|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
20-865 |
0e+00 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 1534.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 20 MIDALADKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGRGIYEDKAIKNLYASEYIWNSIKDNKTVG 99
Cdd:PRK13805 13 ELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDKVIKNHFASEYIYNSYKDEKTVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 100 IIGEDKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDII 179
Cdd:PRK13805 93 VIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAAVAAGAPKDII 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 180 QWIEVPSIEATKQLMNHKGIALVLATGGSGMVKSAYSTGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICA 259
Cdd:PRK13805 173 QWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTFDNGMICA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 260 SEQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQRLENAIMNEQKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIAEISG 339
Cdd:PRK13805 253 SEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFGKENGALNADIVGQSAYKIAEMAGFKVPEDTKILIAEVKG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 340 VGSDYPLSREKLSPVLALVKAQSTKQAFQICEDTLHFGGLGHTAVIHTEDETLQKDFGLRMKACRVLVNTPSAVGGIGDM 419
Cdd:PRK13805 333 VGESEPLSHEKLSPVLAMYKAKDFEDAVEKAEKLVEFGGLGHTAVIYTNDDELIKEFGLRMKACRILVNTPSSQGGIGDL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 420 YNELIPSLTLGCGSYGRNSISHNVSATDLLNIKTIAKRRNNTQIFKVPAQIYFEENAIMSLTT-MDKIEKVMIVCDPGMV 498
Cdd:PRK13805 413 YNKLAPSLTLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLLDeLDGKKRAFIVTDRFMV 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 499 EFGYTKTVENVLRQKTEQPQIKIFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMWMFFEHPETSFFGA 578
Cdd:PRK13805 493 ELGYVDKVTDVLKKRENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLFYEHPETDFEDL 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 579 KQKFLDIGKRTYKIG-MPENATFICIPTTSGTGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTAD 657
Cdd:PRK13805 573 AQKFMDIRKRIYKFPkLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTAD 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 658 TGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG--DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKI 735
Cdd:PRK13805 653 TGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGakDPEAREKMHNASTIAGMAFANAFLGICHSMAHKL 732
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 736 GGEYGIPHGRANAILLPHIIRYNAKDPQKHALFPKYEFFRADTDYADIAKFLGLKGNTTEALVESLAKAVYELGQSVGIE 815
Cdd:PRK13805 733 GAEFHIPHGRANAILLPHVIRYNATDPPKQAAFPQYEYPRADERYAEIARHLGLPGSTTEEKVESLIKAIEELKAELGIP 812
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 88193926 816 MNLKSQGVSEEELNESIDRMAELAFEDQCTTANPKEALISEIKDIIQTSY 865
Cdd:PRK13805 813 MSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYPLISELKEILLDAY 862
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
21-457 |
0e+00 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 685.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 21 IDALADKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGRGIYEDKAIKNLYASEYIWNSIKDNKTVGI 100
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYNDIKDMKTVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 101 IGEDKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDIIQ 180
Cdd:cd07122 81 IEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 181 WIEVPSIEATKQLMNHKGIALVLATGGSGMVKSAYSTGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICAS 260
Cdd:cd07122 161 WIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 261 EQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQRLENAIMNEQKTgIKPDIVGKSAVEIAELAGIPVPENTKLIIAEISGV 340
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDDGGT-LNPDIVGKSAQKIAELAGIEVPEDTKVLVAEETGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 341 GSDYPLSREKLSPVLALVKAQSTKQAFQICEDTLHFGGLGHTAVIHTEDETLQKDFGLRMKACRVLVNTPSAVGGIGDMY 420
Cdd:cd07122 320 GPEEPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPSSLGGIGDTY 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 88193926 421 NELIPSLTLGCGSYGRNSISHNVSATDLLNIKTIAKR 457
Cdd:cd07122 400 NGLAPSLTLGCGSWGGNSTSDNVGPKHLLNIKRVAYR 436
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
465-860 |
0e+00 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 636.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 465 KVPAQIYFEENAIMSL-TTMDKIEKVMIVCDPGMVEFGYTKTVENVLRQKteQPQIKIFSEVEPNPSTNTVYKGLEMMVD 543
Cdd:cd08178 1 KVPPKIYFEPGCLPYLlLELPGVKRAFIVTDRVLYKLGYVDKVLDVLEAR--GVETEVFSDVEPDPTLSTVRKGLEAMNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 544 FQPDTIIALGGGSAMDAAKAMWMFFEHPETSFFGAKQKFLDIGKRTYKI-GMPENATFICIPTTSGTGSEVTPFAVITDS 622
Cdd:cd08178 79 FKPDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFpKLGKKAKLVAIPTTSGTGSEVTPFAVITDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 623 ETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG- 701
Cdd:cd08178 159 KTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGn 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 702 DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKD-PQKHALFPKYEFFRADTDY 780
Cdd:cd08178 239 DIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDpPTKQAAFPQYKYYVAKERY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 781 ADIAKFLGLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEELNESIDRMAELAFEDQCTTANPKEALISEIKDI 860
Cdd:cd08178 319 AEIADLLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISELKEI 398
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
460-865 |
3.37e-163 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 480.00 E-value: 3.37e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 460 NTQIFKVPAQIYFEENAIMSL-TTMDK--IEKVMIVCDPGMVEFGYTKTVENVLRQktEQPQIKIFSEVEPNPSTNTVYK 536
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELgEELKRlgAKRALIVTDPGLAKLGLLDRVLDALEA--AGIEVVVFDDVEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 537 GLEMMVDFQPDTIIALGGGSAMDAAKAMWMFFEHPETsffgakqkFLD-IGKRTYKIGMPEnatFICIPTTSGTGSEVTP 615
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGD--------LEDyLGIKKVPGPPLP---LIAIPTTAGTGSEVTP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 616 FAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLK 695
Cdd:COG1454 148 FAVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 696 SSVEKG-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhalfpkyeff 774
Cdd:COG1454 228 RAVADGdDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAP-------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 775 RADTDYADIAKFLGLK-GNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEAL 853
Cdd:COG1454 294 AAPERYAEIARALGLDvGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEED----LPELAELALADRCLANNPRPLT 369
|
410
....*....|..
gi 88193926 854 ISEIKDIIQTSY 865
Cdd:COG1454 370 EEDIEAILRAAY 381
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
463-865 |
2.16e-159 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 470.13 E-value: 2.16e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 463 IFKVPAQIYFEENAIMSLTTMDKiEKVMIVCDPG-MVEFGYTKTVENVLRQKteQPQIKIFSEVEPNPSTNTVYKGLEMM 541
Cdd:cd08179 1 RFFVPRDIYFGEGALEYLKTLKG-KRAFIVTGGGsMKRNGFLDKVEDYLKEA--GMEVKVFEGVEPDPSVETVEKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 542 VDFQPDTIIALGGGSAMDAAKAMWMFFEHPETSFFGAKQKFlDIGKRTYKigmpenATFICIPTTSGTGSEVTPFAVITD 621
Cdd:cd08179 78 REFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALVPF-PLPELRKK------ARFIAIPSTSGTGSEVTRASVITD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 622 SETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG 701
Cdd:cd08179 151 TEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 702 -DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKDPQKhalfpkyeffradtDY 780
Cdd:cd08179 231 kDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEA--------------RA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 781 ADIAKflgLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEELNESIDRMAELAFEDQCTTANPKEALISEIKDI 860
Cdd:cd08179 297 RYAAL---LIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNDACTGTNPRKPTVEEMKEL 373
|
....*
gi 88193926 861 IQTSY 865
Cdd:cd08179 374 LKAAY 378
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
24-455 |
8.12e-153 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 457.79 E-value: 8.12e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 24 LADKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGRGIYEDKAIKNLYASEYIWNSIKDNKTVGIIGE 103
Cdd:TIGR02518 13 LIRSAKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVYDSIKDMKTIGILSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 104 DKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDIIQWIE 183
Cdd:TIGR02518 93 DKEKKVIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPEGAIGCIT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 184 VPSIEATKQLMNHKGIALVLATGGSGMVKSAYSTGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQV 263
Cdd:TIGR02518 173 VPTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICASEQS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 264 VVIDKEIYKDVTNEFKAHQAYFVKKDELQRLENAIMNEQKTgIKPDIVGKSAVEIAELAGIPVPENTKLIIAEISGVGSD 343
Cdd:TIGR02518 253 IIVEECNKDAVVEELKKQGGYFLTAEEAEKLGKFILRPNGT-MNPQIVGKSPQVIANLAGLTVPEDAKVLIGEQNGVGNK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 344 YPLSREKLSPVLALVKAQSTKQAFQICEDTLHFGGLGHTAVIHTEDETLQKDFGLRMKACRVLVNTPSAVGGIGDMYNeL 423
Cdd:TIGR02518 332 NPYSREKLTTILAFYTEENWHEACELSIELLQNEGAGHTLIIHSENKDIVREFALKKPVSRMLVNTGGSLGGIGATTN-L 410
|
410 420 430
....*....|....*....|....*....|..
gi 88193926 424 IPSLTLGCGSYGRNSISHNVSATDLLNIKTIA 455
Cdd:TIGR02518 411 VPAFTLGCGAVGGSSTSDNITPENLINIRRVA 442
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
464-861 |
6.43e-145 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 431.15 E-value: 6.43e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTTMdKIEKVMIVCDPGMVEFGYTKTVENVLRQKTEqpqIKIFSEVEPNPSTNTVYKGLEMMVD 543
Cdd:cd08180 1 FSLKTKIYSGEDSLERLKEL-KGKRVFIVTDPFMVKSGMVDKVTDELDKSNE---VEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 544 FQPDTIIALGGGSAMDAAKAMwmffehpetSFFGAKQKfldigkrtykiGMPENATFICIPTTSGTGSEVTPFAVITDSE 623
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAKAI---------IYFALKQK-----------GNIKKPLFIAIPTTSGTGSEVTSFAVITDPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 624 TNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-D 702
Cdd:cd08180 137 KGIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGdD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 703 KVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYnakdpqkhalfpkyeffradtdyad 782
Cdd:cd08180 217 LEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF------------------------- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88193926 783 iakflglkgnttealvesLAKAVYELGQSVGIEMNLKSQGVSEEELNESIDRMAELAFEDQCTTANPKEALISEIKDII 861
Cdd:cd08180 272 ------------------LIAAIRRLNKKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIELL 332
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
21-457 |
1.37e-143 |
|
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: 432.07 E-value: 1.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 21 IDALADKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGRGIYEDKAIKNLYASEYIWNSIKDNKTVGI 100
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 101 IGEDKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDIIQ 180
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 181 WIEVPSIEATKQLMNHKGIALVLATGGSGMVKSAYSTGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICAS 260
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 261 EQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQRLENAIMneQKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIAEISGV 340
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVIL--KNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 341 GSDYPLSREKLSPVLALVKAQSTKQAFQICEDTLHFGGLGHTAVIHTeDETLQKD----FGLRMKACRVLVNTPSAVGGI 416
Cdd:cd07081 319 AEHEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSAMYS-DNIKAIEnmnqFANAMKTSRFVKNGPCSQGGL 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 88193926 417 GDMYNELI-PSLTLGCGSYGRNSISHNVSATDLLNIKTIAKR 457
Cdd:cd07081 398 GDLYNFRGwPSMTLGCGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
467-861 |
1.20e-127 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 387.96 E-value: 1.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSLTTMDK---IEKVMIVCDPGMVEFGYTKTVENVLRQktEQPQIKIFSEVEPNPSTNTVYKGLEMMVD 543
Cdd:cd08551 1 PTRIVFGAGALARLGEELKalgGKKVLLVTDPGLVKAGLLDKVLESLKA--AGIEVEVFDDVEPNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 544 FQPDTIIALGGGSAMDAAKAMWMFFEHPETSffgakQKFLDIGKRTYKiGMPenatFICIPTTSGTGSEVTPFAVITDSE 623
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAVLATNGGSI-----RDYEGIGKVPKP-GLP----LIAIPTTAGTGSEVTPNAVITDPE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 624 TNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-D 702
Cdd:cd08551 149 TGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGsD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 703 KVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAK-DPQKhalfpkyeffradtdYA 781
Cdd:cd08551 229 LEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPaCPEK---------------YA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 782 DIAKFLGLK--GNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTAN-PKEALISEIK 858
Cdd:cd08551 294 EIAEALGEDveGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEED----IPELAEDAMKSGRLLSNnPRPLTEEDIR 369
|
...
gi 88193926 859 DII 861
Cdd:cd08551 370 EIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
467-857 |
8.19e-126 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 383.11 E-value: 8.19e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSL-TTMDKI-EKVMIVCDPGMVEFGYTKTVENVLRQKteQPQIKIFSEVEPNPSTNTVYKGLEMMVDF 544
Cdd:pfam00465 1 PTRIVFGAGALAELgEELKRLgARALIVTDPGSLKSGLLDKVLASLEEA--GIEVVVFDGVEPEPTLEEVDEAAALAREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 545 QPDTIIALGGGSAMDAAKAMWMFFEHPETSFFgakqkfLDIGKRTYKIGMPenatFICIPTTSGTGSEVTPFAVITDSET 624
Cdd:pfam00465 79 GADVIIAVGGGSVIDTAKAIALLLTNPGDVWD------YLGGKPLTKPALP----LIAIPTTAGTGSEVTPLAVITDTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 625 NVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-DK 703
Cdd:pfam00465 149 GEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGeDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 704 VSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhalfpkyeffRADTDYADI 783
Cdd:pfam00465 229 EARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAP--------------AAPEKLAQL 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88193926 784 AKFLGlkGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEI 857
Cdd:pfam00465 295 ARALG--EDSDEEAAEEAIEALRELLRELGLPTTLSELGVTEED----LDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
466-861 |
3.61e-115 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 355.76 E-value: 3.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 466 VPAQIYFEENAIMSLTTMDKiEKVMIVCDPGMVEFGYTKTVENVLRQKTEQpqIKIFSEVEPNPSTNTVYKGLEMMVDFQ 545
Cdd:cd14862 5 SSPKIVFGEDALSHLEQLSG-KRALIVTDKVLVKLGLLKKVLKRLLQAGFE--VEVFDEVEPEPPLETVLKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 546 PDTIIALGGGSAMDAAKAMWMFFEHPETSFFGAKqkFLDIGKRTYKigmpenATFICIPTTSGTGSEVTPFAVITDSETN 625
Cdd:cd14862 82 PDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIS--PLDLLGLRKK------AKLIAIPTTSGTGSEATWAIVLTDTEEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 626 VKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-DKV 704
Cdd:cd14862 154 RKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGdDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 705 SREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKDpqkhalfpkyeffraDTDYADIA 784
Cdd:cd14862 234 AREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKV---------------TDERYDLL 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88193926 785 KFLGLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEELNESIDRMAELAFEDQCTTANPKEALISEIKDII 861
Cdd:cd14862 299 KLLGIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
464-861 |
5.22e-112 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 347.58 E-value: 5.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTTMDKI---EKVMIVCDPGMVEFGYTKTVENVLrqKTEQPQIKIFSEVEPNPSTNTVYKGLEM 540
Cdd:cd08188 3 FYIPPVNLFGPGCLKEIGDELKKlggKKALIVTDKGLVKLGLVKKVTDVL--EEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 541 MVDFQPDTIIALGGGSAMDAAKAMWMFFEHPetsffGAKQKFLDIGKRTyKIGMPenatFICIPTTSGTGSEVTPFAVIT 620
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNG-----GEIEDYEGVDKSK-KPGLP----LIAINTTAGTASEVTRFAVIT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 621 DSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEK 700
Cdd:cd08188 151 DEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 701 G-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAK-DPQKhalfpkyeffradt 778
Cdd:cd08188 231 GkDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPaCPER-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 779 dYADIAKFLGLK--GNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISE 856
Cdd:cd08188 297 -FADIARALGENteGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEED----FPLLAENALKDACGPTNPRQATKED 371
|
....*
gi 88193926 857 IKDII 861
Cdd:cd08188 372 VIAIY 376
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
488-862 |
8.98e-104 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 326.04 E-value: 8.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 488 KVMIVCDPGMVEFGYTKTVENVLrqktEQPQIK--IFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMW 565
Cdd:cd08176 30 KALIVTDKGLVKFGIVDKVTDVL----KEAGIAytVFDEVKPNPTIENVMAGVAAYKESGADGIIAVGGGSSIDTAKAIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 566 MFFEHPetsffGAKQKFLDIGKRTYKIGMPenatFICIPTTSGTGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQ 645
Cdd:cd08176 106 IIVANP-----GADVRSLEGVAPTKNPAVP----IIAVPTTAGTGSEVTINYVITDTEKKRKFVCVDPHDIPTVAIVDPD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 646 FVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-DKVSREKMHNASTLAGMAFANAF 724
Cdd:cd08176 177 LMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPnNVEARENMALAQYIAGMAFSNVG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 725 LGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAK-DPQKhalfpkyeffradtdYADIAKFLGLKGN--TTEALVESL 801
Cdd:cd08176 257 LGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPaTGEK---------------YRDIARAMGVDTTgmSDEEAAEAA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88193926 802 AKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEIKDIIQ 862
Cdd:cd08176 322 VDAVKKLSKDVGIPQKLSELGVKEED----IEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
488-865 |
1.11e-102 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 323.33 E-value: 1.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 488 KVMIVCDPGMVEFGYTKTVENVLrqKTEQPQIKIFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMWMF 567
Cdd:cd14863 29 KVLLVTDKGLKKAGIVDKIIDLL--EEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAVL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 568 FEHPetsffGAKQKFLDIGKRTYKIGMPenatFICIPTTSGTGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQFV 647
Cdd:cd14863 107 LTNP-----GPIIDYALAGPPVPKPGIP----LIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLAILDPELT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 648 MSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-DKVSREKMHNASTLAGMAFANAFLG 726
Cdd:cd14863 178 VGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGdNLEARENMLLASNLAGIAFNNAGTH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 727 IAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAK-DPQKhalfpkyeffradtdYADIAKFLGLK--GNTTEALVESLAK 803
Cdd:cd14863 258 IGHAIAHALGALYHIPHGLACALALPVVLEFNAEaYPEK---------------VKKIAKALGVSfpGESDEELGEAVAD 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88193926 804 AVYELGQSVGIEMNLKSQGVSEEELnesiDRMAELAFEDQCTTANPKEALISEIKDIIQTSY 865
Cdd:cd14863 323 AIREFMKELGIPSLFEDYGIDKEDL----DKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
467-865 |
3.47e-101 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 319.48 E-value: 3.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSLTTMDK---IEKVMIVCDPGMVEFGYTKTVENVLRQKTEQPQIkiFSEVEPNPSTNTVYKGLEMMVD 543
Cdd:cd08194 1 PRTIIIGGGALEELGEEAAslgGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAV--FDDVVSEPTDEMVEEGLALYKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 544 FQPDTIIALGGGSAMDAAKAMWMFFEHPET-SFFGAKQKFLdigkrtyKIGMPenatFICIPTTSGTGSEVTPFAVITDS 622
Cdd:cd08194 79 GGCDFIVALGGGSPIDTAKAIAVLATNGGPiRDYMGPRKVD-------KPGLP----LIAIPTTAGTGSEVTRFTVITDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 623 ETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG- 701
Cdd:cd08194 148 ETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 702 DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKD-PQKhalfpkyeffradtdY 780
Cdd:cd08194 228 DLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGaPER---------------Y 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 781 ADIAKFLGL--KGNTTEALVESLAKAVYELGQSVGIEmNLKSQGVSEEELNESIDRMAELAFEDQCTTANPKEALISEIK 858
Cdd:cd08194 293 AEIARAMGIatEGDSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEEII 371
|
....*..
gi 88193926 859 DIIQTSY 865
Cdd:cd08194 372 ELYREAW 378
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
464-865 |
7.38e-99 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 313.32 E-value: 7.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLT---TMDKIEKVMIVCDPGMVEFGYTKTVENVLRQKTEQPQIkiFSEVEPNPSTNTVYKGLEM 540
Cdd:cd14865 3 FFNPTKIVSGAGALENLPaelARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGV--FDDVPPDSSVAVVNEAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 541 MVDFQPDTIIALGGGSAMDAAKAMWMFFEHpetsffGakqkfldiGKRTYKIGMPENAT-----FICIPTTSGTGSEVTP 615
Cdd:cd14865 81 AREAGADGIIAVGGGSVIDTAKGVNILLSE------G--------GDDLDDYGGANRLTrplkpLIAIPTTAGTGSEVTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 616 FAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLK 695
Cdd:cd14865 147 VAVIKDEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 696 SSVEKG-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhalfpkyeff 774
Cdd:cd14865 227 KAVKNGkDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLD-------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 775 RADTDYADIAKFLGL----KGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEELNEsidrMAELAFEDQCTTANPK 850
Cdd:cd14865 293 AAAERYAELALALAYgvtpAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEA----IAELALNDGAILFNPR 368
|
410
....*....|....*
gi 88193926 851 EALISEIKDIIQTSY 865
Cdd:cd14865 369 EVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
486-849 |
8.37e-98 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 310.55 E-value: 8.37e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 486 IEKVMIVCDPGMVEFGYTKTVENVLrqKTEQPQIKIFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMW 565
Cdd:cd08189 27 IKRVLIVTDKGLVKLGLLDPLLDAL--KKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIGGGSVIDCAKVIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 566 MFFEHPETSFfgAKQK-FLDIGKRTykigmpenATFICIPTTSGTGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDP 644
Cdd:cd08189 105 ARAANPKKSV--RKLKgLLKVRKKL--------PPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKLIPDAAVLDP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 645 QFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-DKVSREKMHNASTLAGMAFANA 723
Cdd:cd08189 175 ELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGsDLEARENMLLASYYAGLAFTRA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 724 FLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhalfpkyeffRADTDYADIAKFLGLKGNTTEALVESLA- 802
Cdd:cd08189 255 YVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGP--------------AAEKRLAELADAAGLGDSGESDSEKAEAf 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 88193926 803 -KAVYELGQSVGIEMNLksqgvseEELNES-IDRMAELAFEDqcttANP 849
Cdd:cd08189 321 iAAIRELNRRMGIPTTL-------EELKEEdIPEIAKRALKE----ANP 358
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
487-860 |
1.97e-95 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 304.08 E-value: 1.97e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 487 EKVMIVCDPGMVEFGYTKTVENVLRQktEQPQIKIFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMWM 566
Cdd:cd17814 27 RKVLVVTDPGVIKAGWVDEVLDSLEA--EGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 567 FFEHPetsffGAKQKFLDIGKRTYKigMPenaTFICIPTTSGTGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQF 646
Cdd:cd17814 105 VVSNG-----GHILDYEGVDKVRRP--LP---PLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDPET 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 647 VMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVE-KGDKVSREKMHNASTLAGMAFANAFL 725
Cdd:cd17814 175 LTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVAdPDDLEAREKMMLASLQAGLAFSNASL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 726 GIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNakdpqkhalfpkyeFFRADTDYADIAKFLGL--KGNTTEALVESLAK 803
Cdd:cd17814 255 GAVHAMAHSLGGLLDLPHGECNALLLPHVIRFN--------------FPAAPERYRKIAEAMGLdvDGLDDEEVAERLIE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 88193926 804 AVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEIKDI 860
Cdd:cd17814 321 AIRDLREDLGIPETLSELGVDEED----IPELAKRAMKDPCLVTNPRRPTREDIEEI 373
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
464-860 |
2.20e-91 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 292.95 E-value: 2.20e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTTM---DKIEKVMIVCDPGMVEFGYTKTVenvlRQKTEQPQIKIFSEVEPNPSTNTVYKGLEM 540
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIikeLGGKRGLLVTDPSFIKSGLAKRI----VESLKGRIVAVFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 541 MVDFQPDTIIALGGGSAMDAAKAMWMFFEHPET--SFFGAKQKFLDigkrtykigmpENATFICIPTTSGTGSEVTPFAV 618
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKTDGSieDYLEGKKKIPK-----------KGLPLIAIPTTAGTGSEVTPVAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 619 ITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSV 698
Cdd:cd08196 148 LTDKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 699 EKG-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhALFPKYEffrad 777
Cdd:cd08196 228 NNPnDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAE-----ALPGRLD----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 778 tdyaDIAKFLGLKGnttealVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEI 857
Cdd:cd08196 298 ----ELAKQLGFKD------AEELADKIEELKKRIGLRTRLSELGITEED----LEEIVEESFHPNRANNNPVEVTKEDL 363
|
...
gi 88193926 858 KDI 860
Cdd:cd08196 364 EKL 366
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
464-862 |
3.33e-88 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 285.16 E-value: 3.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTTMDKI--EKVMIVCDPG-MVEFGYTKTVENVLRQK---TEqpqikIFSEVEPNPSTNTVYKG 537
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEALRpgKKALIVTGKGsSKKTGLLDRVKKLLEKAgveVV-----VFDKVEPNPLTTTVMEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 538 LEMMVDFQPDTIIALGGGSAMDAAKAMWMFFEHPETSF---FGAKQKFLdIGKRTYKIgmpenatfICIPTTSGTGSEVT 614
Cdd:cd08185 76 AALAKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWdyiFGGTGKGP-PPEKALPI--------IAIPTTAGTGSEVD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 615 PFAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYL 694
Cdd:cd08185 147 PWAVITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 695 KSSVEKG-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYG-IPHGRANAILLPHIIRYNA-KDPQKhalfpky 771
Cdd:cd08185 227 PRAVKDGsDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIeKAPEK------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 772 effradtdYADIAKFlGLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFE--DQCTTANP 849
Cdd:cd08185 300 --------FAFVARA-EASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEED----IPWLAENAMEtmGGLFANNP 366
|
410
....*....|...
gi 88193926 850 KEALISEIKDIIQ 862
Cdd:cd08185 367 VELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
467-864 |
2.46e-86 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 279.78 E-value: 2.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSLTTM---DKIEKVMIVCDPGMVEFGYTKTVENVLRQKTEQPQIkiFSEVEPNPSTNTVYKGLEMMVD 543
Cdd:cd14861 3 PTRIRFGAGAIAELPEElkaLGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAV--FSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 544 FQPDTIIALGGGSAMDAAKAMWMFFEHPetsffGAKQKFLDIGKRTYKIGmPENATFICIPTTSGTGSEVTPFAVITDSE 623
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMATHP-----GPLWDYEDGEGGPAAIT-PAVPPLIAIPTTAGTGSEVGRAAVITDDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 624 TNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSV----MASdytrGLSLQAIKLTFEYLKSSVE 699
Cdd:cd14861 155 TGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPgfhpMAD----GIALEGLRLISEWLPRAVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 700 KG-DKVSREKMHNASTLAGMAFANAfLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAkdpqkHALFPKyeffradt 778
Cdd:cd14861 231 DGsDLEARGEMMMAALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFNR-----PAVEDK-------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 779 dYADIAKFLGLKGNTtealVESLAKAVYELGQSVGIEMNLKSQGVSEeelnESIDRMAELAFEDQCTTANPKEALISEIK 858
Cdd:cd14861 297 -LARLARALGLGLGG----FDDFIAWVEDLNERLGLPATLSELGVTE----DDLDELAELALADPCHATNPRPVTAEDYR 367
|
....*.
gi 88193926 859 DIIQTS 864
Cdd:cd14861 368 ALLREA 373
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
471-860 |
4.99e-86 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 279.32 E-value: 4.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 471 YFEENAIMSLTTMDK---IEKVMIVCDPGMVEFGYTKTVENVLrqktEQPQI--KIFSEVEPNPSTNTVYKGLEMMVDFQ 545
Cdd:TIGR02638 11 YFGAGAIEDIVDEVKrrgFKKALVVTDKDLIKFGVADKVTDLL----DEAGIayELFDEVKPNPTITVVKAGVAAFKASG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 546 PDTIIALGGGSAMDAAKAMWMFFEHPEtsfFGAKQKFLDIGKrTYKIGMPenatFICIPTTSGTGSEVTPFAVITDSETN 625
Cdd:TIGR02638 87 ADYLIAIGGGSPIDTAKAIGIISNNPE---FADVRSLEGVAP-TKKPGVP----IIAIPTTAGTAAEVTINYVITDEENK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 626 VKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-DKV 704
Cdd:TIGR02638 159 RKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGkDLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 705 SREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNA-KDPQKhalfpkyeffradtdYADI 783
Cdd:TIGR02638 239 AREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAeFTGEK---------------YREI 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88193926 784 AKFLGLK--GNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEIKDI 860
Cdd:TIGR02638 304 AKAMGVKteGMSDEEARDAAVEAVKTLSKRVGIPEGLSELGVKEED----IPALAEAALADVCTGGNPRETTVEEIEEL 378
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
471-865 |
6.42e-84 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 273.80 E-value: 6.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 471 YFEENAIMSLTTMDK---IEKVMIVCDPGMVEFGYTKTVENVLrqktEQPQI--KIFSEVEPNPSTNTVYKGLEMMVDFQ 545
Cdd:PRK10624 12 YFGRGAIGALTDEVKrrgFKKALIVTDKTLVKCGVVAKVTDVL----DAAGLayEIYDGVKPNPTIEVVKEGVEVFKASG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 546 PDTIIALGGGSAMDAAKAMWMFFEHPEtsFfgAKQKFLDIGKRTYKIGMPenatFICIPTTSGTGSEVTPFAVITDSETN 625
Cdd:PRK10624 88 ADYLIAIGGGSPQDTCKAIGIISNNPE--F--ADVRSLEGVAPTKKPSVP----IIAIPTTAGTAAEVTINYVITDEEKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 626 VKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEkGDKVS 705
Cdd:PRK10624 160 RKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVA-GDKEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 706 REKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAkdpqkhalfpkyEFfrADTDYADIAK 785
Cdd:PRK10624 239 GEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA------------DF--TGEKYRDIAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 786 FLGLK--GNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEIKDIIQT 863
Cdd:PRK10624 305 AMGVKveGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEED----IPALAQAAFDDVCTGGNPREATLEDIVELYKK 380
|
..
gi 88193926 864 SY 865
Cdd:PRK10624 381 AW 382
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
467-835 |
7.40e-81 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 265.24 E-value: 7.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSLTTM---DKIEKVMIVCDPGMVEFGYtktVENVLRQKTEQPQIKIFSEVEPNPSTNTVYKGLEMMVD 543
Cdd:cd08182 1 PVKIIFGPGALAELKDLlggLGARRVLLVTGPSAVRESG---AADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 544 FQPDTIIALGGGSAMDAAKAMWMFFEHPETSFFGAKQKfldigkrtyKIGMPENAT-FICIPTTSGTGSEVTPFAVITDS 622
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRTG---------EKAPEENALpLIAIPTTAGTGSEVTPFATIWDE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 623 ETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVE-KG 701
Cdd:cd08182 149 AEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLEnLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 702 DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKDPQKhalfpkyeffrADTDYA 781
Cdd:cd08182 229 NLEAREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDE-----------CDDDPR 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 88193926 782 DIAKFLGLKGNTTealvESLAKAVYELGQSVGIEMNLKSQGVSEEELNESIDRM 835
Cdd:cd08182 298 GREILLALGASDP----AEAAERLRALLESLGLPTRLSEYGVTAEDLEALAASV 347
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
464-865 |
1.49e-76 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 254.46 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTTMDKIEK--VMIVCDPGMVEFGYTKTVENVLRQKTEQPQIkiFSEVEPNPSTNTVYKGLEMM 541
Cdd:cd08191 1 LRSPSRLLFGPGARRALGRVAARLGsrVLIVTDPRLASTPLVAELLAALTAAGVAVEV--FDGGQPELPVSTVADAAAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 542 VDFQPDTIIALGGGSAMDAAKAMWMFFEHPET--SFFGakqkFLDIGKRTykigMPenatFICIPTTSGTGSEVTPFAVI 619
Cdd:cd08191 79 RAFDPDVVIGLGGGSNMDLAKVVALLLAHGGDprDYYG----EDRVPGPV----LP----LIAVPTTAGTGSEVTPVAVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 620 TDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRG---------------LSL 684
Cdd:cd08191 147 TDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPFPRLdpdpvyvgknpltdlLAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 685 QAIKLTFEYLKSSVEKGDKVS-REKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKDPQ 763
Cdd:cd08191 227 EAIRLIGRHLPRAVRDGDDLEaRSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 764 KHalfpkyeffradtdYADIAKFLGLK-GNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEELnesiDRMAELAFED 842
Cdd:cd08191 307 AE--------------LAEIARALGVTtAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADL----PGLAEKALSV 368
|
410 420
....*....|....*....|....
gi 88193926 843 Q-CTTANPKEALISEIKDIIQTSY 865
Cdd:cd08191 369 TrLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
467-862 |
1.53e-76 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 253.96 E-value: 1.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSLTTMDK--IEKVMIVCDPGMVEFGYTKTVENVLRQktEQPQIKIFSeVEPNPSTNTVYKGLEMMVDF 544
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAelGKRALLVTGRSSLRSGRLARLLEALEA--AGIEVALFS-VSGEPTVETVDAAVALAREA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 545 QPDTIIALGGGSAMDAAKAMWMFFEHPetsffGAKQKFLD-IGKRTYKIGMPenATFICIPTTSGTGSEVTPFAVITDSE 623
Cdd:cd08183 78 GCDVVIAIGGGSVIDAAKAIAALLTNE-----GSVLDYLEvVGKGRPLTEPP--LPFIAIPTTAGTGSEVTKNAVLSSPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 624 TNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-D 702
Cdd:cd08183 151 HGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGeD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 703 KVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhALFPKYEFFRADTDYAD 782
Cdd:cd08183 231 LEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLR-----ALREREPDSPALARYRE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 783 IAKFLGLKGnttEALVESLAKAVYELGQSVGIEmNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEIKDIIQ 862
Cdd:cd08183 306 LAGILTGDP---DAAAEDGVEWLEELCEELGIP-RLSEYGLTEED----FPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
485-865 |
6.93e-75 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 250.54 E-value: 6.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 485 KIEKVMIVCDPGMVEFGYTKTVENVLRQktEQPQIKIFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAM 564
Cdd:cd08190 22 GAKKVLVVTDPGLAKLGLVERVLESLEK--AGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 565 WMFFEHPetsffgakQKFLD-----IGKrtykiGMPEN---ATFICIPTTSGTGSEVTPFAVITDSETNVKYPLADFALT 636
Cdd:cd08190 100 NLYATHP--------GDFLDyvnapIGK-----GKPVPgplKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 637 PDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYvsvMASDY---------------------TRGLSLQAIKLTFEYLK 695
Cdd:cd08190 167 PTLAIVDPLLTLTLPPRVTASSGFDVLCHALESY---TARPYnarprpanpderpayqgsnpiSDVWAEKAIELIGKYLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 696 SSVEKGDKV-SREKMHNASTLAGMAFANAFLGIAHSIAHKIGG-------------EYGIPHGRANAILLPHIIRYNAK- 760
Cdd:cd08190 244 RAVNDGDDLeARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppgypvdHPHVPHGLSVALTAPAVFRFTAPa 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 761 DPQKHalfpkyeffradtdyADIAKFLG--LKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAEL 838
Cdd:cd08190 324 CPERH---------------LEAAELLGadTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDD----IPALVEG 384
|
410 420
....*....|....*....|....*...
gi 88193926 839 AFEDQCTTA-NPKEALISEIKDIIQTSY 865
Cdd:cd08190 385 TLPQQRLLKlNPRPVTEEDLEEIFEDAL 412
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
464-862 |
1.73e-71 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 239.41 E-value: 1.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTT-MDKI-EKVMIVCdpGMV---EFGYTKTVENVLrqKTEQPQIKIFSEVEPNPSTNTVYKGL 538
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADeLAALgKKALIVT--GKHsakKNGSLDDVTEAL--EENGIEYFIFDEVEENPSIETVEKGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 539 EMMVDFQPDTIIALGGGSAMDAAKAMWMFFEHP----ETSFFGAKQKFLDIgkrtykigmpenatfICIPTTSGTGSEVT 614
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIALLAANKdgdeDLFQNGKYNPPLPI---------------VAIPTTAGTGSEVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 615 PFAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYL 694
Cdd:cd08181 142 PYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 695 KS-SVEKGDKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKDpqkhalfpkyef 773
Cdd:cd08181 222 PNlLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQ------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 774 frADTDYADIAKFLGLKgnTTEALVESLAKAVYELGQsvgiemnlksqgVSEEElnesIDRMAELAFEDQCTTANPKEAL 853
Cdd:cd08181 290 --EPEKVDKILKLLGFG--SIEEFQKFLNRLLGKKEE------------LSEEE----LEKYADEAMKAKNKKNTPGNVT 349
|
....*....
gi 88193926 854 ISEIKDIIQ 862
Cdd:cd08181 350 KEDILRIYR 358
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
26-456 |
1.14e-70 |
|
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: 238.66 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 26 DKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGR-------------GIYEDKAIKNLYASEYIWNSi 92
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAyirslianwiammGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 93 kDNKTVGIIGEDKekGLTYV-AEPIGVICGVTPTTNPTSTtIFKAMIAIKTGNPIIFAFHPSAqESSKRAAEVVLEAAMK 171
Cdd:cd07077 80 -VGHIQDVLLPDN--GETYVrAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSA-PFTNRALALLFQAADA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 172 AGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATGGSGMVKSAY--STGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGS 249
Cdd:cd07077 155 AHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVkhSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 250 KTFDNgMICASEQVVVIDKEIYKDVTNEFKAHQAYfvkkdelqrlenaimneqktgikpdivgksaveiaelAGIPVPEN 329
Cdd:cd07077 235 KFFDQ-NACASEQNLYVVDDVLDPLYEEFKLKLVV-------------------------------------EGLKVPQE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 330 TKLIIAEISgvGSDYPLSREKLSPVLALVKAQSTKQAFQICEDTLHFGGLGHTAVIHTEDETLQKDFGLRMKACRVLVNT 409
Cdd:cd07077 277 TKPLSKETT--PSFDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNE 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 88193926 410 PSAVGGiGDMYN-ELIPSLTLGCGSYGRNsishNVSATDLLNIKTIAK 456
Cdd:cd07077 355 SSKKGR-GAFAGkGVERIVTSGMNNIFGA----GVGHDALRPLKRLVR 397
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
464-865 |
9.87e-68 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 230.09 E-value: 9.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTTMDK---IEKVMIVCDPGMVEFGYTKTVENVLRqkTEQPQIKIFSEVEPNPSTNTVYKGLEM 540
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELLRelgARRVLLVTDPGLVKAGLADPALAALE--AAGIAVTVFDDVVADPPEAVVEAAVEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 541 MVDFQPDTIIALGGGSAMDAAKAmwmffehpeTSFF-GAKQKFLDIgkrtYKIGmpeNATF-----ICIPTTSGTGSEVT 614
Cdd:cd08193 79 AREAGADGVIGFGGGSSMDVAKL---------VALLaGSDQPLDDI----YGVG---KATGprlplILVPTTAGTGSEVT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 615 PFAVITDSETnVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASD-YTRGLSLQAIKLTFEY 693
Cdd:cd08193 143 PISIVTTGET-EKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNpISDALAREALRLLGAN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 694 LKSSVEKG-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhalfpkye 772
Cdd:cd08193 222 LRRAVEDGsDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLP------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 773 ffRADTDYADIAKFL--GLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEeelnESIDRMAELAFEDQ-CTTANP 849
Cdd:cd08193 290 --AAEALYAELARALlpGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTE----EDLPMLAEDAMKQTrLLVNNP 363
|
410
....*....|....*.
gi 88193926 850 KEALISEIKDIIQTSY 865
Cdd:cd08193 364 REVTEEDALAIYQAAL 379
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
21-417 |
5.24e-66 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 228.25 E-value: 5.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 21 IDALADKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGRGIYEDKAIKNLYASEYIwNSIKDNKTVGI 100
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAEKT-PGVEDLTTEAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 101 IGEDkekGLTYVA-EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDII 179
Cdd:PRK15398 117 TGDN---GLTLIEyAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGGPENLV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 180 QWIEVPSIEATKQLMNHKGIALVLATGGSGMVKSAYSTGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICA 259
Cdd:PRK15398 194 VTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 260 SEQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQRLENAIMnEQKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIAEisg 339
Cdd:PRK15398 274 AEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVL-KNGGTVNKKWVGKDAAKILEAAGINVPKDTRLLIVE--- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 340 VGSDYPL-SREKLSPVLALVKAQSTKQAFQICEDTLHfgGLGHTAVIHTED-ETLQKdFGLRMKACRVLVNTPSAVG-GI 416
Cdd:PRK15398 350 TDANHPFvVTELMMPVLPVVRVKDVDEAIALAVKLEH--GNRHTAIMHSRNvDNLNK-MARAIQTSIFVKNGPSYAGlGL 426
|
.
gi 88193926 417 G 417
Cdd:PRK15398 427 G 427
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
29-418 |
8.49e-64 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 220.96 E-value: 8.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 29 KKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGRGIYEDKAIKNLYASEYIwNSIKDNKTVGIIGEDkekG 108
Cdd:cd07121 14 KAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEKT-PGTEDLTTTAWSGDN---G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 109 LT-YVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSI 187
Cdd:cd07121 90 LTlVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDNLVVTVEEPTI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 188 EATKQLMNHKGIALVLATGGSGMVKSAYSTGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVID 267
Cdd:cd07121 170 ETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 268 KEIYKDVTNEFKAHQAYFVK-KDELQRLENAIMNEQKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIAEisgVGSDYPL 346
Cdd:cd07121 250 DSVADYLIAAMQRNGAYVLNdEQAEQLLEVVLLTNKGATPNKKWVGKDASKILKAAGIEVPADIRLIIVE---TDKDHPF 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88193926 347 -SREKLSPVLALVKAQSTKQAFQICEDTLHfgGLGHTAVIHTED-ETLQKdFGLRMKACRVLVNTPSAVG-GIGD 418
Cdd:cd07121 327 vVEEQMMPILPVVRVKNFDEAIELAVELEH--GNRHTAIIHSKNvENLTK-MARAMQTTIFVKNGPSYAGlGVGG 398
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
488-860 |
3.87e-62 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 214.82 E-value: 3.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 488 KVMIVCDPGMVEFGYTKTVENVLRQKTEQPQIkiFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMWMF 567
Cdd:PRK09860 33 RTLIVTDNMLTKLGMAGDVQKALEERNIFSVI--YDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 568 FEHpetsffGAKQKFLDIGKRTYKIGMPenatFICIPTTSGTGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQFV 647
Cdd:PRK09860 111 AAN------GGDIRDYEGVDRSAKPQLP----MIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 648 MSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKGDKV-SREKMHNASTLAGMAFANAFLG 726
Cdd:PRK09860 181 IGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAkAREAMAYAQFLAGMAFNNASLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 727 IAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKdpqkhalfpkyeffRADTDYADIAKFLG--LKGNTTEALVESLAKA 804
Cdd:PRK09860 261 YVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK--------------VAAARLRDCAAAMGvnVTGKNDAEGAEACINA 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 88193926 805 VYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQCTTANPKEALISEIKDI 860
Cdd:PRK09860 327 IRELAKKVDIPAGLRDLNVKEED----FAVLATNALKDACGFTNPIQATHEEIVAI 378
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
529-860 |
1.05e-51 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 186.39 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 529 PSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMWMFFEHPETSffgakqkfldIGKRTYKIGMPENATFICIPTTSG 608
Cdd:PRK15454 90 PCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDST----------LAEMSETSVLQPRLPLIAIPTTAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 609 TGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIK 688
Cdd:PRK15454 160 TGSETTNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 689 LTFEYLKSSVEKG-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAKDPQKHal 767
Cdd:PRK15454 240 MIGKSLPKAVGYGhDLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRER-- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 768 fpkyeffradtdYADIAKFL-GLKGNTTEALveslaKAVYELGQSVGIEMNLKSQGVSEEELNEsidrMAELAFEDQCTT 846
Cdd:PRK15454 318 ------------FSQIGRALrTKKSDDRDAI-----NAVSELIAEVGIGKRLGDVGATSAHYGA----WAQAALEDICLR 376
|
330
....*....|....
gi 88193926 847 ANPKEALISEIKDI 860
Cdd:PRK15454 377 SNPRTASLEQIVGL 390
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
463-862 |
6.49e-49 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 178.01 E-value: 6.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 463 IFKVPAQIYFEENAIMSLTTM--DKIEKVMIVCDPG-MVEFGYTKTVENVLrqKTEQPQIKIFSEVEPNPSTNTVYKGLE 539
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEikKYGKKVLLVYGGGsIKKNGLYDRVVASL--KEAGIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 540 MMVDFQPDTIIALGGGSAMDAAKAM----------WMFFEHPETsffgakqkfldigkrtykigmPENAT-FICIPTTSG 608
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIaagakydgdvWDFFTGKAP---------------------PEKALpVGTVLTLAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 609 TGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVS-VMASDYTRGLSLQAI 687
Cdd:cd08187 140 TGSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRLAEGLL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 688 KLTFEYLKSSVEKGDKVS-REKMHNASTLAgmafANAFLGI-------AHSIAHKIGGEYGIPHGRANAILLPHIIRYNA 759
Cdd:cd08187 220 RTVIENGPKALKDPDDYEaRANLMWAATLA----LNGLLGAgrggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 760 K-DPQKhalfpkyeffradtdYADIAK--FLGLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMA 836
Cdd:cd08187 296 KkKPER---------------FAQFARrvFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDEED----IEEMA 356
|
410 420
....*....|....*....|....*.
gi 88193926 837 ELAFEDQCTTANPKEALISEIKDIIQ 862
Cdd:cd08187 357 EKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
533-849 |
2.58e-46 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 170.51 E-value: 2.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 533 TVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMWMFFEHPETSFFGAKQkfLDIGKRTYKIGMPENATFICIPTT-SGtgS 611
Cdd:cd08192 67 DVLEAARAVREAGADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDA--LEDGKRIDPNVTGPTLPHIAIPTTlSG--A 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 612 EVTPFAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTF 691
Cdd:cd08192 143 EFTAGAGATDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLF 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 692 EYLKSSVEKGDKV-SREKMHNASTLAGMAFANAF-LGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNA-KDPQKHALf 768
Cdd:cd08192 223 EGLPRSKADPEDLeARLKCQLAAWLSLFGLGSGVpMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNApVNAERQRL- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 769 pkyeffradtdyadIAKFLGLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEELnesiDRMAELAFEDQCTTAN 848
Cdd:cd08192 302 --------------IARALGLVTGGLGREAADAADAIDALIRELGLPRTLRDVGVGRDQL----EKIAENALTDVWCRTN 363
|
.
gi 88193926 849 P 849
Cdd:cd08192 364 P 364
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
470-841 |
1.14e-45 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 168.60 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 470 IYFEENAIMSLTTMDK---IEKVMIVCDPG-MVEFGYTKTVENVLRQKteqpQIK--IFSEVEPNPSTNTVYKGLEMMVD 543
Cdd:cd08186 4 LYFGVGAIAKIKDILKdlgIDKVIIVTGRSsYKKSGAWDDVEKALEEN----GIEyvVYDKVTPNPTVDQADEAAKLARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 544 FQPDTIIALGGGSAMDAAKAMWMFFEHPetsffGAKQKFLDIGKRTYKIGMPenatFICIPTTSGTGSEVTPFAVITDSE 623
Cdd:cd08186 80 FGADAVIAIGGGSPIDTAKSVAVLLAYG-----GKTARDLYGFRFAPERALP----LVAINLTHGTGSEVDRFAVATIPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 624 TNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKGDK 703
Cdd:cd08186 151 KGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 704 VS-REKMHNASTLAGMAFANAFLGIAHSIAHKIGG-EYGIPHGRANAILLPHIIRYnakdpqKHALFPKYeffradtdYA 781
Cdd:cd08186 231 LEaRYWLLYASMIAGIAIDNGLLHLTHALEHPLSGlKPELPHGLGLALLGPAVVKY------IYKAVPET--------LA 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88193926 782 DIAKFL--GLKGNTTEAlvESLAKAVYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFE 841
Cdd:cd08186 297 DILRPIvpGLKGTPDEA--EKAARGVEEFLFSVGFTEKLSDYGFTEDD----VDRLVELAFT 352
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
521-863 |
1.17e-44 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 165.87 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 521 IFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMwmffehpeTSFFGAKQKFLDIGKRTYKIGMPENATF 600
Cdd:cd14866 59 VFDGVRPHSPLETVEAAAEALREADADAVVAVGGGSAIVTARAA--------SILLAEDRDVRELCTRRAEDGLMVSPRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 601 -------ICIPTTSGTGSEVTPFAViTDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSV 673
Cdd:cd14866 131 dapklpiFVVPTTPTTADVKAGSAV-TDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 674 MASDYTRGLSLQAIKLTFEYLKSSVEKGDKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPH 753
Cdd:cd14866 210 HADPLADATLMHALRLLADGLPRLADDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 754 IIRYNAKdpqkhalfpkyeffRADTDYADIAKFLGLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEEELnesiD 833
Cdd:cd14866 290 VLRFNAP--------------ATDGRLDRLAEALGVADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDL----P 351
|
330 340 350
....*....|....*....|....*....|.
gi 88193926 834 RMAELAFEDQCTTANPK-EALISEIKDIIQT 863
Cdd:cd14866 352 AIAEAAMDDWFMDNNPRpVPTAEELEALLEA 382
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
463-841 |
4.22e-42 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 158.31 E-value: 4.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 463 IFKVPAQIYFEENAIMSLTTMDK--IEKVMIVCDPGMVE-FGYTKTVENVLrqKTEQPQIKIFSEVEPNPSTNTVYKGLE 539
Cdd:COG1979 5 TFYNPTKIIFGKGQIAKLGEEIPkyGKKVLLVYGGGSIKkNGLYDQVKAAL--KEAGIEVVEFGGVEPNPRLETVRKGVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 540 MMVDFQPDTIIALGGGSAMDAAK--AMWMFFEHPETSFFgakqkfldIGKRTYKIGMPenatFICIPTTSGTGSEVTPFA 617
Cdd:COG1979 83 LCKEEGIDFILAVGGGSVIDGAKaiAAGAKYDGDPWDIL--------TGKAPVEKALP----LGTVLTLPATGSEMNSGS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 618 VITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSvmasdYTRGLSLQ-----AIkltfe 692
Cdd:COG1979 151 VITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFT-----YPVDAPLQdrfaeGL----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 693 yLKSSVEKGDKVsREKMHN---------ASTLAgmafANAFLGI-------AHSIAHKIGGEYGIPHGRANAILLPHIIR 756
Cdd:COG1979 221 -LRTLIEEGPKA-LKDPEDydaranlmwAATLA----LNGLIGAgvpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 757 YNAKDpqkhalfpkyeffradtdyaDIAKFL-------GLKGNTTEALVESLAKAVYELGQSVGIEMNLKSQGVSEeeln 829
Cdd:COG1979 295 YVLEE--------------------KPEKFAqyaervwGITEGDDEERALEGIEATEEFFESLGLPTRLSEYGIDE---- 350
|
410
....*....|..
gi 88193926 830 ESIDRMAELAFE 841
Cdd:COG1979 351 EDIEEMAEKATA 362
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
464-865 |
7.46e-42 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 157.46 E-value: 7.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 464 FKVPAQIYFEENAIMSLTTMDKI--EKVMIVCDPGMVEFGYTKTVENVLRQKteQPQIKIFSEVEPNPSTNTVYKGLEMM 541
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEygSRFLLITDPVLKESGLADKIVSSLEKA--GISVIVFDEIPASATSDTIDEAAELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 542 VDFQPDTIIALGGGSAMDAAKAMWMFFEHPETSF-FGAKQKfldigkrtykigmPENAT--FICIPTTSGTGSEVTPFAV 618
Cdd:cd14864 79 RKAGADGIIAVGGGKVLDTAKAVAILANNDGGAYdFLEGAK-------------PKKKPlpLIAVPTTPRSGFEFSDRFP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 619 ITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSV 698
Cdd:cd14864 146 VVDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 699 EKG-DKVSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAK-DPQKhalfpkyeffra 776
Cdd:cd14864 226 ADPkNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATsAPDK------------ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 777 dtdYADIAKFLGlkGNTTEALVESLAKAVYELGQSVGIEMNLKSQgVSEEELNESIDRMAELAFEDQCTTANPKEALISE 856
Cdd:cd14864 294 ---YAKIARALG--EDVEGASPEEAAIAAVEGVRRLIAQLNLPTR-LKDLDLASSLEQLAAIAEDAPKLNGLPRSMSSDD 367
|
....*....
gi 88193926 857 IKDIIQTSY 865
Cdd:cd14864 368 IFDILKAAF 376
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
529-762 |
4.91e-37 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 143.13 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 529 PSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKamwmffehpetsFFGAKQ--KFLDIGKRtyKIGMPENATFICIPTT 606
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK------------LLALKGisPVLDLFDG--KIPLIKEKELIIVPTT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 607 SGTGSEVTPFAVITDSETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQA 686
Cdd:cd14860 128 CGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 687 IKLTFEYLKSSVEKGDKVSREKMHN---ASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAILLPHIIR-YNAKDP 762
Cdd:cd14860 208 IEMILEGYQEIAEKGEEARFPLLGDfliASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKnYQEKNP 287
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
486-849 |
2.76e-34 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 134.17 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 486 IEKVMIVCDPGMVEFGytKTVENVLRQKteqpQIKIFSEVEPNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAmw 565
Cdd:cd08177 23 ARRALVLSTPRQRALA--ERVAALLGDR----VAGVFDGAVMHVPVEVAERALAAAREAGADGLVAIGGGSAIGLAKA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 566 mffehpetsffgakqkfldIGKRTykiGMPenatFICIPTTSgTGSEVTPFAVITdsETNVKYPLADFALTPDVAIIDPQ 645
Cdd:cd08177 95 -------------------IALRT---GLP----IVAVPTTY-AGSEMTPIWGET--EDGVKTTGRDPRVLPRTVIYDPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 646 FVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFEYLKSSVEKG-DKVSREKMHNASTLAGMAFANAF 724
Cdd:cd08177 146 LTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPsDLEARSDALYGAWLAGVVLGSVG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 725 LGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYNAkDPQKHALfpkyeffradtdyADIAKFLGlkgnttealVESLAKA 804
Cdd:cd08177 226 MGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNA-PAAPDAM-------------ARLARALG---------GGDAAGG 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 88193926 805 VYELGQSVGIEMNLKSQGVSEEElnesIDRMAELAFEDQctTANP 849
Cdd:cd08177 283 LYDLARRLGAPTSLRDLGMPEDD----IDRAADLALANP--YPNP 321
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
26-415 |
5.71e-33 |
|
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: 131.20 E-value: 5.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 26 DKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETG--RGIYEDKAIKNLYASEYIWNSIKDNKTVGIIGE 103
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 104 DKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEaamkAGAPKDIIQWIE 183
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQE----AGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 184 VPSIEATKQLMNHKGIALVLATGGSGMVKSAY----STGKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICA 259
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMkaaaENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 260 SEQVVVIDKEIYkdvtnefkahqayfvkkDELqrlenaimneqktgikpdivgksaveIAELAGIPVPENTKLIIA--EI 337
Cdd:cd06534 237 AASRLLVHESIY-----------------DEF--------------------------VEKLVTVLVDVDPDMPIAqeEI 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88193926 338 SGvgsdyplsreklsPVLALVKAQSTKQAFQICEDTlhfgGLGHTAVIHTEDETLQKDFGLRMKACRVLVNTPSAVGG 415
Cdd:cd06534 274 FG-------------PVLPVIRFKDEEEAIALANDT----EYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG 334
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
467-801 |
4.08e-32 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 126.32 E-value: 4.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSLTTM--DKIEKVMIVCDPGMVEFgytkTVENVLRQKTEQPQIKIFSEVEPNPSTNTVYKGLEMMVDF 544
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIkrRGFDRALVVSDEGVVKG----VGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 545 QPDTIIALGGGSAMDAAKAMwmffehpetsffgakqkfldigkrtyKIGMPENATFICIPTTSGTGSEVTPFAVITDSET 624
Cdd:cd07766 77 EADAVIAVGGGSTLDTAKAV--------------------------AALLNRGIPFIIVPTTASTDSEVSPKSVITDKGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 625 NVKYplADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMEsyvsvmasdytrglslqaikltfeylkssvekgdkv 704
Cdd:cd07766 131 KNKQ--VGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 705 sREKMHNASTLAGMAFANA-FLGIAHSIAHKIGGEYGIPHGRANAILLPHIIRYN--AKDPQKHALFPKYEFFRaDTDYA 781
Cdd:cd07766 173 -LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVAndMNPEPEAAIEAVFKFLE-DLGLP 250
|
330 340
....*....|....*....|
gi 88193926 782 DIAKFLGLKGNTTEALVESL 801
Cdd:cd07766 251 THLADLGVSKEDIPKLAEKA 270
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
521-749 |
2.09e-24 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 105.43 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 521 IFSEVEPNPST---NTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAMWMFFEHPETSffgAKQKFLDIGKR--TYKIGmp 595
Cdd:cd08184 55 IFVDTTDEPKTdqiDALRAQIRAENDKLPAAVVGIGGGSTMDIAKAVSNMLTNPGSA---ADYQGWDLVKNpgIYKIG-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 596 enatficIPTTSGTGSEVTPFAVITDSEtnVKYPL-ADFALtPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVM 674
Cdd:cd08184 130 -------VPTLSGTGAEASRTAVLTGPE--KKLGInSDYTV-FDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTY 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88193926 675 ASDYTRGLSLQAIKLTFEYLKSSVEKGDKvSREKMHNASTLAGMAFANAFLGIAHSIAHKIGGEYGIPHGRANAI 749
Cdd:cd08184 200 RNAFGDAYAEKALELCRDVFLSDDMMSPE-NREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCI 273
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-415 |
6.85e-15 |
|
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: 78.02 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 60 VLAKLAHEETGRGIYE-----DKAIKNL-YASEYIwnsIKDNKTVGIIGEDKEKGLTyVAEPIGVICGVTPTTNPTSTTI 133
Cdd:cd07078 39 ELAALETLETGKPIEEalgevARAADTFrYYAGLA---RRLHGEVIPSPDPGELAIV-RREPLGVVGAITPWNFPLLLAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 134 FKAMIAIKTGNPIIfaFHPSaqESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATG----GSG 209
Cdd:cd07078 115 WKLAPALAAGNTVV--LKPS--ELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGstavGKA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 210 MVKSAYSTGKP---ALGvgpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKDVTNEFKAHQAYFV 286
Cdd:cd07078 191 IMRAAAENLKRvtlELG---GKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 287 KKDELQR--LENAIMNE-QKTGIkpdivgKSAVEIAE------LAGIPVPENTKL-----IIaeISGVGSDYPLSREKL- 351
Cdd:cd07078 268 VGNPLDPdtDMGPLISAaQLDRV------LAYIEDAKaegaklLCGGKRLEGGKGyfvppTV--LTDVDPDMPIAQEEIf 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88193926 352 SPVLALVKAQSTKQAFQICEDTlHFGGlghTAVIHTEDETLQKDFGLRMKACRVLVNTPSAVGG 415
Cdd:cd07078 340 GPVLPVIPFKDEEEAIELANDT-EYGL---AAGVFTRDLERALRVAERLEAGTVWINDYSVGAE 399
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
467-771 |
4.27e-14 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 75.22 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 467 PAQIYFEENAIMSLTtmDKI---EKVMIVCDPGMV-EFGYTKTVENVLRQKTeqpqIKIFSEVEPNPSTNTVYKGLEMMV 542
Cdd:PRK15138 9 PTRILFGKGAIAGLR--EQIpadARVLITYGGGSVkKTGVLDQVLDALKGMD----VLEFGGIEPNPTYETLMKAVKLVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 543 DFQPDTIIALGGGSAMDAAKAMWMFFEHPETSffgAKQKFLDIGKRTYKIGMPENatfiCIPTTSGTGSEVTPFAVITDS 622
Cdd:PRK15138 83 EEKITFLLAVGGGSVLDGTKFIAAAANYPENI---DPWHILETGGKEIKSAIPMG----SVLTLPATGSESNAGAVISRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 623 ETNVKYPLADFALTPDVAIIDPQFVMSVPKSVTADTGMDVLTHAMESYVSVMASDYTRGLSLQAIKLTFeylkssVEKGD 702
Cdd:PRK15138 156 TTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTL------IEEGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 703 KVSREKMH-----NASTLAGMAFaNAFLGIA-------HSIAHKIGGEYGIPHGRANAILLPHIirYNAKDPQKHALFPK 770
Cdd:PRK15138 230 KALKEPENydvraNVMWAATQAL-NGLIGAGvpqdwatHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQ 306
|
.
gi 88193926 771 Y 771
Cdd:PRK15138 307 Y 307
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
10-418 |
8.47e-14 |
|
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: 74.49 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 10 RGSKEQevaimIDALADKGKKALEALSKKSQEEIDHIVHQMsLAAVDQHM-VLAKLAHEETGRGIYE-----DKAIKNL- 82
Cdd:pfam00171 25 AATAED-----VDAAIAAARAAFPAWRKTPAAERAAILRKA-ADLLEERKdELAELETLENGKPLAEargevDRAIDVLr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 83 YASEYIwnsikdNKTVG-IIGEDKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFafHPSaqESSKRA 161
Cdd:pfam00171 99 YYAGLA------RRLDGeTLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL--KPS--ELTPLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 162 AEVVLEAAMKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATG----GSGMVKSAYSTGKPA---LGvgpGNVPSYIE 234
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGstavGRHIAEAAAQNLKRVtleLG---GKNPLIVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 235 KTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKDVTNEFKAHQAYF---------------VKKDELQRLENAIM 299
Cdd:pfam00171 246 EDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkvgdpldpdtdmgplISKAQLERVLKYVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 300 NEQKTGIKPdivgksaveiaELAGIPVPEN----TKLIIAeisGVGSDYPLSREKL-SPVLALVKAQSTKQAFQICEDTl 374
Cdd:pfam00171 326 DAKEEGAKL-----------LTGGEAGLDNgyfvEPTVLA---NVTPDMRIAQEEIfGPVLSVIRFKDEEEAIEIANDT- 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 88193926 375 hfgGLGHTAVIHTEDETLQKDFGLRMKACRVLVNTPSAV-------GGIGD 418
Cdd:pfam00171 391 ---EYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGdadglpfGGFKQ 438
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
102-454 |
2.58e-13 |
|
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: 73.24 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 102 GEDKEKGLTyVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQE--SSKRAAEVVLEaamkAGAPKDII 179
Cdd:cd07094 111 GSDNRLAWT-IREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVV--LKPASKTplSALELAKILVE----AGVPEGVL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 180 QWIEVPSIEATKQLMNHKGIALVLATGGS--GMVKSAYSTGKP-ALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGM 256
Cdd:cd07094 184 QVVTGEREVLGDAFAADERVAMLSFTGSAavGEALRANAGGKRiALELG-GNAPVIVDRDADLDAAIEALAKGGFYHAGQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 257 ICASEQVVVIDKEIYkdvtNEFKAHqayFVKKDELQRLENAImnEQKTGIKPDI-----------VGKSAVEIAELAGIP 325
Cdd:cd07094 263 VCISVQRIYVHEELY----DEFIEA---FVAAVKKLKVGDPL--DEDTDVGPLIseeaaerverwVEEAVEAGARLLCGG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 326 VPENTKLIIAEISGVGSDYPLSREK-LSPVLALVKAQSTKQAFQICEDTLHfgglGHTAVIHTEDETLQKDFGLRMKACR 404
Cdd:cd07094 334 ERDGALFKPTVLEDVPRDTKLSTEEtFGPVVPIIRYDDFEEAIRIANSTDY----GLQAGIFTRDLNVAFKAAEKLEVGG 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 88193926 405 VLVNTPSAvggigdMYNELIPSLTLGCGSYGRNSISHnvSATDLLNIKTI 454
Cdd:cd07094 410 VMVNDSSA------FRTDWMPFGGVKESGVGREGVPY--AMEEMTEEKTV 451
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
135-418 |
3.20e-12 |
|
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: 69.77 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 135 KAMIAIKTGNPIIFafHPSaqESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATG----GSGM 210
Cdd:COG1012 161 KLAPALAAGNTVVL--KPA--EQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGstavGRRI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 211 VKSAYSTGKPA---LGvgpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKDVTNEFKAHqayfVK 287
Cdd:COG1012 237 AAAAAENLKRVtleLG---GKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAA----AK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 288 K----DELQrlENAIMN-----EQKTGIkpdivgKSAVEIAE------LAGIPVPENTK------LIIAeisGVGSDYPL 346
Cdd:COG1012 310 AlkvgDPLD--PGTDMGpliseAQLERV------LAYIEDAVaegaelLTGGRRPDGEGgyfvepTVLA---DVTPDMRI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 347 SREKL-SPVLALVKAQSTKQAFQICEDTLHfgGLghTAVIHTEDETLQKDFGLRMKACRVLVNTPSAV-------GGIGD 418
Cdd:COG1012 379 AREEIfGPVLSVIPFDDEEEAIALANDTEY--GL--AASVFTRDLARARRVARRLEAGMVWINDGTTGavpqapfGGVKQ 454
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-408 |
3.00e-09 |
|
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: 60.05 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 26 DKGKKALEALSKKSQEEIDHIVHQMSLAAVDQHMVLAKLAHEETGRGIYE-----DKAIKNL-YASEYIwnSIKDNKTVG 99
Cdd:cd07145 28 EVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQsrvevERTIRLFkLAAEEA--KVLRGETIP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 100 IIG-EDKEKGLTY-VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQesskrAAEVVLEAA---MKAGA 174
Cdd:cd07145 106 VDAyEYNERRIAFtVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVV--VKPSSN-----TPLTAIELAkilEEAGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 175 PKDIIQWIEVPSIEATKQLMNHKGIALVLATG----GSGMVKSAYSTGKP-ALGVGpGNVPSYIEKTAHIKRAVNDIIGS 249
Cdd:cd07145 179 PPGVINVVTGYGSEVGDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKvALELG-GSDPMIVLKDADLERAVSIAVRG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 250 KtFDN-GMICASEQVVVIDKEIYkdvtNEFKAHqayFVKKDELQRLENAImnEQKTGIKPDIVGKSAVEIAELAGIPVPE 328
Cdd:cd07145 258 R-FENaGQVCNAVKRILVEEEVY----DKFLKL---LVEKVKKLKVGDPL--DESTDLGPLISPEAVERMENLVNDAVEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 329 NTKLIIAEISGVGSDYP-------------LSREKLSPVLALVKAQSTKQAFQICEDTLHfgglGHTAVIHTEDETLQKD 395
Cdd:cd07145 328 GGKILYGGKRDEGSFFPptvlendtpdmivMKEEVFGPVLPIAKVKDDEEAVEIANSTEY----GLQASVFTNDINRALK 403
|
410
....*....|...
gi 88193926 396 FGLRMKACRVLVN 408
Cdd:cd07145 404 VARELEAGGVVIN 416
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
462-744 |
1.31e-08 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 57.87 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 462 QIFKVPAQIYFEENAIMSLTTMDKI--EKVMIVCDPGMvefgyTKTVENVLRQKTEQPQIKI-FSEVEPNPSTNTVYKGL 538
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADlgKRALIITGPTA-----LKAAGDRLEESLEDAGIEVeVEVFGGECSEEEIERLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 539 EMMVDFQPDTIIALGGGSAMDAAKAMwmffehpetsffgAkqkfldigkrtYKIGMPenatFICIPTTSGTGSEVTPFAV 618
Cdd:COG0371 76 EEAKEQGADVIIGVGGGKALDTAKAV-------------A-----------YRLGLP----VVSVPTIASTDAPASPLSV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 619 ITDSETNVKYPLAdFALTPDVAIIDPQFVMSVPKSVTAdTGM-DVLTHAMESYVSVMASDYTRG-----LSLQAIKLTFE 692
Cdd:COG0371 128 IYTEDGAFDGYSF-LAKNPDLVLVDTDIIAKAPVRLLA-AGIgDALAKWYEARDWSLAHRDLAGeyyteAAVALARLCAE 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88193926 693 YLkssVEKGDKVSREKMHNAST------------LAGMAFANAF----LGIAHSIAH---KIGGEYGIPHG 744
Cdd:COG0371 206 TL---LEYGEAAIKAVEAGVVTpalervveanllLSGLAMGIGSsrpgSGAAHAIHNgltALPETHHALHG 273
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
114-281 |
1.38e-08 |
|
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: 58.05 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 114 EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSaqESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATKQL 193
Cdd:cd07088 132 VPIGVVAGILPWNFPFFLIARKLAPALVTGNTIV--IKPS--EETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDAL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 194 MNHKGIALVLATGGSG-----MVKSAYSTGKPALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDK 268
Cdd:cd07088 208 VAHPKVGMISLTGSTEagqkiMEAAAENITKVSLELG-GKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHE 286
|
170
....*....|...
gi 88193926 269 EIYKDVTNEFKAH 281
Cdd:cd07088 287 DIYDEFMEKLVEK 299
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
112-418 |
1.09e-07 |
|
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: 55.41 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 112 VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEaamkAGAPKDIIQWIEVPSIEATK 191
Cdd:cd07150 116 VRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEE----AGLPKGVFNVVTGGGAEVGD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 192 QLMNHKGIALVLATGGSGM-----VKSAYSTGKPALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVI 266
Cdd:cd07150 192 ELVDDPRVRMVTFTGSTAVgreiaEKAGRHLKKITLELG-GKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 267 DKEIYKDVTNEFKAHQAYFVKKDELQRlenaimneqKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIAE---------- 336
Cdd:cd07150 271 EEPVYDEFVKKFVARASKLKVGDPRDP---------DTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGkydgnfyqpt 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 337 -ISGVGSDYPLSREK-LSPVLALVKAQSTKQAFQICEDTLHfgglGHTAVIHTEDETLQKDFGLRMKACRVLVNTPS--- 411
Cdd:cd07150 342 vLTDVTPDMRIFREEtFGPVTSVIPAKDAEEALELANDTEY----GLSAAILTNDLQRAFKLAERLESGMVHINDPTild 417
|
330
....*....|.
gi 88193926 412 ----AVGGIGD 418
Cdd:cd07150 418 eahvPFGGVKA 428
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
115-251 |
2.02e-07 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 54.30 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 115 PIGVIcGVtpttnptsttIFK---------AMIAIKTGNPIIF-----AFHpsaqesSKRA-AEVVLEAAMKAGAPKDII 179
Cdd:PRK00197 115 PLGVI-GV----------IYEsrpnvtvdaAALCLKSGNAVILrggseAIH------SNRAlVAVIQEALEEAGLPADAV 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88193926 180 QWIEVPSIEATKQLMNHKG-IALVLATGGSGMVK--SAYSTgKPALGVGPGNVPSYIEKTAHIKRAVNDIIGSKT 251
Cdd:PRK00197 178 QLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRrvVENAT-VPVIEHGDGICHIYVDESADLDKALKIVLNAKT 251
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
99-408 |
7.32e-07 |
|
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: 52.75 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 99 GIIGEDK-------EKGLTY-VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFafhpsaqESSKRAAEVVLEAA- 169
Cdd:cd07108 93 GLAGELKgetlpfgPDVLTYtVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL-------KAAEDAPLAVLLLAe 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 170 -MKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATGGSGMVKSAYSTGKP-----ALGVGpGNVPSYIEKTAHIKRAV 243
Cdd:cd07108 166 iLAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADrlipvSLELG-GKSPMIVFPDADLDDAV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 244 NDIIGSKTFD-NGMICASEQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQRLEN--AIMNE-QKTGIKPDI-VGKSAVEI 318
Cdd:cd07108 245 DGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDigAIISEkQFAKVCGYIdLGLSTSGA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 319 AELAGIPVPENTKLiiAE--------ISGVGSDYPLSREKL-SPVLALVKAQSTKQAFQICEDTlHFgglGHTAVIHTED 389
Cdd:cd07108 325 TVLRGGPLPGEGPL--ADgffvqptiFSGVDNEWRLAREEIfGPVLCAIPWKDEDEVIAMANDS-HY---GLAAYVWTRD 398
|
330
....*....|....*....
gi 88193926 390 ETLQKDFGLRMKACRVLVN 408
Cdd:cd07108 399 LGRALRAAHALEAGWVQVN 417
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
61-292 |
6.83e-06 |
|
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: 49.66 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 61 LAKLAHEETGRGI----YE-DKAIKNLYASEYIWNSIK------DNKTVGiigeDKEKGLTyVAEPIGVICGVTPTTNPT 129
Cdd:cd07146 60 FARLITLESGLCLkdtrYEvGRAADVLRFAAAEALRDDgesfscDLTANG----KARKIFT-LREPLGVVLAITPFNHPL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 130 STTIFKAMIAIKTGNPIIfaFHPSaqESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATGGSG 209
Cdd:cd07146 135 NQVAHKIAPAIAANNRIV--LKPS--EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 210 MVKS-AYSTG--KPALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKDVTNEFKAHQAYFV 286
Cdd:cd07146 211 VGKAiAATAGykRQLLELG-GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALV 289
|
....*.
gi 88193926 287 KKDELQ 292
Cdd:cd07146 290 VGDPMD 295
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
504-731 |
1.50e-05 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 47.92 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 504 KTVENVLRQKTEQPQIKIFSevePNPSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKAmwmffehpetsffgakqkfl 583
Cdd:cd08550 39 EKLEKSLEEAGIDYEVEVFG---GECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKA-------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 584 dIGkrtYKIGMPenatFICIPTTSGTGSEVTPFAVITDSETNVKYPLAdFALTPDVAIIDPQFVMSVPKSVTAdTGM-DV 662
Cdd:cd08550 96 -VA---DRLGLP----VVTVPTIAATCAAWSALSVLYDEEGEFLGYSL-LKRSPDLVLVDTDIIAAAPVRYLA-AGIgDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 663 LT--HAMESYVSVMASDYTRGLSLQAIKLTFEYLK-------SSVEKGdKVSR--EKMHNAST-LAGMAF----ANAFLG 726
Cdd:cd08550 166 LAkwYEARPSSRGGPDDLALQAAVQLAKLAYDLLLeygvqavEDVRQG-KVTPalEDVVDAIIlLAGLVGslggGGCRTA 244
|
....*
gi 88193926 727 IAHSI 731
Cdd:cd08550 245 AAHAI 249
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
111-422 |
2.16e-05 |
|
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: 47.98 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 111 YVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQE--SSKRAAEVVLEaamkAGAPKDIIQWIEVPSIE 188
Cdd:cd07149 119 TIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV--LKPASQTplSALKLAELLLE----AGLPKGALNVVTGSGET 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 189 ATKQLMNHKGIALVLATGGsgmvksaYSTG----------KPALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMIC 258
Cdd:cd07149 193 VGDALVTDPRVRMISFTGS-------PAVGeaiarkaglkKVTLELG-SNAAVIVDADADLEKAVERCVSGAFANAGQVC 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 259 ASEQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQRlenaimneqKTGIKPDIVGKSAVEIAELAGIPVPENTKLII---- 334
Cdd:cd07149 265 ISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE---------DTDVGPMISEAEAERIEEWVEEAVEGGARLLTggkr 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 335 -------AEISGVGSDYPLS-REKLSPVLALVKAQSTKQAFQICEDT---LHFGglghtavIHTEDetLQKdfglRMKAC 403
Cdd:cd07149 336 dgailepTVLTDVPPDMKVVcEEVFAPVVSLNPFDTLDEAIAMANDSpygLQAG-------VFTND--LQK----ALKAA 402
|
330
....*....|....*....
gi 88193926 404 RVLvntpsAVGGIgdMYNE 422
Cdd:cd07149 403 REL-----EVGGV--MIND 414
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
109-418 |
4.73e-05 |
|
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: 46.66 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 109 LTY-VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQE--SSKRAAEVVLEaamkAGAPKDIIQWIEVP 185
Cdd:cd07115 110 LNYtVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVV--LKPAELTplSALRIAELMAE----AGFPAGVLNVVTGF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 186 SIEATKQLMNHKGIALVLATG----GSGMVKSAYSTGKP-ALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICAS 260
Cdd:cd07115 184 GEVAGAALVEHPDVDKITFTGstavGRKIMQGAAGNLKRvSLELG-GKSANIVFADADLDAAVRAAATGIFYNQGQMCTA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 261 EQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQRlenaimneqKTGIKPDIVGK------SAVEIAELAGIPVPENTKLII 334
Cdd:cd07115 263 GSRLLVHESIYDEFLERFTSLARSLRPGDPLDP---------KTQMGPLVSQAqfdrvlDYVDVGREEGARLLTGGKRPG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 335 AE--------ISGVGSDYPLSREKL-SPVLALVKAQSTKQAFQICEDTLHfgGLGhtAVIHTEDETLQKDFGLRMKACRV 405
Cdd:cd07115 334 ARgffveptiFAAVPPEMRIAQEEIfGPVVSVMRFRDEEEALRIANGTEY--GLA--AGVWTRDLGRAHRVAAALKAGTV 409
|
330
....*....|....*....
gi 88193926 406 LVNTPSAV------GGIGD 418
Cdd:cd07115 410 WINTYNRFdpgspfGGYKQ 428
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
114-412 |
7.31e-05 |
|
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: 46.09 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 114 EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFafhpsaqessKRAAEVVLEAAM------KAGAPKDIIQWIEVPSI 187
Cdd:cd07097 134 EPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVF----------KPAELTPASAWAlveileEAGLPAGVFNLVMGSGS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 188 EATKQLMNHKGIALVLATGGSGM-----VKSAYSTGKPALGVGPGNvPSYIEKTAHIKRAVNDIIGSKTFDNGMIC-ASE 261
Cdd:cd07097 204 EVGQALVEHPDVDAVSFTGSTAVgrriaAAAAARGARVQLEMGGKN-PLVVLDDADLDLAVECAVQGAFFSTGQRCtASS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 262 QVVViDKEIYKDVTNEFKAHQAYFVKKDELqrlenaimnEQKTGIKPdIVGK-------SAVEI-----AELA--GIPVP 327
Cdd:cd07097 283 RLIV-TEGIHDRFVEALVERTKALKVGDAL---------DEGVDIGP-VVSErqlekdlRYIEIarsegAKLVygGERLK 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 328 ENTK---LIIAEISGVGSDYPLSREKL-SPVLALVKAQSTKQAFQICEDTlhfgGLGHTAVIHTEDetLQK--DFGLRMK 401
Cdd:cd07097 352 RPDEgyyLAPALFAGVTNDMRIAREEIfGPVAAVIRVRDYDEALAIANDT----EFGLSAGIVTTS--LKHatHFKRRVE 425
|
330
....*....|.
gi 88193926 402 ACRVLVNTPSA 412
Cdd:cd07097 426 AGVVMVNLPTA 436
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
114-430 |
8.33e-05 |
|
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: 45.90 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 114 EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGApkdiiqwIEV--PSIEATK 191
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGV-------LNVvnGKGAVGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 192 QLMNHKGIALVLATG----GSGMVKSAYSTGKPA-LGVGPGNvPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVI 266
Cdd:cd07113 214 QLISHPDVAKVSFTGsvatGKKIGRQAASDLTRVtLELGGKN-AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 267 DKEIYKDVTNEFKAHQAYFVKKDELQrlENAIMNEQKTGIKPDIVgKSAVEIAELAGIPVPENTKLIIAE--------IS 338
Cdd:cd07113 293 HRSKFDELVTKLKQALSSFQVGSPMD--ESVMFGPLANQPHFDKV-CSYLDDARAEGDEIVRGGEALAGEgyfvqptlVL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 339 GVGSDYPLSREK-LSPVLALVKAQSTKQAFQICEDTlhfgGLGHTAVIHTEDETLQKDFGLRMKACRVLVNtpsavggig 417
Cdd:cd07113 370 ARSADSRLMREEtFGPVVSFVPYEDEEELIQLINDT----PFGLTASVWTNNLSKALRYIPRIEAGTVWVN--------- 436
|
330
....*....|...
gi 88193926 418 dMYNELIPSLTLG 430
Cdd:cd07113 437 -MHTFLDPAVPFG 448
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
139-366 |
1.25e-04 |
|
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: 45.29 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 139 AIKTGNPIIFafHPSaqESSKRAAEVvLEAAMKAGAPKDIIQWI--EVPsiEATKqLMNHKgIALVLATGgSGMV----- 211
Cdd:cd07135 132 AIAAGCTVVL--KPS--ELTPHTAAL-LAELVPKYLDPDAFQVVqgGVP--ETTA-LLEQK-FDKIFYTG-SGRVgriia 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 212 KSAYSTGKP-ALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIY-------KDVTNEF----- 278
Cdd:cd07135 202 EAAAKHLTPvTLELG-GKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYdefveelKKVLDEFypgga 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 279 KAHQAY--FVKKDELQRLENAImneQKTgiKPDIVGKSAVEIAELAGIPvpentkLIIAEISgvGSDYPLSREKLSPVLA 356
Cdd:cd07135 281 NASPDYtrIVNPRHFNRLKSLL---DTT--KGKVVIGGEMDEATRFIPP------TIVSDVS--WDDSLMSEELFGPVLP 347
|
250
....*....|
gi 88193926 357 LVKAQSTKQA 366
Cdd:cd07135 348 IIKVDDLDEA 357
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
133-408 |
1.64e-04 |
|
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: 45.26 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 133 IFKAMI--AIKTGNPIIFafHPSaqESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATGGSGM 210
Cdd:cd07125 183 IFTGQIaaALAAGNTVIA--KPA--EQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTET 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 211 VK----------------SAYSTGKPALgvgpgnvpsYIEKTAHIKRAVNDIIGSkTFDN-GMICASEQVVVIDKEIYKD 273
Cdd:cd07125 259 AKlinralaerdgpilplIAETGGKNAM---------IVDSTALPEQAVKDVVQS-AFGSaGQRCSALRLLYLQEEIAER 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 274 VtnefkahqayfvkkdeLQRLENAiMNEQKTG----IKPDI---VGKSAVEIAE------------LAGIPVPENTKLII 334
Cdd:cd07125 329 F----------------IEMLKGA-MASLKVGdpwdLSTDVgplIDKPAGKLLRahtelmrgeawlIAPAPLDDGNGYFV 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88193926 335 AE--ISGVGSDYpLSREKLSPVLALVKAQSTK--QAFQICEDTlhfgGLGHTAVIHTEDETLQKDFGLRMKACRVLVN 408
Cdd:cd07125 392 APgiIEIVGIFD-LTTEVFGPILHVIRFKAEDldEAIEDINAT----GYGLTLGIHSRDEREIEYWRERVEAGNLYIN 464
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
112-408 |
1.78e-04 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 44.89 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 112 VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSaqESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATK 191
Cdd:PRK09847 154 VREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVI--LKPS--EKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 192 QLMNHKGIALVLATGGSgmvksaySTGKPAL-GVGPGNVPS-YIE---KTAHI--------KRAVNDIIGSKTFDNGMIC 258
Cdd:PRK09847 230 ALSRHNDIDAIAFTGST-------RTGKQLLkDAGDSNMKRvWLEaggKSANIvfadcpdlQQAASATAAGIFYNQGQVC 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 259 ASEQVVVIDKEIYKDVTNEFKAHQAYFVKKDELQ---RLENAIMNEQKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIA 335
Cdd:PRK09847 303 IAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDpatTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPT 382
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88193926 336 EISGVGSDYPLSREKL-SPVLALVKAQSTKQAFQICEDTLHfgGLGhtAVIHTEDETLQKDFGLRMKACRVLVN 408
Cdd:PRK09847 383 IFVDVDPNASLSREEIfGPVLVVTRFTSEEQALQLANDSQY--GLG--AAVWTRDLSRAHRMSRRLKAGSVFVN 452
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
61-389 |
2.44e-04 |
|
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: 44.65 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 61 LAKLAHEETGRGIYEDKA--IKNLYASEYIWNSIKDNKTVGIIGEDKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMI 138
Cdd:cd07131 79 LARLVTREMGKPLAEGRGdvQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 139 AIKTGNPIIfaFHPSaqESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATG----GSGMVKSA 214
Cdd:cd07131 159 ALVCGNTVV--FKPA--EDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGstevGERIGETC 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 215 YSTGKP-ALGVGPGNvPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKdvtnEFKAHqayFVKKDELQR 293
Cdd:cd07131 235 ARPNKRvALEMGGKN-PIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYD----EFLKR---FVERAKRLR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 294 LENAimNEQKTGIKPdIVGKSAVE-IAELAGIPVPENTKLIIAE------------------ISGVGSDYPLSREKL-SP 353
Cdd:cd07131 307 VGDG--LDEETDMGP-LINEAQLEkVLNYNEIGKEEGATLLLGGerltgggyekgyfveptvFTDVTPDMRIAQEEIfGP 383
|
330 340 350
....*....|....*....|....*....|....*.
gi 88193926 354 VLALVKAQSTKQAFQICEDTlhfgGLGHTAVIHTED 389
Cdd:cd07131 384 VVALIEVSSLEEAIEIANDT----EYGLSSAIYTED 415
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
139-206 |
4.74e-04 |
|
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: 43.68 E-value: 4.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88193926 139 AIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSIEATKQLMNHKGIALVLATG 206
Cdd:cd07129 131 ALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTG 198
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
21-280 |
8.37e-04 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 42.97 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 21 IDAlADKGKKALEALSKKSQEEIDHIVHQMSLAAVDQhmvLAKLAHEETGRGIYEDKAiKNLYASEYI-WNSIKDNKTVG 99
Cdd:PRK11241 54 IDA-ANRALPAWRALTAKERANILRRWFNLMMEHQDD---LARLMTLEQGKPLAEAKG-EISYAASFIeWFAEEGKRIYG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 100 --IIGEDKEKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQesSKRAAEVVLEAAMKAGAPKD 177
Cdd:PRK11241 129 dtIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMV--LKPASQ--TPFSALALAELAIRAGIPAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 178 IIQWIEVPSIEATKQLMNHKGIALVLATGGSG-----MVKSAYSTGKPALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTF 252
Cdd:PRK11241 205 VFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEigrqlMEQCAKDIKKVSLELG-GNAPFIVFDDADLDKAVEGALASKFR 283
|
250 260
....*....|....*....|....*...
gi 88193926 253 DNGMICASEQVVVIDKEIYKDVTNEFKA 280
Cdd:PRK11241 284 NAGQTCVCANRLYVQDGVYDRFAEKLQQ 311
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
139-426 |
9.49e-04 |
|
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: 42.62 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 139 AIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGApkdiiqWIEVP-SIEATKQLMNHKGIALVLATGGSG---MVKSA 214
Cdd:cd07147 147 AIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGA------FSVLPcSRDDADLLVTDERIKLLSFTGSPAvgwDLKAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 215 YSTGKPALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKDVTNEFKAHQAYFVKKDElqrl 294
Cdd:cd07147 221 AGKKKVVLELG-GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDP---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 295 enaimNEQKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIA-EISG----------VGSDYPLSREKL-SPVLALVKAQS 362
Cdd:cd07147 296 -----KDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGgKRDGalleptiledVPPDMEVNCEEVfGPVVTVEPYDD 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88193926 363 TKQAFQICEDTlHFGglghtavihtedetLQ-----KDFGLRMKACRVLvntpsAVGG--IGDmynelIPS 426
Cdd:cd07147 371 FDEALAAVNDS-KFG--------------LQagvftRDLEKALRAWDEL-----EVGGvvIND-----VPT 416
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
139-320 |
1.13e-03 |
|
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: 42.23 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 139 AIKTGNPIIFafHPSAQESSkrAAEVVLEAAMKAGAPKDIIQWIeVPSIEATKQLMNHKGIALVLATGGS-GMVKSAYST 217
Cdd:cd07102 140 ALLAGNAVIL--KHSPQTPL--CGERFAAAFAEAGLPEGVFQVL-HLSHETSAALIADPRIDHVSFTGSVaGGRAIQRAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 218 GKPALGVG---PGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYkdvtNEFKAHqayFVKKDELQRL 294
Cdd:cd07102 215 AGRFIKVGlelGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIY----DAFVEA---FVAVVKGYKL 287
|
170 180
....*....|....*....|....*.
gi 88193926 295 ENAImnEQKTGIKPDIVGKSAVEIAE 320
Cdd:cd07102 288 GDPL--DPSTTLGPVVSARAADFVRA 311
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
114-277 |
1.14e-03 |
|
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: 42.29 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 114 EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGApKDIIQwievpSIEATKQL 193
Cdd:cd07090 115 EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGV-FNVVQ-----GGGETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 194 M-NHKGIALVLATG----GSGMVKSAYSTGKPA---LGvgpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVV 265
Cdd:cd07090 189 LcEHPDVAKVSFTGsvptGKKVMSAAAKGIKHVtleLG---GKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVF 265
|
170
....*....|..
gi 88193926 266 IDKEIYKDVTNE 277
Cdd:cd07090 266 VQRSIKDEFTER 277
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
135-284 |
1.16e-03 |
|
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: 42.55 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 135 KAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEAAMKAGAPKDIIQWIEVPSiEATKQLMNHKGIALVLATGGSGM---- 210
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVgrrv 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88193926 211 -VKSAYSTGKPALGVGpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKDVTNEFKAhqAY 284
Cdd:cd07086 232 gETVARRFGRVLLELG-GNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVK--AY 303
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
95-430 |
1.75e-03 |
|
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: 41.75 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 95 NKTVGIIGEDKEKGLTYVA-EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQESSKRAAEVVLEaamkAG 173
Cdd:cd07143 123 DKIHGQVIETDIKKLTYTRhEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPE----AG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 174 APKDIIQWIEVPSIEATKQLMNHKGIALVLATGGSG---MVKSAYSTG---KPALGVGpGNVPSYIEKTAHIKRAVNDII 247
Cdd:cd07143 199 FPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLvgrKVMEAAAKSnlkKVTLELG-GKSPNIVFDDADLESAVVWTA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 248 GSKTFDNGMICASEQVVVIDKEIYKDVTNEFKA---------------HQAYFVKKDELQRLENAIMNEQKTGIKPDIVG 312
Cdd:cd07143 278 YGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEkakklkvgdpfaedtFQGPQVSQIQYERIMSYIESGKAEGATVETGG 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 313 K----SAVEIAELAGIPVPENTKLIIAEISGvgsdyplsreklsPVLALVKAQSTKQAFQICEDTLHfgglGHTAVIHTE 388
Cdd:cd07143 358 KrhgnEGYFIEPTIFTDVTEDMKIVKEEIFG-------------PVVAVIKFKTEEEAIKRANDSTY----GLAAAVFTN 420
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 88193926 389 DETLQKDFGLRMKACRVLVNTpsavggigdmYNELIPSLTLG 430
Cdd:cd07143 421 NINNAIRVANALKAGTVWVNC----------YNLLHHQVPFG 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
139-400 |
2.38e-03 |
|
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: 41.41 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 139 AIKTGNPIIFafhpSAQESSKRAAEVVLEAAMKAGAPKDIIQWI-----EVPSIeaTKQLMNHKGIALVLATG----GSG 209
Cdd:cd07105 122 PLAAGNTVVL----KASELSPRTHWLIGRVFHEAGLPKGVLNVVthspeDAPEV--VEALIAHPAVRKVNFTGstrvGRI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 210 MVKSAYSTGKPA---LGvgpGNVPSYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVVVIDKEIYKDVTNEFKAH-QAYF 285
Cdd:cd07105 196 IAETAAKHLKPVlleLG---GKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAaEKLF 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88193926 286 VKKDELQRLENAIMNEQKTGIKPDIVGKSAVEIAELAGIPVPENTKLIIAEISGVGSDYPL-SREKLSPVLALVKAQSTK 364
Cdd:cd07105 273 AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPPTILDNVTPDMDIySEESFGPVVSIIRVKDEE 352
|
250 260 270
....*....|....*....|....*....|....*.
gi 88193926 365 QAFQICEDTlhfgGLGHTAVIHTEDETLqkdfGLRM 400
Cdd:cd07105 353 EAVRIANDS----EYGLSAAVFTRDLAR----ALAV 380
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
487-563 |
5.85e-03 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 39.70 E-value: 5.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88193926 487 EKVMIVCDPGMVEFgYTKTVENVLRQKTEQPQIKIFS-EVepnpSTNTVYKGLEMMVDFQPDTIIALGGGSAMDAAKA 563
Cdd:cd08170 23 KKALVIADPFVLDL-VGERLEESLEKAGLEVVFEVFGgEC----SREEIERLAAIARANGADVVIGIGGGKTIDTAKA 95
|
|
| |
