAVRA-MRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 412 KMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIIS---SAECPFGGV 488
Cdd:PRK09407 386 DMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGM 465
|
490
....*....|....*....
gi 1728938489 489 KQSGLGREGSKYGIDEYLE 507
Cdd:PRK09407 466 KDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
43-511 |
1.13e-108 |
|
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: 332.19 E-value: 1.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 43 GGLVGGRWVET--PAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDA-GAAWGR-LPAKERSVRLRRWYELMVENKDE 118
Cdd:cd07143 8 GLFINGEFVDSvhGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLkVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 119 LARIITAENGKP-LKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKdRRMLVLKQPVGVSAIITPWNFPSAMITRKVG 197
Cdd:cd07143 88 LASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIK-KLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 198 AALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQQTsavGEVLCTDPLVAKISFTGSTATGKILLKHA 277
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTC---GNAISSHMDIDKVAFTGSTLVGRKVMEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 278 AGT-VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFaKAIERELRVGSGFD 356
Cdd:cd07143 244 AKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRF-KEKAKKLKVGDPFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 357 ENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEA 436
Cdd:cd07143 323 EDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEA 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 437 VAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07143 403 IKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
59-512 |
1.52e-108 |
|
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: 331.71 E-value: 1.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAkERSVRLRRWYELMVENKDELARIITAENGKPLKEAQG 136
Cdd:cd07113 19 ITNPATEQVIASVASATEADVDAAVASAWRAfvSAWAKTTPA-ERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 137 -EILYSASFLEWFAEEARRVYGDI----IPASAKDR-RMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKP 210
Cdd:cd07113 98 fEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 211 AEDTPLSALALGELANQAGIPAGVYNVVpcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGG 290
Cdd:cd07113 178 SEFTPLTLLRVAELAKEAGIPDGVLNVV----NGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 291 HAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGFDENTTQGPLINEKAV 370
Cdd:cd07113 254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALS-SFQVGSPMDESVMFGPLANQPHF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 371 EKVERHINDAVSQGASIVTGGKRHSlGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAG 449
Cdd:cd07113 333 DKVCSYLDDARAEGDEIVRGGEALA-GEGYFvQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTA 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 450 YFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVC 512
Cdd:cd07113 412 SVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
46-511 |
1.78e-108 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 332.47 E-value: 1.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVETP--AVFPVQDPASGEELGRV-----ADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDE 118
Cdd:PLN02467 12 IGGEWREPVlgKRIPVVNPATEETIGDIpaataEDVDAAVEAARKAFKRNKGKDWARTTGAVRAKYLRAIAAKITERKSE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 119 LARIITAENGKPLKEAQGEILYSASFLEWFAEEAR----RVYGDI-IPASAKDRRmlVLKQPVGVSAIITPWNFPSAMIT 193
Cdd:PLN02467 92 LAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldaKQKAPVsLPMETFKGY--VLKEPLGVVGLITPWNYPLLMAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 194 RKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQQTsavGEVLCTDPLVAKISFTGSTATGKIL 273
Cdd:PLN02467 170 WKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEA---GAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 274 LKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGS 353
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAK-NIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 354 GFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKR-HSLGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFD 431
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 432 TEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
56-511 |
3.07e-108 |
|
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: 330.85 E-value: 3.07e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 56 VFPVQDPASGEELGRVADCGVAEAREAVRAAHDA---GAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKP-L 131
Cdd:cd07141 23 TFPTINPATGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPfS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 132 KEAQGEILYSASFLEWFAEEARRVYGDIIPASAkDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPA 211
Cdd:cd07141 103 KSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 212 EDTPLSALALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT-VKRVSMELGG 290
Cdd:cd07141 182 EQTPLTALYLASLIKEAGFPPGVVNVVP---GYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSnLKRVTLELGG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 291 HAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnfaKAIER--ELRVGSGFDENTTQGPLINEK 368
Cdd:cd07141 259 KSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVK---RSVERakKRVVGNPFDPKTEQGPQIDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 369 AVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLA 448
Cdd:cd07141 336 QFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 449 GYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07141 416 AAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
61-511 |
5.23e-108 |
|
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: 329.27 E-value: 5.23e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILY 140
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 141 SASFLEWFAEEARRVYGD-----IIPASAKDRrmlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTP 215
Cdd:cd07101 82 VAIVARYYARRAERLLKPrrrrgAIPVLTRTT---VNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 216 LSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEvlctdPLVAK---ISFTGSTATGKILLKHAAGTVKRVSMELGGHA 292
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGP---GSEVGG-----AIVDNadyVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 293 PFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEK 372
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVART-RALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 373 VERHINDAVSQGASIVTGGK-RHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYF 451
Cdd:cd07101 310 VTAHVDDAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 452 YSQDPAQIWRVAEQLEVGMVGVNEGIIS---SAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
59-511 |
9.90e-108 |
|
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: 328.94 E-value: 9.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLK-EAQGE 137
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 138 ILYSASFLEWFAEEARRVYGDIIPAsAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLS 217
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 218 ALALGELANQAgIPAGVYNVVPCSRQQtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVF 297
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEE---CGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 298 DSANVDCAVAGALAS-KYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERH 376
Cdd:cd07108 236 PDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKL-SKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 377 INDAVS-QGASIVTGGKRHSLGKN----FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYF 451
Cdd:cd07108 315 IDLGLStSGATVLRGGPLPGEGPLadgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1728938489 452 YSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYG-IDEYLEIKYV 511
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
59-509 |
3.87e-106 |
|
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: 324.31 E-value: 3.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADcgvAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07146 3 VRNPYTGEVVGTVPA---GTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIP----ASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDT 214
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFScdltANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 215 PLSALALGELANQAGIPAGVYNVVPCSRQQtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAGtvKRVSMELGGHAPF 294
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVVTGEPGE---IGDELITHPDVDLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 295 IVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAiERELRVGSGFDENTTQGPLINEKAVEKVE 374
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEK-SAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 375 RHINDAVSQGASIVTGGKRHSLgknFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQ 454
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQRQGA---LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1728938489 455 DPAQIWRVAEQLEVGMVGVNEGI-ISSAECPFGGVKQSGLG-REGSKYGIDEYLEIK 509
Cdd:cd07146 391 DLDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
48-511 |
2.90e-105 |
|
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: 322.72 E-value: 2.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 48 GRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITA 125
Cdd:cd07151 1 GEWRDgtSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 126 ENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCT 205
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 206 VVVKPAEDTPLSA-LALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRV 284
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGA---GSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 285 SMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGFDENTTQGPL 364
Cdd:cd07151 238 ALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVK-ALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 365 INEKAVEKVERHINDAVSQGASIVTGGKRHSlgkNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAAD 444
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEAEG---NVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728938489 445 VGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIIS-SAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
45-502 |
2.84e-104 |
|
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: 320.29 E-value: 2.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPAVF-PVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGR-LPAKERSVRLRRWYELMVENKDELARI 122
Cdd:cd07082 5 LINGEWKESSGKTiEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 123 ITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIP----ASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGA 198
Cdd:cd07082 85 LMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPgdwfPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 199 ALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVpcsrqqT---SAVGEVLCTDPLVAKISFTGSTATGKILLK 275
Cdd:cd07082 165 ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVV------TgrgREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 276 haAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGF 355
Cdd:cd07082 239 --QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVA-KLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 356 DENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRhsLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAE 435
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1728938489 436 AVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE----GIISsaeCPFGGVKQSGLGREGSKYGI 502
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrGPDH---FPFLGRKDSGIGTQGIGDAL 461
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
42-509 |
1.56e-103 |
|
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: 318.90 E-value: 1.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 42 WGGLVGGRWVeTPA---VFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDE 118
Cdd:cd07559 1 YDNFINGEWV-APSkgeYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 119 LARIITAENGKPLKEAQG-EILYSASFLEWFAEEARRVYGDIipaSAKDRRML--VLKQPVGVSAIITPWNFPSAMITRK 195
Cdd:cd07559 80 LAVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSL---SEIDEDTLsyHFHEPLGVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 196 VGAALAAGCTVVVKPAEDTPLSALALGELANQAgIPAGVYNVVpcsRQQTSAVGEVLCTDPLVAKISFTGSTATGKILLK 275
Cdd:cd07559 157 LAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVV---TGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 276 HAAGTVKRVSMELGGHAPFIVFDSA-----NVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnfaKAIER--E 348
Cdd:cd07559 233 YAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIE---RAVERfeA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 349 LRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKN----FFEPTLLTNVTTKMLCTQEETFGPL 424
Cdd:cd07559 310 IKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLdkgyFYEPTLIKGGNNDMRIFQEEIFGPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 425 APVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDE 504
Cdd:cd07559 390 LAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDH 469
|
....*
gi 1728938489 505 YLEIK 509
Cdd:cd07559 470 YQQTK 474
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
46-511 |
3.69e-102 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 315.99 E-value: 3.69e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVETPA--VFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELAR 121
Cdd:PLN02766 25 INGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 122 IITAENGKPLKEAQG-EILYSASFLEWFAEEARRVYGDIIPASAKdRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAAL 200
Cdd:PLN02766 105 LDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 201 AAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT 280
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVT---GFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 281 -VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENT 359
Cdd:PLN02766 261 nLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKA-KDWVVGDPFDPRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 360 TQGPLINEKAVEKVERHINDAVSQGASIVTGGKrhSLGKN--FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAV 437
Cdd:PLN02766 340 RQGPQVDKQQFEKILSYIEHGKREGATLLTGGK--PCGDKgyYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728938489 438 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
22-507 |
5.45e-102 |
|
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: 314.72 E-value: 5.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 22 PGPAAARWRSSWaLPASLVRWGGLVGGRWV--ETPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAK 99
Cdd:cd07111 3 PAPESAACALAW-LDAHDRSFGHFINGKWVkpENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 100 ERSVRLRRWYELMVENKDELARIITAENGKPLKEAQ-GEILYSASFLEWFAeearrvygdiIPASAKDRRMLVLKqPVGV 178
Cdd:cd07111 82 VRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHA----------GWAQLLDTELAGWK-PVGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 179 SAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVpcsrQQTSAVGEVLCTDPLV 258
Cdd:cd07111 151 VGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIV----TGNGSFGSALANHPGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 259 AKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFV 338
Cdd:cd07111 227 DKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 339 ENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQE 418
Cdd:cd07111 307 RKLKERMSH-LRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 419 ETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGS 498
Cdd:cd07111 386 EIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGG 465
|
....*....
gi 1728938489 499 KYGIDEYLE 507
Cdd:cd07111 466 KEGLYEYLR 474
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
59-511 |
6.96e-102 |
|
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: 313.54 E-value: 6.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 59 VQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEI 138
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 139 LYSASFLEWFAEEARRVYGDIIPASAKDRRMlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSA 218
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHY-TLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 219 LALGELANQAgIPAGVYNVVPCSRQQtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFD 298
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGAT---AGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 299 SANVDCAVAGALAS-KYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHI 377
Cdd:cd07107 236 DADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAA-IKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 378 NDAVSQGASIVTGGKR---HSLGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYS 453
Cdd:cd07107 315 DSAKREGARLVTGGGRpegPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728938489 454 QDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
45-511 |
7.31e-100 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 311.36 E-value: 7.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPA--VFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELA 120
Cdd:PLN02466 61 LINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 121 RIITAENGKPLKE-AQGEILYSASFLEWFAEEARRVYGDIIPASAkDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAA 199
Cdd:PLN02466 141 ALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTVPADG-PHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 200 LAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVpcSRQQTSAvGEVLCTDPLVAKISFTGSTATGKILLKHAAG 279
Cdd:PLN02466 220 LACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVV--SGFGPTA-GAALASHMDVDKLAFTGSTDTGKIVLELAAK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 280 T-VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnfaKAIERELR--VGSGFD 356
Cdd:PLN02466 297 SnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVE---KAKARALKrvVGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 357 ENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEA 436
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEV 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 437 VAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:PLN02466 454 IRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
65-511 |
3.60e-99 |
|
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: 306.14 E-value: 3.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 65 GEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASF 144
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 145 LEWFAEEARRVYGDIIPaSAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSA-LALGE 223
Cdd:cd07152 81 LHEAAGLPTQPQGEILP-SAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 224 LANQAGIPAGVYNVVPCSrqqtSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVD 303
Cdd:cd07152 160 LFEEAGLPAGVLHVLPGG----ADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 304 CAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFA-KAieRELRVGSGFDENTTQGPLINEKAVEKVERHINDAVS 382
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAaKA--KHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 383 QGASIVTGGKRHSLgknFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRV 462
Cdd:cd07152 314 AGARLEAGGTYDGL---FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1728938489 463 AEQLEVGMVGVNEGIIsSAEC--PFGGVKQSGLG-REGSKYGIDEYLEIKYV 511
Cdd:cd07152 391 ADRLRTGMLHINDQTV-NDEPhnPFGGMGASGNGsRFGGPANWEEFTQWQWV 441
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
42-509 |
5.69e-98 |
|
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: 304.38 E-value: 5.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 42 WGGLVGGRWV--ETPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDEL 119
Cdd:cd07117 1 YGLFINGEWVkgSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 120 ARIITAENGKPLKEAQG-EILYSASFLEWFAEEARRVYGDIIPASaKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGA 198
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMID-EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 199 ALAAGCTVVVKPAEDTPLSALALGELANQAgIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAA 278
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVT---GKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 279 GTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDEN 358
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFEN-VKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 359 TTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGK----NFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEA 434
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 435 EAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
46-513 |
1.21e-97 |
|
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: 303.65 E-value: 1.21e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVETPA--VFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRLPAKERSVRLRRWYELMVENKDELAR 121
Cdd:cd07140 10 INGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 122 IITAENGK----PLKEAQGeilYSASFLEWFAEEARRVYGDIIPAS-AKDRRMLVL--KQPVGVSAIITPWNFPSAMITR 194
Cdd:cd07140 90 IESLDSGAvytlALKTHVG---MSIQTFRYFAGWCDKIQGKTIPINqARPNRNLTLtkREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 195 KVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILL 274
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGS---GSLVGQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 275 KHAA-GTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGS 353
Cdd:cd07140 244 KSCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEV-KKMKIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 354 GFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTE 433
Cdd:cd07140 323 PLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 434 AEAVAIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07140 403 DVDGVLQRANDTeyGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
..
gi 1728938489 512 CF 513
Cdd:cd07140 483 TI 484
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
45-511 |
1.36e-95 |
|
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: 298.22 E-value: 1.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPA-VFPVQDPASGEELGRVADCGVAEAREAVRAAHDA--GAAWGRlpAKERSVR-LRRWYELMVENKDELA 120
Cdd:TIGR04284 4 LIDGKLVAGSAgTFPTVNPATEEVLGVAADATAADMDAAIAAARRAfdETDWSR--DTALRVRcLRQLRDALRAHVEELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 121 RIITAENGKPLKEAQGEILYS-ASFLEWFAEEA-----RRVYGDIIPASAKDRRmLVLKQPVGVSAIITPWNFPSAMITR 194
Cdd:TIGR04284 82 ELTIAEVGAPRMLTAGAQLEGpVDDLGFAADLAesyawTTDLGVASPMGIPTRR-TLRREAVGVVGAITPWNFPHQINLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 195 KVGAALAAGCTVVVKPAEDTPLSALALGEL-ANQAGIPAGVYNVVPCSRQqtsAVGEVLCTDPLVAKISFTGSTATGKIL 273
Cdd:TIGR04284 161 KLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDH---RLGALLAKDPRVDMVSFTGSTATGRAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 274 LKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnFAKAIERELRVGS 353
Cdd:TIGR04284 238 MADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVA-AAAATMGSIKPGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 354 GFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHS-LGKNFF-EPTLLTNVTTKMLCTQEETFGPLAPVIKFD 431
Cdd:TIGR04284 317 PADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRPAdRDRGFFvEPTVIAGLDNNARVAREEIFGPVLTVIAHD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 432 TEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:TIGR04284 397 GDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
45-506 |
6.02e-95 |
|
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: 297.60 E-value: 6.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPAVFPVQDPASGEE-LGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADPSEvLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKqPVGVSAIITPWNFPSAMITRKVGAALAAG 203
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 204 CTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT--- 280
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGP---GEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 281 ---VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGFDE 357
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTK-ALKVGDPEDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 358 NTTQGPLINEKAVEKVERHINDAVSQGaSIVTGGKRHSLGKN--FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAE 435
Cdd:cd07124 351 EVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728938489 436 AVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISS--AECPFGGVKQSGLgreGSKYGIDEYL 506
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGAlvGRQPFGGFKMSGT---GSKAGGPDYL 499
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
45-503 |
4.00e-91 |
|
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: 286.72 E-value: 4.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVE--TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARI 122
Cdd:cd07085 4 FINGEWVEskTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 123 ITAENGKPLKEAQGEILYSASFLEwFAEEARRVY-GDIIPASAKDRRMLVLKQPVGVSAIITPWNFPsAMITR-KVGAAL 200
Cdd:cd07085 84 ITLEHGKTLADARGDVLRGLEVVE-FACSIPHLLkGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwMFPMAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 201 AAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRqqtsAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT 280
Cdd:cd07085 162 ACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK----EAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 281 VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTT 360
Cdd:cd07085 238 GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERA-KKLKVGAGDDPGAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 361 QGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGK----NFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEA 436
Cdd:cd07085 317 MGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGyengNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728938489 437 VAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGI-ISSAECPFGGVKQSGLGrEGSKYGID 503
Cdd:cd07085 397 IAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSFFG-DLHFYGKD 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
61-514 |
8.98e-91 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 285.09 E-value: 8.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILY 140
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 141 SASFLEWFAEEARRVYGDIiPASAKD---RRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLS 217
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADE-PADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 218 ALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLcTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVF 297
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQTLLVG---SGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 298 DSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERHI 377
Cdd:PRK09406 242 PSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARM-AALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 378 NDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPA 457
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1728938489 458 QIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYVCFG 514
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
88-503 |
1.09e-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: 282.21 E-value: 1.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 88 DAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDII-PASAKD 166
Cdd:cd07102 29 AAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRvPEKDGF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 167 RRMLVlKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqtS 246
Cdd:cd07102 109 ERYIR-REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLS----H 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 247 AVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNR 326
Cdd:cd07102 184 ETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIER 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 327 FLVQKGIHDKFVENFAkAIERELRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSL---GKNFFEP 403
Cdd:cd07102 264 IYVHESIYDAFVEAFV-AVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPEdkaGGAYLAP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 404 TLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAEC 483
Cdd:cd07102 343 TVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPAL 422
|
410 420
....*....|....*....|
gi 1728938489 484 PFGGVKQSGLGREGSKYGID 503
Cdd:cd07102 423 AWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
61-513 |
3.09e-88 |
|
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: 278.80 E-value: 3.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQ-GEIL 139
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 140 YSASFLEWFAEEARRVygdIIPASAKDRRMLVLK------QPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAED 213
Cdd:cd07098 82 VTCEKIRWTLKHGEKA---LRPESRPGGLLMFYKrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 214 TPLSALALGELANQA----GIPAGVYNVVPCsrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELG 289
Cdd:cd07098 159 VAWSSGFFLSIIREClaacGHDPDLVQLVTC----LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 290 GHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKA 369
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQA-LRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 370 VEKVERHINDAVSQGASIVTGGKRHSLGK----NFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADV 445
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRYPHPEypqgHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 446 GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAEC--PFGGVKQSGLGREGSKYGIDEYLEIKYVCF 513
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
55-509 |
2.03e-83 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 267.15 E-value: 2.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 55 AVFPVQDPASGEELGRVA---DCGVAEAREAVRAAHDAGAaWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPL 131
Cdd:PRK09847 35 ETFETVDPVTQAPLAKIArgkSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 132 KEA-QGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVlKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKP 210
Cdd:PRK09847 114 RHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 211 AEDTPLSALALGELANQAGIPAGVYNVVPCSRQQTsavGEVLCTDPLVAKISFTGSTATGKILLKHAAGT-VKRVSMELG 289
Cdd:PRK09847 193 SEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEA---GQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEAG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 290 GHAPFIVF-DSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVeNFAKAIERELRVGSGFDENTTQGPLINEK 368
Cdd:PRK09847 270 GKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFL-ALLKQQAQNWQPGHPLDPATTMGTLIDCA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 369 AVEKVERHINDAVSQGASIVTGgkRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLA 448
Cdd:PRK09847 349 HADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLG 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1728938489 449 GYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:PRK09847 427 AAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
45-506 |
1.19e-77 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 252.55 E-value: 1.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPAVFPVQDPASGEEL-GRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:PRK03137 40 IIGGERITTEDKIVSINPANKSEVvGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILYSASFLEWFAEEARRvYGDIIP-ASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAA 202
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPvESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 203 GCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT-- 280
Cdd:PRK03137 199 GNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGS---GSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVqp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 281 ----VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVEnfaKAIER--ELRVGSG 354
Cdd:PRK03137 276 gqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLE---KVVELtkELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 355 fDENTTQGPLINEKAVEKVERHINDAvSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEA 434
Cdd:PRK03137 353 -EDNAYMGPVINQASFDKIMSYIEIG-KEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 435 EAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGI---ISSAEcPFGGVKQSGlgrEGSKYGIDEYL 506
Cdd:PRK03137 431 HALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCtgaIVGYH-PFGGFNMSG---TDSKAGGPDYL 501
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
94-504 |
2.11e-77 |
|
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: 250.41 E-value: 2.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 94 GRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIP----ASAKDRRM 169
Cdd:cd07148 39 NWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 170 LVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQqtsaVG 249
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA----VA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 250 EVLCTDPLVAKISFTGSTATGKIL-LKHAAGTvkRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFL 328
Cdd:cd07148 195 EKLVTDPRVAFFSFIGSARVGWMLrSKLAPGT--RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 329 VQKGIHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRhsLGKNFFEPTLLTN 408
Cdd:cd07148 273 VPAEIADDFAQRLAAAAEK-LVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 409 VTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAE-CPFGG 487
Cdd:cd07148 350 PPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAG 429
|
410
....*....|....*..
gi 1728938489 488 VKQSGLGREGSKYGIDE 504
Cdd:cd07148 430 RRQSGYGTGGIPYTMHD 446
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
61-511 |
2.34e-77 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 250.55 E-value: 2.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 61 DPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILY 140
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 141 SASFLEWFAEEArrvygdiiPASAKDRRMLVLKQ-------PVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAED 213
Cdd:PRK13968 93 SANLCDWYAEHG--------PAMLKAEPTLVENQqavieyrPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 214 TPLSALALGELANQAGIPAGVYNVVPCSRQQTSAvgevLCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAP 293
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ----MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 294 FIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGFDENTTQGPLINEKAVEKV 373
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAA-ALKMGDPRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 374 ERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYS 453
Cdd:PRK13968 320 HHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728938489 454 QDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:PRK13968 400 TDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
42-509 |
1.08e-75 |
|
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: 246.59 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 42 WGGLVGGRWVEtPA---VFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDE 118
Cdd:cd07116 1 YDNFIGGEWVA-PVkgeYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 119 LARIITAENGKPLKEAQG-EILYSASFLEWFAEEARRVYGDIipaSAKDRRMLV--LKQPVGVSAIITPWNFPSAMITRK 195
Cdd:cd07116 80 LAVAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI---SEIDENTVAyhFHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 196 VGAALAAGCTVVVKPAEDTPLSALALGELANQAgIPAGVYNVVpcsRQQTSAVGEVLCTDPLVAKISFTGSTATGKILLK 275
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVV---NGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 276 HAAGTVKRVSMELGGHAPFIVFDS------ANVDCAVAGALASKYrNSGQTCVCTNRFLVQKGIHDKFVEnfaKAIER-- 347
Cdd:cd07116 233 YASENIIPVTLELGGKSPNIFFADvmdaddAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFME---RALERvk 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 348 ELRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKN----FFEPTLLTNvTTKMLCTQEETFGP 423
Cdd:cd07116 309 AIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 424 LAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAECPFGGVKQSGLGREGSKYGID 503
Cdd:cd07116 388 VLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLD 467
|
....*.
gi 1728938489 504 EYLEIK 509
Cdd:cd07116 468 HYQQTK 473
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
44-498 |
2.63e-74 |
|
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: 242.88 E-value: 2.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 44 GLVGGRWVETPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILysasflEW-----FA-EEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVG 197
Cdd:cd07130 81 SLEMGKILPEGLGEVQ------EMidicdFAvGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 198 AALAAGCTVVVKPAEDTPLSALALGELANQA----GIPAGVYNVVPCSRQqtsaVGEVLCTDPLVAKISFTGSTATGKIL 273
Cdd:cd07130 155 IALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGAD----VGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 274 LKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGS 353
Cdd:cd07130 231 GQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAY-KQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 354 GFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLTnVTTKMLCTQEETFGPLAPVIKFDTE 433
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 434 AEAVAIANAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVNEGiISSAEC--PFGGVKQSGLGRE-GS 498
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTTDLRNAfrWLGPKGSDCGIVNVNIG-TSGAEIggAFGGEKETGGGREsGS 457
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
45-506 |
2.18e-73 |
|
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: 241.31 E-value: 2.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPAVFPVQDPASGEE-LGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:TIGR01237 36 VINGERVETENKIVSINPCDKSEvVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAG 203
Cdd:TIGR01237 116 VKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 204 CTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGT--- 280
Cdd:TIGR01237 196 NCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGS---GSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVqpg 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 281 ---VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKaIERELRVGSGFDE 357
Cdd:TIGR01237 273 qkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVE-ITESLKVGPPDSA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 358 NTTQGPLINEKAVEKVERHINDAVSQGaSIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAV 437
Cdd:TIGR01237 352 DVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEAL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728938489 438 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GIISSAEcPFGGVKQSGLgreGSKYGIDEYL 506
Cdd:TIGR01237 431 EIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRnitGAIVGYQ-PFGGFKMSGT---DSKAGGPDYL 498
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-503 |
5.71e-72 |
|
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: 235.24 E-value: 5.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 87 HDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEwFAEEARRVYGDIIPASAKD 166
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAYHERTGERATPMAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 167 RRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVpcsrQQTS 246
Cdd:cd07095 89 GRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV----QGGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 247 AVGEVLCTDPLVAKISFTGSTATGKILLKHAAGTV-KRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTN 325
Cdd:cd07095 165 ETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCAR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 326 RFLVQKG-IHDKFVENFAKAIEReLRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPT 404
Cdd:cd07095 245 RLIVPDGaVGDAFLERLVEAAKR-LRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 405 LLtNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGII-SSAEC 483
Cdd:cd07095 324 II-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTgASSTA 402
|
410 420
....*....|....*....|
gi 1728938489 484 PFGGVKQSGLGREGSKYGID 503
Cdd:cd07095 403 PFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
45-506 |
1.10e-70 |
|
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: 234.40 E-value: 1.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPAVFPVQDPASGEE-LGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAAG 203
Cdd:cd07125 116 AAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 204 CTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKILLK---HAAGT 280
Cdd:cd07125 196 NTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDG---EEIGEALVAHPRIDGVIFTGSTETAKLINRalaERDGP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 281 VKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGFDENTT 360
Cdd:cd07125 273 ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMA-SLKVGDPWDLSTD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 361 QGPLINEKAVEKVERHINDAVSQGASIVTgGKRHSLGKNFFEPTLLTNVTTKMLctQEETFGPLAPVIKFDTEAEAVAIA 440
Cdd:cd07125 352 VGPLIDKPAGKLLRAHTELMRGEAWLIAP-APLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFKAEDLDEAIE 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 441 NAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSA--ECPFGGVKQSGLgreGSKYGIDEYL 506
Cdd:cd07125 429 DINATgyGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIvgRQPFGGWGLSGT---GPKAGGPNYL 495
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
96-505 |
2.13e-70 |
|
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: 231.34 E-value: 2.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 96 LPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEA--------QGEILYSASFLEWFAEEARRVYGDIIPASAKDR 167
Cdd:cd07135 24 KDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETlltevsgvKNDILHMLKNLKKWAKDEKVKDGPLAFMFGKPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 168 rmlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAgIPAGVYNVVpcsrqqTSA 247
Cdd:cd07135 104 ---IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVV------QGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 248 VGEvlcTDPLVA----KISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVC 323
Cdd:cd07135 174 VPE---TTALLEqkfdKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 324 TNRFLVQKGIHDKFVENFAKAIERelRVGSGFDENTTQGPLINEKAVEKVERHINDAvsqGASIVTGGKRhSLGKNFFEP 403
Cdd:cd07135 251 PDYVLVDPSVYDEFVEELKKVLDE--FYPGGANASPDYTRIVNPRHFNRLKSLLDTT---KGKVVIGGEM-DEATRFIPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 404 TLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGII--SSA 481
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVD 404
|
410 420
....*....|....*....|....
gi 1728938489 482 ECPFGGVKQSGLGREGSKYGIDEY 505
Cdd:cd07135 405 NAPFGGVGDSGYGAYHGKYGFDTF 428
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
97-504 |
2.44e-68 |
|
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: 225.48 E-value: 2.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 97 PAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQ--------GEILYSASFLEWFAEEaRRVYGDII--PASAKd 166
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiavvlGEIDHALKHLKKWMKP-RRVSVPLLlqPAKAY- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 167 rrmlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAgIPAGVYNVVPCSRQQTS 246
Cdd:cd07087 96 ----VIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVAT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 247 AvgevLCTDPLvAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNR 326
Cdd:cd07087 171 A----LLAEPF-DHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 327 FLVQKGIHDKFVENFAKAIERELrvGSGFDENTTQGPLINEKAVEKVERHINDAvsqgaSIVTGGKRHSlGKNFFEPTLL 406
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKEFY--GEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGGQVDK-EERYIAPTIL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 407 TNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGII--SSAECP 484
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLP 397
|
410 420
....*....|....*....|
gi 1728938489 485 FGGVKQSGLGREGSKYGIDE 504
Cdd:cd07087 398 FGGVGNSGMGAYHGKAGFDT 417
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
91-505 |
8.71e-67 |
|
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: 221.72 E-value: 8.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 91 AAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQ--------GEILYSASFLE-WFAeeARRVYGDIIP 161
Cdd:cd07134 12 LALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWMK--PKRVRTPLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 162 ASAKDRrmlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVynvvpcs 241
Cdd:cd07134 90 FGTKSK---IRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 242 rqqTSAVGEVLCTDPLVAK----ISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNS 317
Cdd:cd07134 160 ---AVFEGDAEVAQALLELpfdhIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 318 GQTCVCTNRFLVQKGIHDKFVENFAKAIERELrvgsGFDENTTQGP----LINEKAVEKVERHINDAVSQGASIVTGGKr 393
Cdd:cd07134 237 GQTCIAPDYVFVHESVKDAFVEHLKAEIEKFY----GKDAARKASPdlarIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 394 HSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGV 473
Cdd:cd07134 312 FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVV 391
|
410 420 430
....*....|....*....|....*....|....
gi 1728938489 474 NEGIISSAE--CPFGGVKQSGLGREGSKYGIDEY 505
Cdd:cd07134 392 NDVVLHFLNpnLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
46-506 |
4.50e-64 |
|
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: 216.68 E-value: 4.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVETPAVFPVQDP-ASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIIT 124
Cdd:cd07083 23 IGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 125 AENGKPLKEAQGEILYSASFLEWFAEEARRVYG--DIIPASAKDRRMLVLkQPVGVSAIITPWNFPSAMITRKVGAALAA 202
Cdd:cd07083 103 YEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 203 GCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQQtsaVGEVLCTDPLVAKISFTGSTATGKILLKHAA---- 278
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEE---VGAYLTEHERIRGINFTGSLETGKKIYEAAArlap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 279 --GTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGFD 356
Cdd:cd07083 259 gqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAER-LSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 357 ENTTQGPLINEKAVEKVERHINDAVSQGaSIVTGGKRHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEA 436
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728938489 437 VAIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISS--AECPFGGVKQSGlgrEGSKYGIDEYL 506
Cdd:cd07083 417 EALEVANSTpyGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAlvGVQPFGGFKLSG---TNAKTGGPHYL 487
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
97-512 |
3.58e-58 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 200.64 E-value: 3.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 97 PAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQ--------GEILYSASFL-EWFAEEARRVYGDIIPASAKdr 167
Cdd:PTZ00381 27 PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEHLLKHLdEYLKPEKVDTVGVFGPGKSY-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 168 rmlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAgIPAGVYNVVPCSRQQTSA 247
Cdd:PTZ00381 105 ---IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 248 vgevLCTDPLvAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRF 327
Cdd:PTZ00381 181 ----LLKEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 328 LVQKGIHDKFVENFAKAIERELrvGSGFDENTTQGPLINEKAVEKVERHINDavsQGASIVTGGKrHSLGKNFFEPTLLT 407
Cdd:PTZ00381 256 LVHRSIKDKFIEALKEAIKEFF--GEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 408 NVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAE--CPF 485
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNpnLPF 409
|
410 420
....*....|....*....|....*..
gi 1728938489 486 GGVKQSGLGREGSKYGIDEYLEIKYVC 512
Cdd:PTZ00381 410 GGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
45-509 |
3.21e-55 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 192.66 E-value: 3.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPA--VFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARI 122
Cdd:PLN00412 19 YADGEWRTSSSgkSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 123 ITAENGKPLKEAQGEILYSASFLEWFAEEARRVYG-------DIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRK 195
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 196 VGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPcsrQQTSAVGEVLCTDPLVAKISFTGSTaTGkILLK 275
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVT---GKGSEIGDFLTMHPGVNCISFTGGD-TG-IAIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 276 HAAGTVKrVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIEReLRVGSGf 355
Cdd:PLN00412 254 KKAGMVP-LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAK-LTVGPP- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 356 DENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSlgkNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAE 435
Cdd:PLN00412 331 EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREG---NLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 436 AVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAE-CPFGGVKQSGLGREGSKYGIDEYLEIK 509
Cdd:PLN00412 408 GIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVK 482
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
153-503 |
8.85e-54 |
|
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: 187.71 E-value: 8.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 153 RRVYGDIIPASAKDRRMlvlKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPA 232
Cdd:cd07136 81 KRVKTPLLNFPSKSYIY---YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 233 GVYnVVPCSRQQTSAVGEvLCTDplvaKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALAS 312
Cdd:cd07136 158 YVA-VVEGGVEENQELLD-QKFD----YIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 313 KYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIERelRVGSGFDENTTQGPLINEKAVEKVERHINDAvsqgaSIVTGGK 392
Cdd:cd07136 232 KFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKK--FYGEDPLESPDYGRIINEKHFDRLAGLLDNG-----KIVFGGN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 393 rHSLGKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVG 472
Cdd:cd07136 305 -TDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGC 383
|
330 340 350
....*....|....*....|....*....|...
gi 1728938489 473 VNEGII--SSAECPFGGVKQSGLGREGSKYGID 503
Cdd:cd07136 384 INDTIMhlANPYLPFGGVGNSGMGSYHGKYSFD 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
21-511 |
1.58e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 190.73 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 21 PPGPAAARWRSSW--------ALPASLVRWGGLVGGRWVET--PAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAG 90
Cdd:PLN02419 85 PLRPQFLALRSSWlstspeqsTQPQMPPRVPNLIGGSFVESqsSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 91 AAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRML 170
Cdd:PLN02419 165 PLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 171 VLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQQTSAVge 250
Cdd:PLN02419 245 SIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAI-- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 251 vlCTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLV- 329
Cdd:PLN02419 323 --CDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFv 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 330 --QKGIHDKFVENfAKAiereLRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIVTGGKR-----HSLGkNFFE 402
Cdd:PLN02419 401 gdAKSWEDKLVER-AKA----LKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKG-NFIG 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 403 PTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGI-ISSA 481
Cdd:PLN02419 475 PTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLP 554
|
490 500 510
....*....|....*....|....*....|..
gi 1728938489 482 ECPFGGVKQSGLGREG--SKYGIDEYLEIKYV 511
Cdd:PLN02419 555 FFSFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
46-503 |
2.42e-53 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 187.47 E-value: 2.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE-TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIIT 124
Cdd:PRK09457 5 INGDWIAgQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 125 AENGKPLKEAQGEI--------LYSASFLEWFAEEARrvygdiipaSAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKV 196
Cdd:PRK09457 85 RETGKPLWEAATEVtaminkiaISIQAYHERTGEKRS---------EMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 197 GAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRqqtsAVGEVLCTDPLVAKISFTGSTATGKILLKH 276
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGR----ETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 277 AAG-TVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIH-DKFVENFAKAIEReLRVGSG 354
Cdd:PRK09457 232 FAGqPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR-LTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 355 FDENTT-QGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLL--TNVTTKmlcTQEETFGPLAPVIKFD 431
Cdd:PRK09457 311 DAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIdvTGVAEL---PDEEYFGPLLQVVRYD 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 432 TEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GIISSAecPFGGVKQSGLGREGSKYGID 503
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKpltGASSAA--PFGGVGASGNHRPSAYYAAD 460
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
98-495 |
5.36e-53 |
|
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: 185.38 E-value: 5.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 98 AKERSVRLRRWYELMVENKDELARIITAENGKPLKE---------AQGEILYSASFL-EWFAEEARRVYGDIIPASAKdr 167
Cdd:cd07133 19 LEERRDRLDRLKALLLDNQDALAEAISADFGHRSRHetllaeilpSIAGIKHARKHLkKWMKPSRRHVGLLFLPAKAE-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 168 rmlVLKQPVGVSAIITPWNFP-----SAMItrkvgAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVynvvpcsr 242
Cdd:cd07133 97 ---VEYQPLGVVGIIVPWNYPlylalGPLI-----AALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 243 qqtsavgEVLCTDPLVAK---------ISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASK 313
Cdd:cd07133 161 -------AVVTGGADVAAafsslpfdhLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 314 YRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIERELRVGSGFDENTtqgPLINEKAVEKVERHINDAVSQGASIVTGGKR 393
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYT---SIINERHYARLQGLLEDARAKGARVIELNPA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 394 HSL--GKNFFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMV 471
Cdd:cd07133 311 GEDfaATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV 390
|
410 420
....*....|....*....|....*.
gi 1728938489 472 GVNEGI--ISSAECPFGGVKQSGLGR 495
Cdd:cd07133 391 TINDTLlhVAQDDLPFGGVGASGMGA 416
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
45-506 |
2.14e-51 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 182.80 E-value: 2.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPAVFPVQDPASGEE-LGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:TIGR01238 41 IIGHSYKADGEAQPVTNPADRRDiVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIpasakdrrmlvlKQPVGVSAIITPWNFPSAMITRKVGAALAAG 203
Cdd:TIGR01238 121 VREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFS------------VESRGVFVCISPWNFPLAIFTGQISAALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 204 CTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPcSRQQTsaVGEVLCTDPLVAKISFTGSTATGKILLKHAAgtvKR 283
Cdd:TIGR01238 189 NTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLP-GRGAD--VGAALTSDPRIAGVAFTGSTEVAQLINQTLA---QR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 284 VS------MELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIErELRVGSGFDE 357
Cdd:TIGR01238 263 EDapvpliAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQ-ELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 358 NTTQGPLINEKAVEKVERHINDAVSQGASI---VTGGKRHSLGKNFFEPTLLTNVTTKMLctQEETFGPLAPVIKF--DT 432
Cdd:TIGR01238 342 TTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFELDDIAEL--SEEVFGPVLHVVRYkaRE 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728938489 433 EAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSAEC--PFGGvkqSGLGREGSKYGIDEYL 506
Cdd:TIGR01238 420 LDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG---QGLSGTGPKAGGPHYL 492
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
43-506 |
4.28e-46 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 173.08 E-value: 4.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 43 GGLVGGrwveTPAVFPVQDPASGEE-LGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELAR 121
Cdd:PRK11904 554 GPIING----EGEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 122 IITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDII--PASAKDRRMLVLkQPVGVSAIITPWNFPSAMITRKVGAA 199
Cdd:PRK11904 630 LCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEklPGPTGESNELRL-HGRGVFVCISPWNFPLAIFLGQVAAA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 200 LAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKI----LLK 275
Cdd:PRK11904 709 LAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGD---GATVGAALTADPRIAGVAFTGSTETARIinrtLAA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 276 HAAGTVKRVSmELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGF 355
Cdd:PRK11904 786 RDGPIVPLIA-ETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAM-AELKVGDPR 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 356 DENTTQGPLINEKAVEKVERHInDAVSQGASIVTGGKRHSLGKN--FFEPTL--LTNVttKMLctQEETFGPLAPVIKFD 431
Cdd:PRK11904 864 LLSTDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPLPAGTENghFVAPTAfeIDSI--SQL--EREVFGPILHVIRYK 938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 432 TEaeavaianaadvGLA---------GY-----FYSQDPAQIWRVAEQLEVGMVGVNEGIISSA--ECPFGGvkqSGLGR 495
Cdd:PRK11904 939 AS------------DLDkvidainatGYgltlgIHSRIEETADRIADRVRVGNVYVNRNQIGAVvgVQPFGG---QGLSG 1003
|
490
....*....|.
gi 1728938489 496 EGSKYGIDEYL 506
Cdd:PRK11904 1004 TGPKAGGPHYL 1014
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
43-506 |
5.61e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 165.39 E-value: 5.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 43 GGLVGGRWVETPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARI 122
Cdd:PLN02315 22 GCYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 123 ITAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITRKVGAALAA 202
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 203 GCTVVVKPAEDTPLSALAL----GELANQAGIPAGVYNVVpCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAA 278
Cdd:PLN02315 182 GNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSF-CG---GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 279 GTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDEN 358
Cdd:PLN02315 258 ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVY-KQVKIGDPLEKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 359 TTQGPLINEKAVEKVERHINDAVSQGASIVTGGKRHSLGKNFFEPTLLtNVTTKMLCTQEETFGPLAPVIKFDTEAEAVA 438
Cdd:PLN02315 337 TLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728938489 439 IANAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVNEGiISSAEC--PFGGVKQSGLGREGSKYGIDEYL 506
Cdd:PLN02315 416 INNSVPQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNIP-TNGAEIggAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
45-431 |
1.38e-44 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 168.58 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRwVETPAVFPVQDPASGEE-LGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARII 123
Cdd:COG4230 561 LIAGE-AASGEARPVRNPADHSDvVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 124 TAENGKPLKEAQGEILYSASFLEWFAEEARRVYGDIIPAsakdrrmlvlkQPVGVSAIITPWNFPSAMITRKVGAALAAG 203
Cdd:COG4230 640 VREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVL-----------RGRGVFVCISPWNFPLAIFTGQVAAALAAG 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 204 CTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKI----LLKHAAG 279
Cdd:COG4230 709 NTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGD---GETVGAALVADPRIAGVAFTGSTETARLinrtLAARDGP 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 280 TVKRVSmELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTC-----VCtnrflVQKGIHDKFVENFAKAIeRELRVGSG 354
Cdd:COG4230 786 IVPLIA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCsalrvLC-----VQEDIADRVLEMLKGAM-AELRVGDP 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 355 FDENTTQGPLINEKAVEKVERHINDAVSQGASIvtggKRHSLGKN-----FFEPTL--LTNVttKMLctQEETFGPLAPV 427
Cdd:COG4230 859 ADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLPEEcangtFVAPTLieIDSI--SDL--EREVFGPVLHV 930
|
....
gi 1728938489 428 IKFD 431
Cdd:COG4230 931 VRYK 934
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
36-494 |
2.19e-44 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 168.12 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 36 PASLVRW--GGLVGGRWVETPAVfPVQDPA-SGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELM 112
Cdd:PRK11905 547 AFAAKTWhaAPLLAGGDVDGGTR-PVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLM 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 113 VENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRvygdiipASAKDRRmlvlkQPVGVSAIITPWNFPSAMI 192
Cdd:PRK11905 626 EAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARR-------LLNGPGH-----KPLGPVVCISPWNFPLAIF 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 193 TRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVLCTDPLVAKISFTGSTATGKI 272
Cdd:PRK11905 694 TGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGD---GRTVGAALVADPRIAGVMFTGSTEVARL 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 273 ----LLKHAAGTVKRVSmELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTnRFL-VQKGIHDKFVENFAKAIEr 347
Cdd:PRK11905 771 iqrtLAKRSGPPVPLIA-ETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVLcLQEDVADRVLTMLKGAMD- 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 348 ELRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQGASIvtggKRHSLGKN-----FFEPTLLTnvTTKMLCTQEETFG 422
Cdd:PRK11905 848 ELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPAEtekgtFVAPTLIE--IDSISDLEREVFG 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 423 PLAPVIKFDTEaeaVAIANAADVGLAGY-----FYSQDPAQIWRVAEQLEVGMVGVNEGII-----SSaecPFGGVKQSG 492
Cdd:PRK11905 922 PVLHVVRFKAD---ELDRVIDDINATGYgltfgLHSRIDETIAHVTSRIRAGNIYVNRNIIgavvgVQ---PFGGEGLSG 995
|
..
gi 1728938489 493 LG 494
Cdd:PRK11905 996 TG 997
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
97-503 |
3.35e-43 |
|
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: 158.92 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 97 PAKERSVRLRRWYELMVENKDELARIITAENGKPLKEA--------QGEILYSASFL-EWFAEEarrvYGDIIPASAKDR 167
Cdd:cd07132 18 PLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLpEWMKPE----PVKKNLATLLDD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 168 RMLVlKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELanqagIPAGV----YNVVpcsrq 243
Cdd:cd07132 94 VYIY-KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVV----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 244 qtsaVGEVLCTDPLVA----KISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQ 319
Cdd:cd07132 163 ----LGGVEETTELLKqrfdYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 320 TCVCTNRFLVQKGIHDKFVENFAKAIERelRVGSGFDENTTQGPLINEKAVEKVERHINdavsqGASIVTGGkRHSLGKN 399
Cdd:cd07132 239 TCIAPDYVLCTPEVQEKFVEALKKTLKE--FYGEDPKESPDYGRIINDRHFQRLKKLLS-----GGKVAIGG-QTDEKER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 400 FFEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIIS 479
Cdd:cd07132 311 YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMH 390
|
410 420
....*....|....*....|....*.
gi 1728938489 480 SA--ECPFGGVKQSGLGREGSKYGID 503
Cdd:cd07132 391 YTldSLPFGGVGNSGMGAYHGKYSFD 416
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
97-511 |
2.68e-41 |
|
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: 153.72 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 97 PAKERSVRLRRWYELMVENKDELARIITAENGKPLKEA-QGEI--LYSASFL------EWFAEEARRVYGDIIPASAKdr 167
Cdd:cd07137 19 SAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvLVSSCKLaikelkKWMAPEKVKTPLTTFPAKAE-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 168 rmlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELanqagIPAGVYNVVPCSRQQTSA 247
Cdd:cd07137 97 ---IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-----IPEYLDTKAIKVIEGGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 248 VGEVLcTDPLVAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKY-RNSGQTCVCTNR 326
Cdd:cd07137 169 ETTAL-LEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 327 FLVQKGihdkFVENFAKAIERELRVGSGFDENTTQ--GPLINEKAVEKVERHINDAVSQgASIVTGGKRHSlGKNFFEPT 404
Cdd:cd07137 248 VLVEES----FAPTLIDALKNTLEKFFGENPKESKdlSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERDE-KNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 405 LLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSA--E 482
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAidT 401
|
410 420
....*....|....*....|....*....
gi 1728938489 483 CPFGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
88-494 |
3.59e-39 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 152.82 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 88 DAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVYgdiipaSAKDR 167
Cdd:PRK11809 693 NAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDF------DNDTH 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 168 RmlvlkqPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPcSRQQTsa 247
Cdd:PRK11809 767 R------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLP-GRGET-- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 248 VGEVLCTDPLVAKISFTGSTATGKILLKHAAGtvkRVS---------MELGGHAPFIVFDSANVDCAVAGALASKYRNSG 318
Cdd:PRK11809 838 VGAALVADARVRGVMFTGSTEVARLLQRNLAG---RLDpqgrpipliAETGGQNAMIVDSSALTEQVVADVLASAFDSAG 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 319 QTCVCTNRFLVQKGIHDKFVENFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERHI------NDAVSQGASIVTGGK 392
Cdd:PRK11809 915 QRCSALRVLCLQDDVADRTLKMLRGAM-AECRMGNPDRLSTDIGPVIDAEAKANIERHIqamrakGRPVFQAARENSEDW 993
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 393 RHSlgkNFFEPTLLTNVTTKMLctQEETFGPLAPVIKFDTEAEAVAIANaadVGLAGY-----FYSQDPAQIWRVAEQLE 467
Cdd:PRK11809 994 QSG---TFVPPTLIELDSFDEL--KREVFGPVLHVVRYNRNQLDELIEQ---INASGYgltlgVHTRIDETIAQVTGSAH 1065
|
410 420
....*....|....*....|....*....
gi 1728938489 468 VGMVGVNEGIISSAEC--PFGGVKQSGLG 494
Cdd:PRK11809 1066 VGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
101-511 |
3.64e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 140.25 E-value: 3.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 101 RSVRLRRWYELMVENKDELARIITAENGKPLKEAQ----GEILYSASFL-----EWFAEEARRVYGDIIPASAKdrrmlV 171
Cdd:PLN02203 30 RKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYrdevGVLTKSANLAlsnlkKWMAPKKAKLPLVAFPATAE-----V 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 172 LKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGelanqAGIPAGVYNVVPCSRQQTSAVGEV 251
Cdd:PLN02203 105 VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPKYLDSKAVKVIEGGPAVGEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 252 LCTDPLvAKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIV--FDSA-NVDCAVAGALASKYRN-SGQTCVCTNRF 327
Cdd:PLN02203 180 LLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 328 LVQKGIHDKFVENFAKAIERELrvGSGFDENTTQGPLINEKAVEKVERHINDAVSQgASIVTGGkrHSLGKNFF-EPTLL 406
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFF--GENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGG--SIDEKKLFiEPTIL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 407 TNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGIISSA--ECP 484
Cdd:PLN02203 334 LNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSLP 413
|
410 420
....*....|....*....|....*..
gi 1728938489 485 FGGVKQSGLGREGSKYGIDEYLEIKYV 511
Cdd:PLN02203 414 FGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
147-516 |
2.92e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 126.31 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 147 WFAEEARRVYGDIIPASAKdrrmlVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELAN 226
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 227 QAGIPAGVyNVVPCSRQQTSAVGEVLCTdplvaKISFTGSTATGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAV 306
Cdd:PLN02174 164 QYLDSSAV-RVVEGAVTETTALLEQKWD-----KIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 307 AGALASKYR-NSGQTCVCTNRFLVQKGIHDKFVEnfAKAIERELRVGSGFDENTTQGPLINEKAVEKVERHInDAVSQGA 385
Cdd:PLN02174 238 RRIIAGKWGcNNGQACISPDYILTTKEYAPKVID--AMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLL-DEKEVSD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 386 SIVTGGKRHSlgKNF-FEPTLLTNVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAE 464
Cdd:PLN02174 315 KIVYGGEKDR--ENLkIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAA 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1728938489 465 QLEVGMVGVNEGIISSA--ECPFGGVKQSGLGREGSKYGIDEYLEIKYVCFGGL 516
Cdd:PLN02174 393 TVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSL 446
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
178-492 |
1.55e-28 |
|
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: 118.84 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 178 VSAIiTPWNFPSamitrkVGAALAA-----GCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSrqqTSAVGEVL 252
Cdd:cd07123 174 VYAV-SPFNFTA------IGGNLAGapalmGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD---GPVVGDTV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 253 CTDPLVAKISFTGSTATGKILLKHAAG------TVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNR 326
Cdd:cd07123 244 LASPHLAGLHFTGSTPTFKSLWKQIGEnldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 327 FLVQKGIHDKFVENFAKAIErELRVGSGFDENTTQGPLINEKAVEKVERHINDAVSQ-GASIVTGGK-RHSLGKnFFEPT 404
Cdd:cd07123 324 AYVPESLWPEVKERLLEELK-EIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKcDDSVGY-FVEPT 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 405 LL--TNVTTKMLctQEETFGPLAPVIKFDTEAEAVAIANAADV---GLAGYFYSQDPAQIWRVAEQLE--VGMVGVNE-- 475
Cdd:cd07123 402 VIetTDPKHKLM--TEEIFGPVLTVYVYPDSDFEETLELVDTTspyALTGAIFAQDRKAIREATDALRnaAGNFYINDkp 479
|
330
....*....|....*...
gi 1728938489 476 -GIIsSAECPFGGVKQSG 492
Cdd:cd07123 480 tGAV-VGQQPFGGARASG 496
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
87-468 |
5.04e-26 |
|
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: 110.41 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 87 HDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAqGEILYSASFLEWFAE--EARRVYGDIIPASA 164
Cdd:cd07084 9 DISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFviYSYRIPHEPGNHLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 165 KDRRMLVLKQ--PVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGI-PAGVYNVVpCS 241
Cdd:cd07084 88 QGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLI-NG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 242 RQQTSAvgeVLCTDPLVAKISFTGSTATGKILLKHAAGTvkRVSMELGGHAPFIVFDSANVDCAVAGALA-SKYRNSGQT 320
Cdd:cd07084 167 DGKTMQ---ALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVqDMTACSGQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 321 CVCTNRFLV-----QKGIHDKFVENFAKAIERELRVGSGFDENTtqgplinEKAVEKVERHINDAVSQGASIVtggKRHS 395
Cdd:cd07084 242 CTAQSMLFVpenwsKTPLVEKLKALLARRKLEDLLLGPVQTFTT-------LAMIAHMENLLGSVLLFSGKEL---KNHS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 396 LGKNF--FEPTLLTNVTTKMLCT----QEETFGPLAPVIKF--DTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLE 467
Cdd:cd07084 312 IPSIYgaCVASALFVPIDEILKTyelvTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLW 391
|
.
gi 1728938489 468 V 468
Cdd:cd07084 392 V 392
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
46-466 |
1.45e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 104.02 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE-TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIIT 124
Cdd:PRK11903 9 VAGRWQAgSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 125 AENGKPLKEA----QGEILYSASFLEWFAE-EARRVYGDIIPAS-AKDRR---MLVLKQPVGVSAIITPWNFPSAMITRK 195
Cdd:PRK11903 89 ANSGTTRNDSavdiDGGIFTLGYYAKLGAAlGDARLLRDGEAVQlGKDPAfqgQHVLVPTRGVALFINAFNFPAWGLWEK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 196 VGAALAAGCTVVVKPAEDTPLSALALGELANQAGI-PAGVYNVVpC--SRQQTSAVGE--VLctdplvakiSFTGSTATG 270
Cdd:PRK11903 169 AAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV-CgsSAGLLDHLQPfdVV---------SFTGSAETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 271 KILLKHAAGTVK--RVSME---------LGGHAPfivfDSANVDCAVAGALASKYRNSGQTCVCTNRFLVQKGIHDKFVE 339
Cdd:PRK11903 239 AVLRSHPAVVQRsvRVNVEadslnsallGPDAAP----GSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 340 NFAKAIeRELRVGSGFDENTTQGPLINEKAVEKVERHInDAVSQGASIVTGGKRHSL------GKNFFEPTLL--TNVTT 411
Cdd:PRK11903 315 ALAARL-AKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACVGPTLLgaSDPDA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1728938489 412 KMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAQIWRVAEQL 466
Cdd:PRK11903 393 ATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
87-433 |
9.22e-22 |
|
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: 98.00 E-value: 9.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 87 HDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIITAENGKPLKEAQGEILYSASFLEWFAEEARR--VYGDII---- 160
Cdd:cd07129 9 AAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsWLDARIdpad 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 161 ----PASAKD-RRMLVlkqPVGVSAIITPWNFPSAMITrkVG----AALAAGCTVVVKPAEDTPLSALALGELANQA--- 228
Cdd:cd07129 89 pdrqPLPRPDlRRMLV---PLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARAIRAAlra 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 229 -GIPAGVYNVVPCSRqqtSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAgtvKR-----VSMELGGHAPFIVFDSANV 302
Cdd:cd07129 164 tGLPAGVFSLLQGGG---REVGVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARpepipFYAELGSVNPVFILPGALA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 303 DCAVA---GALASKYRNSGQTCVCTNRFLVQKGIH-DKFVENFAKAIERelrvgsgfdenTTQGPLINEKAVEKVERHIN 378
Cdd:cd07129 238 ERGEAiaqGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA-----------APAQTMLTPGIAEAYRQGVE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728938489 379 DAVSQGASIVTGGKRHSLGKNFFEPTLLTNVTTKMLCT---QEETFGPLAPVIKFDTE 433
Cdd:cd07129 307 ALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLADpalQEEVFGPASLVVRYDDA 364
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
46-470 |
2.79e-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: 96.96 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 46 VGGRWVE-TPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAKERSVRLRRWYELMVENKDELARIiT 124
Cdd:cd07128 5 VAGQWHAgTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYAL-S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 125 AENGKPLKEAQGEILYSASFLEWFAEEARR--------VYGDIIPASaKD-----RRMLVLKQpvGVSAIITPWNFPSAM 191
Cdd:cd07128 84 AATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLS-KDgtfvgQHILTPRR--GVAVHINAFNFPVWG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 192 ITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGI-PAGVYNVVpcsrqqTSAVGEVLctDPLVAK--ISFTGSTA 268
Cdd:cd07128 161 MLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLI------CGSVGDLL--DHLGEQdvVAFTGSAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 269 TGKILLKHAAGTVK--RVSMELgghapfivfDSANvdCAVAGA-------------------LASKyrnSGQTCVCTNRF 327
Cdd:cd07128 233 TAAKLRAHPNIVARsiRFNAEA---------DSLN--AAILGPdatpgtpefdlfvkevareMTVK---AGQKCTAIRRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 328 LVQKGIHDKFVENfAKAIERELRVGSGFDENTTQGPLINEKAVEKVERHInDAVSQGASIVTGGKRHSLGKN-------F 400
Cdd:cd07128 299 FVPEARVDAVIEA-LKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGadaekgaF 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728938489 401 FEPTLLT--NVTTKMLCTQEETFGPLAPVIKFDTEAEAVAIANAADVGLAGYFYSQDPAqiwrVAEQLEVGM 470
Cdd:cd07128 377 FPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPA----FARELVLGA 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
45-433 |
5.45e-09 |
|
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: 58.28 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 45 LVGGRWVETPAVFPVQDPASGEELGRVADCGVAEAREAVRAAHDAGAAWGRLPAK--ER-----SVRLRRWYEL-MVENK 116
Cdd:cd07126 2 LVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERyllygDVSHRVAHELrKPEVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 117 DELARIITAENGKPLKEAQGEILYSASFLEWFAEEARRVY--GDIIPASAKDRRMLVLKQPVGVSAIITPWNFPSAMITR 194
Cdd:cd07126 82 DFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLarSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 195 KVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGVYNVVPCSRQQTSAVgeVLCTDPLVakISFTGSTATGKILL 274
Cdd:cd07126 162 QLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKI--LLEANPRM--TLFTGSSKVAERLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 275 KHAAGTVKrvsMELGGHAPFIVF-DSANVDCAVAGALASKYRNSGQTCVCTNRFL-----VQKGIHDKFVenfAKAIERE 348
Cdd:cd07126 238 LELHGKVK---LEDAGFDWKILGpDVSDVDYVAWQCDQDAYACSGQKCSAQSILFahenwVQAGILDKLK---ALAEQRK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 349 LrvgsgfdENTTQGPLINEKAvEKVERHINDAVS-QGASIVTGGK---RHSLGKNF--FEPT--------LLTNVTTKML 414
Cdd:cd07126 312 L-------EDLTIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKpltNHSIPSIYgaYEPTavfvpleeIAIEENFELV 383
|
410
....*....|....*....
gi 1728938489 415 CTqeETFGPLAPVIKFDTE 433
Cdd:cd07126 384 TT--EVFGPFQVVTEYKDE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
88-342 |
3.92e-07 |
|
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: 52.23 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 88 DAGAAWGRLPAKERSVRLRR----WYELMVENKDELARIITAENGKPLKEAqgeilysasflewfaeearRVYGDIIPAS 163
Cdd:cd07077 31 DTRQRLASEAVSERGAYIRSlianWIAMMGCSESKLYKNIDTERGITASVG-------------------HIQDVLLPDN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 164 AKdrrMLVLKQPVGVSAIITPWNFPSAMITrKVGAALAAGCTVVVKPAEDTPLSALALgELANQAGIPA-GVYNVVPCSR 242
Cdd:cd07077 92 GE---TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL-ALLFQAADAAhGPKILVLYVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 243 QQTSAVGEVLCTDPLVAKISFTGSTATGKILLKHAAGtvKRVsMELGGHAPFIVFDS-ANVDCAVAGALASKYRNsGQTC 321
Cdd:cd07077 167 HPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPH--IPV-IGFGAGNSPVVVDEtADEERASGSVHDSKFFD-QNAC 242
|
250 260
....*....|....*....|.
gi 1728938489 322 VCTNRFLVQKGIHDKFVENFA 342
Cdd:cd07077 243 ASEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
175-469 |
2.13e-06 |
|
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: 50.17 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 175 PVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGV-YNVVPCSRQQTSA-VGEVL 252
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFdPNLVTLAADTPEEpIAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 253 CTDPLVAKISFTGSTATGKILLKHAAGtvKRVSMELGGHAPFIVfDSANVDCAVAGALA---SKYrnSGQTCVCTNRFLV 329
Cdd:cd07127 273 ATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVV-DSTDDLKAMLRNLAfslSLY--SGQMCTTPQNIYV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 330 QK-GI--------HDKFVENFAKAIERELrvGSGFDENTTQGPLINEKAVEKVErhindAVSQGASIVTGGKrhSLGKNF 400
Cdd:cd07127 348 PRdGIqtddgrksFDEVAADLAAAIDGLL--ADPARAAALLGAIQSPDTLARIA-----EARQLGEVLLASE--AVAHPE 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728938489 401 FE------PTLLTNVTTKMLCTQEETFGPLAPVIKFDT--EAEAVAIANAADVG-LAGYFYSQDPAQIWRVAE-QLEVG 469
Cdd:cd07127 419 FPdarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDStdHSIELARESVREHGaMTVGVYSTDPEVVERVQEaALDAG 497
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
170-342 |
9.19e-06 |
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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: 48.03 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 170 LVLKQPVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPAGV-YNVVPCSRQQTSAV 248
Cdd:cd07081 90 LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGApENLIGWIDNPSIEL 169
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 249 GEVLCTDPLVAKISFTGstatGKILLKHAAGTVKRVSMELGGHAPFIVFDSANVDCAVAGALASKYRNSGQTCVCTNRFL 328
Cdd:cd07081 170 AQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVI 245
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170
....*....|....
gi 1728938489 329 VQKGIHDKFVENFA 342
Cdd:cd07081 246 VVDSVYDEVMRLFE 259
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| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
175-309 |
5.30e-03 |
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aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 39.50 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 175 PVGVSAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPLSALALGELANQAGIPA-GVYNVVPCSRQQTSAVGEVLC 253
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAgGPENLVVTVAEPTIETAQRLM 208
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728938489 254 TDPLVAKISFTGSTATGKILLKhaagTVKRVSMELGGHAPFIVFDSANVDCA----VAGA 309
Cdd:PRK15398 209 KHPGIALLVVTGGPAVVKAAMK----SGKKAIGAGAGNPPVVVDETADIEKAardiVKGA 264
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