|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
11-865 |
0e+00 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 1557.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 11 ESNKDEVTQMIDSLAEKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGRGIYEDKAIKNLYASEYIWN 90
Cdd:PRK13805 4 EEMAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDKVIKNHFASEYIYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 91 SIKDNKTVGIIGEDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAI 170
Cdd:PRK13805 84 SYKDEKTVGVIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 171 KAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSGMVKSAYSTGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSK 250
Cdd:PRK13805 164 AAGAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 251 TFDNGMICASEQVMVVDKEVYSDVVKEFKLHQTYFVNKNELQQLEDAIMNEDKTAVKPDIVGKSAVNIAKLSGISVPEKT 330
Cdd:PRK13805 244 TFDNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFGKENGALNADIVGQSAYKIAEMAGFKVPEDT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 331 KLLVAEIDGIGKDYPLSREKLSPVLAMVTAKSTRHALQICEDTLKFGGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTP 410
Cdd:PRK13805 324 KILIAEVKGVGESEPLSHEKLSPVLAMYKAKDFEDAVEKAEKLVEFGGLGHTAVIYTNDDELIKEFGLRMKACRILVNTP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 411 SAVGGIGNMYNELIPSLTLGCGSYGRNSISHNVSAVDLLNIKTIAKRRNNMQWFKLPPKVYFEENSVMYL-TEMDNVERA 489
Cdd:PRK13805 404 SSQGGIGDLYNKLAPSLTLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLlDELDGKKRA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 490 MIVCDPGMVNIGYTDIVEQVLRRRENQPQIKVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWMFFE 569
Cdd:PRK13805 484 FIVTDRFMVELGYVDKVTDVLKKRENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLFYE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 570 HPETSFFGAKQKFLDIRKRTYKISK-PKNAKFICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQFVL 648
Cdd:PRK13805 564 HPETDFEDLAQKFMDIRKRIYKFPKlGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVM 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 649 SVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE--NDKHSREKMHNASTMAGMAFANAFLG 726
Cdd:PRK13805 644 TMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNgaKDPEAREKMHNASTIAGMAFANAFLG 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 727 ISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKDPQKHTLFPKYDFFRADTDYADIAKFLGLKGNTTEELVEALANAVY 806
Cdd:PRK13805 724 ICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPPKQAAFPQYEYPRADERYAEIARHLGLPGSTTEEKVESLIKAIE 803
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1545705897 807 DLGCSIGIDMNLKSQGVTEELLHSTIDRMAELAFEDQCTTANPKEPLISELKGIIERAY 865
Cdd:PRK13805 804 ELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYPLISELKEILLDAY 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: 692.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 21 IDSLAEKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGRGIYEDKAIKNLYASEYIWNSIKDNKTVGI 100
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYNDIKDMKTVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 101 IGEDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAIKAGAPKDCIQ 180
Cdd:cd07122 81 IEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 181 WIEIPSIEATKQLMNHKDIALVLATGGSGMVKSAYSTGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICAS 260
Cdd:cd07122 161 WIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 261 EQVMVVDKEVYSDVVKEFKLHQTYFVNKNELQQLEDAIMNEDKTaVKPDIVGKSAVNIAKLSGISVPEKTKLLVAEIDGI 340
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDDGGT-LNPDIVGKSAQKIAELAGIEVPEDTKVLVAEETGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 341 GKDYPLSREKLSPVLAMVTAKSTRHALQICEDTLKFGGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTPSAVGGIGNMY 420
Cdd:cd07122 320 GPEEPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPSSLGGIGDTY 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 1545705897 421 NELIPSLTLGCGSYGRNSISHNVSAVDLLNIKTIAKR 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: 640.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 465 KLPPKVYFEENSVMYL-TEMDNVERAMIVCDPGMVNIGYTDIVEQVLRRRenQPQIKVFNEVEPNPSTHTVYKGLEMFMN 543
Cdd:cd08178 1 KVPPKIYFEPGCLPYLlLELPGVKRAFIVTDRVLYKLGYVDKVLDVLEAR--GVETEVFSDVEPDPTLSTVRKGLEAMNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 544 FQPDTIIALGGGSAMDAAKAIWMFFEHPETSFFGAKQKFLDIRKRTYKISKP-KNAKFICIPTTSGTGSEVTPFAVITDS 622
Cdd:cd08178 79 FKPDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLgKKAKLVAIPTTSGTGSEVTPFAVITDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 623 ETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-N 701
Cdd:cd08178 159 KTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNgN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 702 DKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKD-PQKHTLFPKYDFFRADTDY 780
Cdd:cd08178 239 DIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDpPTKQAAFPQYKYYVAKERY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 781 ADIAKFLGLKGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEELLHSTIDRMAELAFEDQCTTANPKEPLISELKGI 860
Cdd:cd08178 319 AEIADLLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISELKEI 398
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
460-865 |
7.11e-172 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 502.34 E-value: 7.11e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 460 NMQWFKLPPKVYFEENSVMYL-TEMD--NVERAMIVCDPGMVNIGYTDIVEQVLRRRenQPQIKVFNEVEPNPSTHTVYK 536
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELgEELKrlGAKRALIVTDPGLAKLGLLDRVLDALEAA--GIEVVVFDDVEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 537 GLEMFMNFQPDTIIALGGGSAMDAAKAIWMFFEHPETSffgakQKFLDIRKrtykISKPKnAKFICIPTTSGTGSEVTPF 616
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDL-----EDYLGIKK----VPGPP-LPLIAIPTTAGTGSEVTPF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 617 AVITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKS 696
Cdd:COG1454 149 AVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 697 SVQE-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffR 775
Cdd:COG1454 229 AVADgDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAP--------------A 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 776 ADTDYADIAKFLGLK-GNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLI 854
Cdd:COG1454 295 APERYAEIARALGLDvGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEE----DLPELAELALADRCLANNPRPLTE 370
|
410
....*....|.
gi 1545705897 855 SELKGIIERAY 865
Cdd:COG1454 371 EDIEAILRAAY 381
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
463-865 |
3.14e-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: 469.75 E-value: 3.14e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 463 WFKLPPKVYFEENSVMYLTEMDNvERAMIVCDPG-MVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMF 541
Cdd:cd08179 1 RFFVPRDIYFGEGALEYLKTLKG-KRAFIVTGGGsMKRNGFLDKVEDYLK--EAGMEVKVFEGVEPDPSVETVEKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 542 MNFQPDTIIALGGGSAMDAAKAIWMFFEHPETsffgakqKFLDIrKRTYKISKPKN-AKFICIPTTSGTGSEVTPFAVIT 620
Cdd:cd08179 78 REFEPDWIIAIGGGSVIDAAKAMWVFYEYPEL-------TFEDA-LVPFPLPELRKkARFIAIPSTSGTGSEVTRASVIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 621 DSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE 700
Cdd:cd08179 150 DTEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 701 N-DKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKDPQKhtlfpkydffradtD 779
Cdd:cd08179 230 GkDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEA--------------R 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 780 YADIAKflgLKGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEELLHSTIDRMAELAFEDQCTTANPKEPLISELKG 859
Cdd:cd08179 296 ARYAAL---LIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNDACTGTNPRKPTVEEMKE 372
|
....*.
gi 1545705897 860 IIERAY 865
Cdd:cd08179 373 LLKAAY 378
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
13-455 |
2.17e-155 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 464.34 E-value: 2.17e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 13 NKDEVT-QMIDSLAEKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGRGIYEDKAIKNLYASEYIWNS 91
Cdd:TIGR02518 1 DKDLYSiQQVRNLIRSAKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVYDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 92 IKDNKTVGIIGEDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAIK 171
Cdd:TIGR02518 81 IKDMKTIGILSEDKEKKVIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 172 AGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSGMVKSAYSTGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKT 251
Cdd:TIGR02518 161 AGAPEGAIGCITVPTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 252 FDNGMICASEQVMVVDKEVYSDVVKEFKLHQTYFVNKNELQQLEDAIMNEDKTaVKPDIVGKSAVNIAKLSGISVPEKTK 331
Cdd:TIGR02518 241 FDNGTICASEQSIIVEECNKDAVVEELKKQGGYFLTAEEAEKLGKFILRPNGT-MNPQIVGKSPQVIANLAGLTVPEDAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 332 LLVAEIDGIGKDYPLSREKLSPVLAMVTAKSTRHALQICEDTLKFGGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTPS 411
Cdd:TIGR02518 320 VLIGEQNGVGNKNPYSREKLTTILAFYTEENWHEACELSIELLQNEGAGHTLIIHSENKDIVREFALKKPVSRMLVNTGG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1545705897 412 AVGGIGNMYNeLIPSLTLGCGSYGRNSISHNVSAVDLLNIKTIA 455
Cdd:TIGR02518 400 SLGGIGATTN-LVPAFTLGCGAVGGSSTSDNITPENLINIRRVA 442
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
21-457 |
1.51e-145 |
|
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: 437.08 E-value: 1.51e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 21 IDSLAEKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGRGIYEDKAIKNLYASEYIWNSIKDNKTVGI 100
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 101 IGEDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAIKAGAPKDCIQ 180
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 181 WIEIPSIEATKQLMNHKDIALVLATGGSGMVKSAYSTGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICAS 260
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 261 EQVMVVDKEVYSDVVKEFKLHQTYFVNKNELQQLEDAIMNEdkTAVKPDIVGKSAVNIAKLSGISVPEKTKLLVAEIDGI 340
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKN--GDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 341 GKDYPLSREKLSPVLAMVTAKSTRHALQICEDTLKFGGLGHTAVIHTEDSQLQQK---FGLKMKACRVLVNTPSAVGGIG 417
Cdd:cd07081 319 AEHEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSAMYSDNIKAIENmnqFANAMKTSRFVKNGPCSQGGLG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1545705897 418 NMYNELI-PSLTLGCGSYGRNSISHNVSAVDLLNIKTIAKR 457
Cdd:cd07081 399 DLYNFRGwPSMTLGCGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
464-862 |
1.45e-138 |
|
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: 414.97 E-value: 1.45e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSVMYLTEMDNvERAMIVCDPGMVNIGYTDIVEQVLrrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMN 543
Cdd:cd08180 1 FSLKTKIYSGEDSLERLKELKG-KRVFIVTDPFMVKSGMVDKVTDEL---DKSNEVEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 544 FQPDTIIALGGGSAMDAAKAIwMFFehpetsffgakqkfldIRKRTYKISKPKnakFICIPTTSGTGSEVTPFAVITDSE 623
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAKAI-IYF----------------ALKQKGNIKKPL---FIAIPTTSGTGSEVTSFAVITDPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 624 THVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-ND 702
Cdd:cd08180 137 KGIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDgDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 703 KHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYnakdpqkhtlfpkydffradtdyad 782
Cdd:cd08180 217 LEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 783 iakflglkgntteelveaLANAVYDLGCSIGIDMNLKSQGVTEELLHSTIDRMAELAFEDQCTTANPKEPLISELKGIIE 862
Cdd:cd08180 272 ------------------LIAAIRRLNKKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
467-861 |
5.17e-130 |
|
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: 394.12 E-value: 5.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYLTEM---DNVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMN 543
Cdd:cd08551 1 PTRIVFGAGALARLGEElkaLGGKKVLLVTDPGLVKAGLLDKVLESLK--AAGIEVEVFDDVEPNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 544 FQPDTIIALGGGSAMDAAKAIWMFFEHPET--SFFGAKqkfldirkrtyKISKPKnAKFICIPTTSGTGSEVTPFAVITD 621
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAVLATNGGSirDYEGIG-----------KVPKPG-LPLIAIPTTAGTGSEVTPNAVITD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 622 SETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE- 700
Cdd:cd08551 147 PETGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 701 NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK-DPQKhtlfpkydffradtd 779
Cdd:cd08551 227 SDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPaCPEK--------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 780 YADIAKFLGLK--GNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTAN-PKEPLISE 856
Cdd:cd08551 292 YAEIAEALGEDveGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEE----DIPELAEDAMKSGRLLSNnPRPLTEED 367
|
....*
gi 1545705897 857 LKGII 861
Cdd:cd08551 368 IREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
467-857 |
2.16e-127 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 386.96 E-value: 2.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYL-TEMDNV-ERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMNF 544
Cdd:pfam00465 1 PTRIVFGAGALAELgEELKRLgARALIVTDPGSLKSGLLDKVLASLE--EAGIEVVVFDGVEPEPTLEEVDEAAALAREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 545 QPDTIIALGGGSAMDAAKAIWMFFEHPETsffgakqkflDIRKRTYKISKPKNAKFICIPTTSGTGSEVTPFAVITDSET 624
Cdd:pfam00465 79 GADVIIAVGGGSVIDTAKAIALLLTNPGD----------VWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 625 HVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-NDK 703
Cdd:pfam00465 149 GEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADgEDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 704 HSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffRADTDYADI 783
Cdd:pfam00465 229 EARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAP--------------AAPEKLAQL 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545705897 784 AKFLGlkGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEELlhstIDRMAELAFEDQCTTANPKEPLISEL 857
Cdd:pfam00465 295 ARALG--EDSDEEAAEEAIEALRELLRELGLPTTLSELGVTEED----LDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
463-861 |
1.05e-118 |
|
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: 365.01 E-value: 1.05e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 463 WFKLPPKVYFEENSVMYLTEMDNvERAMIVCDPGMVNIGYTD-IVEQVLRRRENqpqIKVFNEVEPNPSTHTVYKGLEMF 541
Cdd:cd14862 2 WYFSSPKIVFGEDALSHLEQLSG-KRALIVTDKVLVKLGLLKkVLKRLLQAGFE---VEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 542 MNFQPDTIIALGGGSAMDAAKAIWMFFEHPETSFFGAKqkFLdirkrtYKISKPKNAKFICIPTTSGTGSEVTPFAVITD 621
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIS--PL------DLLGLRKKAKLIAIPTTSGTGSEATWAIVLTD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 622 SETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE- 700
Cdd:cd14862 150 TEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 701 NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKDpqkhtlfpkydffraDTDY 780
Cdd:cd14862 230 DDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKV---------------TDER 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 781 ADIAKFLGLKGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEELLHSTIDRMAELAFEDQCTTANPKEPLISELKGI 860
Cdd:cd14862 295 YDLLKLLGIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSEEDLKKL 374
|
.
gi 1545705897 861 I 861
Cdd:cd14862 375 F 375
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
464-862 |
1.49e-115 |
|
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: 356.82 E-value: 1.49e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSVMYLTEM---DNVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEM 540
Cdd:cd08188 3 FYIPPVNLFGPGCLKEIGDElkkLGGKKALIVTDKGLVKLGLVKKVTDVLE--EAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 541 FMNFQPDTIIALGGGSAMDAAKAIWMFFEHPetsffGAKQKFLDIRKrtykiSKPKNAKFICIPTTSGTGSEVTPFAVIT 620
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNG-----GEIEDYEGVDK-----SKKPGLPLIAINTTAGTASEVTRFAVIT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 621 DSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE 700
Cdd:cd08188 151 DEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 701 -NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK-DPQKhtlfpkydffradt 778
Cdd:cd08188 231 gKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPaCPER-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 779 dYADIAKFLGLK--GNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLISE 856
Cdd:cd08188 297 -FADIARALGENteGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEE----DFPLLAENALKDACGPTNPRQATKED 371
|
....*.
gi 1545705897 857 LKGIIE 862
Cdd:cd08188 372 VIAIYR 377
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
464-860 |
6.05e-109 |
|
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: 339.52 E-value: 6.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSV-MYLTEMD--NVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEM 540
Cdd:cd08176 3 FVLNPTSYFGWGAIeEIGEEAKkrGFKKALIVTDKGLVKFGIVDKVTDVLK--EAGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 541 FMNFQPDTIIALGGGSAMDAAKAIWMFFEHPetsffgakqkFLDIRKRT-YKISKPKNAKFICIPTTSGTGSEVTPFAVI 619
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGIIVANP----------GADVRSLEgVAPTKNPAVPIIAVPTTAGTGSEVTINYVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 620 TDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQ 699
Cdd:cd08176 151 TDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 700 E-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK-DPQKhtlfpkydffrad 777
Cdd:cd08176 231 NpNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPaTGEK------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 778 tdYADIAKFLGLKGN--TTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLIS 855
Cdd:cd08176 298 --YRDIARAMGVDTTgmSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEE----DIEALAEDALNDVCTPGNPREATKE 371
|
....*
gi 1545705897 856 ELKGI 860
Cdd:cd08176 372 DIIAL 376
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
464-865 |
8.12e-105 |
|
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: 329.12 E-value: 8.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSVM---YLTEMDNVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEM 540
Cdd:cd14865 3 FFNPTKIVSGAGALEnlpAELARLGARRPLIVTDKGLAAAGLLKKVEDALG--DAIEIVGVFDDVPPDSSVAVVNEAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 541 FMNFQPDTIIALGGGSAMDAAKAIWMFFEHpetsffGAKqkflDIRKRTYKISKPKNAK-FICIPTTSGTGSEVTPFAVI 619
Cdd:cd14865 81 AREAGADGIIAVGGGSVIDTAKGVNILLSE------GGD----DLDDYGGANRLTRPLKpLIAIPTTAGTGSEVTLVAVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 620 TDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQ 699
Cdd:cd14865 151 KDEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 700 E-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffRADT 778
Cdd:cd14865 231 NgKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLD--------------AAAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 779 DYADIAKFLGL----KGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLI 854
Cdd:cd14865 297 RYAELALALAYgvtpAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEE----QLEAIAELALNDGAILFNPREVDP 372
|
410
....*....|.
gi 1545705897 855 SELKGIIERAY 865
Cdd:cd14865 373 EDILAILEAAY 383
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
464-865 |
6.96e-104 |
|
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: 326.41 E-value: 6.96e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSV----MYLTEMdNVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLE 539
Cdd:cd14863 2 YSQLTPVIFGAGAVeqigELLKEL-GCKKVLLVTDKGLKKAGIVDKIIDLLE--EAGIEVVVFDDVEPDPPDEIVDEAAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 540 MFMNFQPDTIIALGGGSAMDAAKAIWMFFEHPetsffGAKQKFLDIRKRTYKISKPknakFICIPTTSGTGSEVTPFAVI 619
Cdd:cd14863 79 IAREEGADGVIGIGGGSVLDTAKAIAVLLTNP-----GPIIDYALAGPPVPKPGIP----LIAIPTTAGTGSEVTPIAVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 620 TDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQ 699
Cdd:cd14863 150 TDEENGVKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 700 E-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK-DPQKhtlfpkydffrad 777
Cdd:cd14863 230 DgDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEaYPEK------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 778 tdYADIAKFLGLK--GNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLIS 855
Cdd:cd14863 297 --VKKIAKALGVSfpGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKE----DLDKIAEAVLKDPFAMFNPRPITEE 370
|
410
....*....|
gi 1545705897 856 ELKGIIERAY 865
Cdd:cd14863 371 EVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
488-865 |
1.91e-100 |
|
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: 317.55 E-value: 1.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 488 RAMIVCDPGMVNIGYTDIVEQVLRRRENQPQikVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWMF 567
Cdd:cd08194 25 RALIVTDKVMVKLGLVDKVTQLLAEAGIAYA--VFDDVVSEPTDEMVEEGLALYKEGGCDFIVALGGGSPIDTAKAIAVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 568 FEHPEtsffgakqkflDIRK-RTYKISKPKNAKFICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQF 646
Cdd:cd08194 103 ATNGG-----------PIRDyMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLPAVAIVDPEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 647 VLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-NDKHSREKMHNASTMAGMAFANAFL 725
Cdd:cd08194 172 TLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADgDDLEAREAMMLAALEAGIAFSNSSV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 726 GISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKD-PQKhtlfpkydffradtdYADIAKFLGL--KGNTTEELVEALA 802
Cdd:cd08194 252 ALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGaPER---------------YAEIARAMGIatEGDSDEEAAEKLV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1545705897 803 NAVYDLGCSIGIDmNLKSQGVTEELLHSTIDRMAELAFEDQCTTANPKEPLISELKGIIERAY 865
Cdd:cd08194 317 EALERLCADLEIP-TLREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEEIIELYREAW 378
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
467-852 |
7.71e-100 |
|
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: 315.95 E-value: 7.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYLTE---MDNVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMN 543
Cdd:cd08189 5 EPELFEGAGSLLQLPEalkKLGIKRVLIVTDKGLVKLGLLDPLLDALK--KAGIEYVVFDGVVPDPTIDNVEEGLALYKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 544 FQPDTIIALGGGSAMDAAKAIWMFFEHPETSFfgAKQK-FLDIRKRTykiskpknAKFICIPTTSGTGSEVTPFAVITDS 622
Cdd:cd08189 83 NGCDAIIAIGGGSVIDCAKVIAARAANPKKSV--RKLKgLLKVRKKL--------PPLIAVPTTAGTGSEATIAAVITDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 623 ETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-N 701
Cdd:cd08189 153 ETHEKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDgS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 702 DKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffRADTDYA 781
Cdd:cd08189 233 DLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGP--------------AAEKRLA 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1545705897 782 DIAKFLGL--KGNTTEELVEALANAVYDLGCSIGIDMNLksqgvtEELLHSTIDRMAELAFEDqcttANPKEP 852
Cdd:cd08189 299 ELADAAGLgdSGESDSEKAEAFIAAIRELNRRMGIPTTL------EELKEEDIPEIAKRALKE----ANPLYP 361
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
485-860 |
1.09e-98 |
|
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: 312.56 E-value: 1.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 485 NVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAI 564
Cdd:cd17814 25 GARKVLVVTDPGVIKAGWVDEVLDSLE--AEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 565 WMFFEHPetsffGAKQKFLDIRKrtykISKPkNAKFICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDP 644
Cdd:cd17814 103 GIVVSNG-----GHILDYEGVDK----VRRP-LPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 645 QFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-NDKHSREKMHNASTMAGMAFANA 723
Cdd:cd17814 173 ETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADpDDLEAREKMMLASLQAGLAFSNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 724 FLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNakdpqkhtlfpkydFFRADTDYADIAKFLGL--KGNTTEELVEAL 801
Cdd:cd17814 253 SLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFN--------------FPAAPERYRKIAEAMGLdvDGLDDEEVAERL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1545705897 802 ANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLISELKGI 860
Cdd:cd17814 319 IEAIRDLREDLGIPETLSELGVDEE----DIPELAKRAMKDPCLVTNPRRPTREDIEEI 373
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
464-860 |
9.16e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 302.19 E-value: 9.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSVMYLTEM---DNVERAMIVCDPGMVNIGYTDIVEQVLRRREnqpqIKVFNEVEPNPSTHTVYKGLEM 540
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIikeLGGKRGLLVTDPSFIKSGLAKRIVESLKGRI----VAVFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 541 FMNFQPDTIIALGGGSAMDAAKAIWMFFEHPET--SFFGAKQKFldirkrtykisKPKNAKFICIPTTSGTGSEVTPFAV 618
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKTDGSieDYLEGKKKI-----------PKKGLPLIAIPTTAGTGSEVTPVAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 619 ITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSV 698
Cdd:cd08196 148 LTDKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 699 QE-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKDpqkhtlfpkyDFFRAD 777
Cdd:cd08196 228 NNpNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEA----------LPGRLD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 778 tdyaDIAKFLGLKGntteelVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLISEL 857
Cdd:cd08196 298 ----ELAKQLGFKD------AEELADKIEELKKRIGLRTRLSELGITEE----DLEEIVEESFHPNRANNNPVEVTKEDL 363
|
...
gi 1545705897 858 KGI 860
Cdd:cd08196 364 EKL 366
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
467-864 |
4.89e-90 |
|
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: 289.80 E-value: 4.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYL-TEMDN--VERAMIVCDPGMVNIGytdIVEQVLRRRENQP-QIKVFNEVEPNPSTHTVYKGLEMFM 542
Cdd:cd14861 3 PTRIRFGAGAIAELpEELKAlgIRRPLLVTDPGLAALG---IVDRVLEALGAAGlSPAVFSDVPPNPTEADVEAGVAAYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 543 NFQPDTIIALGGGSAMDAAKAIWMFFEHPetsffGAKQKFLDIRKRTYKISkPKNAKFICIPTTSGTGSEVTPFAVITDS 622
Cdd:cd14861 80 EGGCDGIIALGGGSAIDAAKAIALMATHP-----GPLWDYEDGEGGPAAIT-PAVPPLIAIPTTAGTGSEVGRAAVITDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 623 ETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSV----MASdytrGLSLQAIKLTFDYLKSSV 698
Cdd:cd14861 154 DTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPgfhpMAD----GIALEGLRLISEWLPRAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 699 QE-NDKHSREKMHNASTMAGMAFANAfLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffRAD 777
Cdd:cd14861 230 ADgSDLEARGEMMMAALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRP--------------AVE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 778 TDYADIAKFLGLKGNTTEELVEALAnavyDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLISEL 857
Cdd:cd14861 295 DKLARLARALGLGLGGFDDFIAWVE----DLNERLGLPATLSELGVTED----DLDELAELALADPCHATNPRPVTAEDY 366
|
....*..
gi 1545705897 858 KGIIERA 864
Cdd:cd14861 367 RALLREA 373
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
488-865 |
6.47e-85 |
|
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: 276.24 E-value: 6.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 488 RAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWMF 567
Cdd:TIGR02638 31 KALVVTDKDLIKFGVADKVTDLLD--EAGIAYELFDEVKPNPTITVVKAGVAAFKASGADYLIAIGGGSPIDTAKAIGII 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 568 FEHPEtsffgakqkFLDIRKRTyKISKPKNAK--FICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQ 645
Cdd:TIGR02638 109 SNNPE---------FADVRSLE-GVAPTKKPGvpIIAIPTTAGTAAEVTINYVITDEENKRKFVCVDPHDIPDVAVIDAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 646 FVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-NDKHSREKMHNASTMAGMAFANAF 724
Cdd:TIGR02638 179 MMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGgKDLEAREQMALGQYVAGMGFSNVG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 725 LGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNA-KDPQKhtlfpkydffradtdYADIAKFLGLK--GNTTEELVEAL 801
Cdd:TIGR02638 259 LGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAeFTGEK---------------YREIAKAMGVKteGMSDEEARDAA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545705897 802 ANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLISElkgiIERAY 865
Cdd:TIGR02638 324 VEAVKTLSKRVGIPEGLSELGVKEE----DIPALAEAALADVCTGGNPRETTVEE----IEELY 379
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
488-862 |
1.90e-84 |
|
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: 275.14 E-value: 1.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 488 RAMIVCDPG-MVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWM 566
Cdd:cd08185 27 KALIVTGKGsSKKTGLLDRVKKLLE--KAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFVIGLGGGSSMDAAKAIAF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 567 FFEHPETSF---FGAKQKFLdIRKRTYKIskpknakfICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVD 643
Cdd:cd08185 105 MATNPGDIWdyiFGGTGKGP-PPEKALPI--------IAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPALFPKVSIVD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 644 PQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-NDKHSREKMHNASTMAGMAFAN 722
Cdd:cd08185 176 PELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDgSDLEAREKMAWASTLAGIVIAN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 723 AFLGISHSIAHKIGGEYG-IPHGRTNAILLPHVIRYNA-KDPQKhtlfpkydffradtdYADIAKFlGLKGNTTEELVEA 800
Cdd:cd08185 256 SGTTLPHGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIeKAPEK---------------FAFVARA-EASGLSDAKAAED 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545705897 801 LANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFE--DQCTTANPKEPLISELKGIIE 862
Cdd:cd08185 320 FIEALRKLLKDIGLDDLLSDLGVTEE----DIPWLAENAMEtmGGLFANNPVELTEEDIVEIYE 379
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
487-865 |
3.19e-82 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 269.17 E-value: 3.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 487 ERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWM 566
Cdd:PRK10624 31 KKALIVTDKTLVKCGVVAKVTDVLD--AAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 567 FFEHPEtsffgakqkFLDIRK-----RTYKISKPknakFICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAI 641
Cdd:PRK10624 109 ISNNPE---------FADVRSlegvaPTKKPSVP----IIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 642 VDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVqENDKHSREKMHNASTMAGMAFA 721
Cdd:PRK10624 176 VDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAV-AGDKEAGEGMALGQYIAGMGFS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 722 NAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAkdpqkhtlfpkyDFfrADTDYADIAKFLGLK--GNTTEELVE 799
Cdd:PRK10624 255 NVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA------------DF--TGEKYRDIARAMGVKveGMSLEEARN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1545705897 800 ALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLISELKGIIERAY 865
Cdd:PRK10624 321 AAVEAVKALNRDVGIPPHLRDVGVKEE----DIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
467-835 |
8.56e-82 |
|
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: 267.55 E-value: 8.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYLTEM---DNVERAMIVCDPGMVNIGYtdiVEQVLRRRENQPQIKVFNEVEPNPSTHTVYKGLEMFMN 543
Cdd:cd08182 1 PVKIIFGPGALAELKDLlggLGARRVLLVTGPSAVRESG---AADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 544 FQPDTIIALGGGSAMDAAKAIWMFFEHPETSffgakqkfLDIRKRTYKISKPKNAKFICIPTTSGTGSEVTPFAVITDSE 623
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAALLGSPGEN--------LLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 624 THVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-ND 702
Cdd:cd08182 150 EGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENlPN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 703 KHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKDPQKhtlfpkydffrADTDYAD 782
Cdd:cd08182 230 LEAREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDE-----------CDDDPRG 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1545705897 783 IAKFLGLKGNTTEELVEALANavydLGCSIGIDMNLKSQGVTEELLHSTIDRM 835
Cdd:cd08182 299 REILLALGASDPAEAAERLRA----LLESLGLPTRLSEYGVTAEDLEALAASV 347
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
488-865 |
4.81e-81 |
|
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: 266.40 E-value: 4.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 488 RAMIVCDPGMVNIGYTDIVEQVLRRRENQPQikVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWMF 567
Cdd:cd08191 27 RVLIVTDPRLASTPLVAELLAALTAAGVAVE--VFDGGQPELPVSTVADAAAAARAFDPDVVIGLGGGSNMDLAKVVALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 568 FEHPET--SFFGakqkFLDIRKRTykisKPknakFICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQ 645
Cdd:cd08191 105 LAHGGDprDYYG----EDRVPGPV----LP----LIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAIVDPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 646 FVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRG---------------LSLQAIKLTFDYLKSSVQE-NDKHSREKM 709
Cdd:cd08191 173 LTLTCPPGVTADSGIDALTHAIESYTARDFPPFPRLdpdpvyvgknpltdlLALEAIRLIGRHLPRAVRDgDDLEARSGM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 710 HNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKDPQKHtlfpkydffradtdYADIAKFLGL 789
Cdd:cd08191 253 ALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAE--------------LAEIARALGV 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545705897 790 K-GNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQ-CTTANPKEPLISELKGIIERAY 865
Cdd:cd08191 319 TtAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEA----DLPGLAEKALSVTrLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
524-862 |
6.43e-75 |
|
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: 249.34 E-value: 6.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 524 EVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWMFFEHPetsffGAKQKFLDIRKRTYKISKPKnAKFICI 603
Cdd:cd08183 57 SVSGEPTVETVDAAVALAREAGCDVVIAIGGGSVIDAAKAIAALLTNE-----GSVLDYLEVVGKGRPLTEPP-LPFIAI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 604 PTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLS 683
Cdd:cd08183 131 PTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 684 LQAIKLTFDYLKSSVQE-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdp 762
Cdd:cd08183 211 REGLRLAARSLRRAYEDgEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLR-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 763 qkhTLFPKYDFFRADTDYADIAKFLGLKGNTTeelVEALANAVYDLGCSIGIDmNLKSQGVTEEllhsTIDRMAELAFED 842
Cdd:cd08183 289 ---ALREREPDSPALARYRELAGILTGDPDAA---AEDGVEWLEELCEELGIP-RLSEYGLTEE----DFPEIVEKARGS 357
|
330 340
....*....|....*....|
gi 1545705897 843 QCTTANPKEPLISELKGIIE 862
Cdd:cd08183 358 SSMKGNPIELSDEELLEILE 377
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
485-865 |
2.69e-74 |
|
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: 249.00 E-value: 2.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 485 NVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAI 564
Cdd:cd08190 22 GAKKVLVVTDPGLAKLGLVERVLESLE--KAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 565 WMFFEHPetsffgakQKFLDIRKRTYKISKPKNAK---FICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAI 641
Cdd:cd08190 100 NLYATHP--------GDFLDYVNAPIGKGKPVPGPlkpLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLRPTLAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 642 VDPQFVLSVPKDIAADTGMDVLTHAIESYvsvMASDYTR--------------G-------LSLQAIKLTFDYLKSSV-Q 699
Cdd:cd08190 172 VDPLLTLTLPPRVTASSGFDVLCHALESY---TARPYNArprpanpderpayqGsnpisdvWAEKAIELIGKYLRRAVnD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 700 ENDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGG-------------EYGIPHGRTNAILLPHVIRYNAK-DPQKH 765
Cdd:cd08190 249 GDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppgypvdHPHVPHGLSVALTAPAVFRFTAPaCPERH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 766 tlfpkydffradtdyADIAKFLG--LKGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQ 843
Cdd:cd08190 329 ---------------LEAAELLGadTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSED----DIPALVEGTLPQQ 389
|
410 420
....*....|....*....|...
gi 1545705897 844 CTTA-NPKEPLISELKGIIERAY 865
Cdd:cd08190 390 RLLKlNPRPVTEEDLEEIFEDAL 412
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
464-865 |
3.95e-70 |
|
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: 236.64 E-value: 3.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSVMYLTEM---DNVERAMIVCDPGMVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEM 540
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELlreLGARRVLLVTDPGLVKAGLADPALAALE--AAGIAVTVFDDVVADPPEAVVEAAVEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 541 FMNFQPDTIIALGGGSAMDAAKAIWMFFehpetsffGAKQKFLDIrkrtYKISKPKNAK--FICIPTTSGTGSEVTPFAV 618
Cdd:cd08193 79 AREAGADGVIGFGGGSSMDVAKLVALLA--------GSDQPLDDI----YGVGKATGPRlpLILVPTTAGTGSEVTPISI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 619 ITDSEThVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSV----MASDytrGLSLQAIKLTFDYL 694
Cdd:cd08193 147 VTTGET-EKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRhkknPISD---ALAREALRLLGANL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 695 KSSVQE-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydf 773
Cdd:cd08193 223 RRAVEDgSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLP------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 774 fRADTDYADIAKFL--GLKGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEELLhstiDRMAELAFEDQ-CTTANPK 850
Cdd:cd08193 290 -AAEALYAELARALlpGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDL----PMLAEDAMKQTrLLVNNPR 364
|
410
....*....|....*
gi 1545705897 851 EPLISELKGIIERAY 865
Cdd:cd08193 365 EVTEEDALAIYQAAL 379
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
464-805 |
3.06e-69 |
|
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: 233.63 E-value: 3.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSV-MYLTEMDNV-ERAMIVCdpGMVNI---GYTDIVEQVLRRRENQPQIkvFNEVEPNPSTHTVYKGL 538
Cdd:cd08181 1 FYMPTKVYFGKNCVeKHADELAALgKKALIVT--GKHSAkknGSLDDVTEALEENGIEYFI--FDEVEENPSIETVEKGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 539 EMFMNFQPDTIIALGGGSAMDAAKAIWMFFEHPetsffgakqkflDIRKRTYKISKPKNAK-FICIPTTSGTGSEVTPFA 617
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIALLAANK------------DGDEDLFQNGKYNPPLpIVAIPTTAGTGSEVTPYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 618 VITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKS- 696
Cdd:cd08181 145 ILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 697 SVQENDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK-DPQKHTLFPKYDFFr 775
Cdd:cd08181 225 LGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKqEPEKVDKILKLLGF- 303
|
330 340 350
....*....|....*....|....*....|....
gi 1545705897 776 adTDYADIAKFL----GLKGNTTEELVEALANAV 805
Cdd:cd08181 304 --GSIEEFQKFLnrllGKKEELSEEELEKYADEA 335
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
26-456 |
1.41e-68 |
|
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: 232.88 E-value: 1.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 26 EKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGR-------------GIYEDKAIKNLYASEYIWNSi 92
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAyirslianwiammGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 93 kDNKTVGIIGEDKqkGLTYV-AEPIGVICGVTPTTNPTSTtIFKAMIAIKTGNPIIFAFHPSAQQSSkHAAKVILEAAIK 171
Cdd:cd07077 80 -VGHIQDVLLPDN--GETYVrAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 172 AGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSGMVKSAY--STGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGS 249
Cdd:cd07077 155 AHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVkhSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 250 KTFDNgMICASEQVMVVDKEVYSDVVKEFKLHQTYfvnknelqqledaimnedktavkpdivgksavniaklSGISVPEK 329
Cdd:cd07077 235 KFFDQ-NACASEQNLYVVDDVLDPLYEEFKLKLVV-------------------------------------EGLKVPQE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 330 TKLLVAEIdgIGKDYPLSREKLSPVLAMVTAKSTRHALQICEDTLKFGGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNT 409
Cdd:cd07077 277 TKPLSKET--TPSFDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNE 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1545705897 410 PSAVGGiGNMYN-ELIPSLTLGCGSYGRNsishNVSAVDLLNIKTIAK 456
Cdd:cd07077 355 SSKKGR-GAFAGkGVERIVTSGMNNIFGA----GVGHDALRPLKRLVR 397
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
21-417 |
1.85e-67 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 232.10 E-value: 1.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 21 IDSLAEKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGRGIYEDKAIKNLYASEYIwNSIKDNKTVGI 100
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAEKT-PGVEDLTTEAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 101 IGEDkqkGLTYVaE--PIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAIKAGAPKDC 178
Cdd:PRK15398 117 TGDN---GLTLI-EyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGGPENL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 179 IQWIEIPSIEATKQLMNHKDIALVLATGGSGMVKSAYSTGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMIC 258
Cdd:PRK15398 193 VVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPC 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 259 ASEQVMVVDKEVYSDVVKEFKLHQTYFVNKNELQQLEDAIMnEDKTAVKPDIVGKSAVNIAKLSGISVPEKTKLLVAEID 338
Cdd:PRK15398 273 IAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVL-KNGGTVNKKWVGKDAAKILEAAGINVPKDTRLLIVETD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 339 gigKDYPL-SREKLSPVLAMVTAKSTRHALqicEDTLKF-GGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTPSAVG-G 415
Cdd:PRK15398 352 ---ANHPFvVTELMMPVLPVVRVKDVDEAI---ALAVKLeHGNRHTAIMHSRNVDNLNKMARAIQTSIFVKNGPSYAGlG 425
|
..
gi 1545705897 416 IG 417
Cdd:PRK15398 426 LG 427
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
25-417 |
7.95e-65 |
|
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: 223.65 E-value: 7.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 25 AEKGQEALKELSKKSQQEINDIVHQMSMATVDQhmhLAKLAYDETGRGIYEDKAIKNLYASEYIwNSIKDNKTVGIIGED 104
Cdd:cd07121 13 AKAAQKQYRKCTLADREKIIEAIREALLSNAEE---LAEMAVEETGMGRVEDKIAKNHLAAEKT-PGTEDLTTTAWSGDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 105 kqkGLT-YVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAIKAGAPKDCIQWIE 183
Cdd:cd07121 89 ---GLTlVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDNLVVTVE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 184 IPSIEATKQLMNHKDIALVLATGGSGMVKSAYSTGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQV 263
Cdd:cd07121 166 EPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 264 MVVDKEVYSDVVKEFKLHQTYFVN-KNELQQLEDAIMNEDKTAVKPDIVGKSAVNIAKLSGISVPEKTKLLVAEIDgigK 342
Cdd:cd07121 246 VIAVDSVADYLIAAMQRNGAYVLNdEQAEQLLEVVLLTNKGATPNKKWVGKDASKILKAAGIEVPADIRLIIVETD---K 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545705897 343 DYPL-SREKLSPVLAMVTAKSTRHALqicEDTLKF-GGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTPSAVG-GIG 417
Cdd:cd07121 323 DHPFvVEEQMMPILPVVRVKNFDEAI---ELAVELeHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNGPSYAGlGVG 397
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
488-864 |
6.70e-61 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 211.74 E-value: 6.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 488 RAMIVCDPGMVNIGYTDIVEQVLRRRENQPQIkvFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWMF 567
Cdd:PRK09860 33 RTLIVTDNMLTKLGMAGDVQKALEERNIFSVI--YDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 568 FEHpetsffGAkqkflDIRK-----RTYKISKPknakFICIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIV 642
Cdd:PRK09860 111 AAN------GG-----DIRDyegvdRSAKPQLP----MIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 643 DPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQENDK-HSREKMHNASTMAGMAFA 721
Cdd:PRK09860 176 DSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNaKAREAMAYAQFLAGMAFN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 722 NAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffRADTDYADIAKFLG--LKGNTTEELVE 799
Cdd:PRK09860 256 NASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK--------------VAAARLRDCAAAMGvnVTGKNDAEGAE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545705897 800 ALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQCTTANPKEPLISELKGIIERA 864
Cdd:PRK09860 322 ACINAIRELAKKVDIPAGLRDLNVKEE----DFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
503-864 |
6.99e-53 |
|
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: 189.00 E-value: 6.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 503 TDIVEQvLRRRENQPQIKVFNEVEPnpstHT----VYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWMFFEHPETSFFGA 578
Cdd:cd08192 38 TDVIKR-LEEALGDRHVGVFSGVRQ----HTpredVLEAARAVREAGADLLVSLGGGSPIDAAKAVALALAEDVTDVDQL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 579 KQKFLDIRKRTYKisKPKNAKFICIPTT-SGtgSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAAD 657
Cdd:cd08192 113 DALEDGKRIDPNV--TGPTLPHIAIPTTlSG--AEFTAGAGATDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 658 TGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-NDKHSREKMHNASTMAGMAFANAF-LGISHSIAHKI 735
Cdd:cd08192 189 TGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADpEDLEARLKCQLAAWLSLFGLGSGVpMGASHAIGHQL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 736 GGEYGIPHGRTNAILLPHVIRYNAKDPqkhtlfpkydffrADTDyADIAKFLGLKGNTTEELVEALANAVYDLGCSIGID 815
Cdd:cd08192 269 GPLYGVPHGITSCIMLPAVLRFNAPVN-------------AERQ-RLIARALGLVTGGLGREAADAADAIDALIRELGLP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1545705897 816 MNLKSQGVTEELLhstiDRMAELAFEDQCTTANPkEPLIS--ELKGIIERA 864
Cdd:cd08192 335 RTLRDVGVGRDQL----EKIAENALTDVWCRTNP-RPITDkdDVLEILESA 380
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
464-841 |
1.09e-51 |
|
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: 185.71 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSVMYLTEM--DNVERAMIVCDPG-MVNIGYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEM 540
Cdd:cd08187 4 FYNPTKIIFGKGAIEELGEEikKYGKKVLLVYGGGsIKKNGLYDRVVASLK--EAGIEVVEFGGVEPNPRLETVREGIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 541 FMNFQPDTIIALGGGSAMDAAKAI----------WMFFEHPEtsffgakqkfldirkrtykisKPKNA-KFICIPTTSGT 609
Cdd:cd08187 82 AREENVDFILAVGGGSVIDAAKAIaagakydgdvWDFFTGKA---------------------PPEKAlPVGTVLTLAAT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 610 GSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVS-VMASDYTRGLSLQAIK 688
Cdd:cd08187 141 GSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRLAEGLLR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 689 LTFDYLKSSVQE-NDKHSREKMHNASTMAgmafANAFLGI-------SHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK 760
Cdd:cd08187 221 TVIENGPKALKDpDDYEARANLMWAATLA----LNGLLGAgrggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 761 -DPQKhtlfpkydffradtdYADIAK--FLGLKGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAE 837
Cdd:cd08187 297 kKPER---------------FAQFARrvFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDEE----DIEEMAE 357
|
....
gi 1545705897 838 LAFE 841
Cdd:cd08187 358 KAVR 361
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
547-850 |
6.59e-47 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 172.52 E-value: 6.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 547 DTIIALGGGSAMDAAKAIWMFFEHPEtsffgakQKFLDIRKRTykISKPKnAKFICIPTTSGTGSEVTPFAVITDSETHV 626
Cdd:PRK15454 108 DGVIAFGGGSVLDAAKAVALLVTNPD-------STLAEMSETS--VLQPR-LPLIAIPTTAGTGSETTNVTVIIDAVSGR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 627 KYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSV-QENDKHS 705
Cdd:PRK15454 178 KQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVgYGHDLAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 706 REKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKDPQKHtlfpkydffradtdYADIAK 785
Cdd:PRK15454 258 RESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRER--------------FSQIGR 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545705897 786 flGLKGNTTEELvEALAnAVYDLGCSIGIDMNLKSQGVTEELLHStidrMAELAFEDQCTTANPK 850
Cdd:PRK15454 324 --ALRTKKSDDR-DAIN-AVSELIAEVGIGKRLGDVGATSAHYGA----WAQAALEDICLRSNPR 380
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
467-864 |
7.97e-47 |
|
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: 172.03 E-value: 7.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYL-TEMDNV--ERAMIVCDPGMV-NIGYTDIVEQVLRRRENQpqikVFNEVEPNPSTHTVYKGLEMFM 542
Cdd:cd14866 5 PLRLFSGRGALARLgRELDRLgaRRALVVCGSSVGaNPDLMDPVRAALGDRLAG----VFDGVRPHSPLETVEAAAEALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 543 NFQPDTIIALGGGSAMDAAKAIWMF------FEHPETSFFGakqkflDIRKRTYKISKPKNAKFIcIPTTSGTGSEVTPF 616
Cdd:cd14866 81 EADADAVVAVGGGSAIVTARAASILlaedrdVRELCTRRAE------DGLMVSPRLDAPKLPIFV-VPTTPTTADVKAGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 617 AViTDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKS 696
Cdd:cd14866 154 AV-TDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 697 SVQENDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffRA 776
Cdd:cd14866 233 LADDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAP--------------AT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 777 DTDYADIAKFLGLKGNTTEELVEALANAVYDLGCSIGIDMNLKSQGVTEELLhstiDRMAELAFEDQCTTANPK-EPLIS 855
Cdd:cd14866 299 DGRLDRLAEALGVADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDL----PAIAEAAMDDWFMDNNPRpVPTAE 374
|
....*....
gi 1545705897 856 ELKGIIERA 864
Cdd:cd14866 375 ELEALLEAA 383
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
468-841 |
7.43e-44 |
|
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: 163.21 E-value: 7.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 468 PKVYFEENSVmylTEMDN------VERAMIVCDPGMVNI-GYTDIVEQVLRrrENQPQIKVFNEVEPNPSTHTVYKGLEM 540
Cdd:cd08186 2 TTLYFGVGAI---AKIKDilkdlgIDKVIIVTGRSSYKKsGAWDDVEKALE--ENGIEYVVYDKVTPNPTVDQADEAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 541 FMNFQPDTIIALGGGSAMDAAKAIWMFFEHPetsffGAKQKFLDIRKRTYKISKPknakFICIPTTSGTGSEVTPFAVIT 620
Cdd:cd08186 77 ARDFGADAVIAIGGGSPIDTAKSVAVLLAYG-----GKTARDLYGFRFAPERALP----LVAINLTHGTGSEVDRFAVAT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 621 DSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE 700
Cdd:cd08186 148 IPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALAN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 701 -NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGG-EYGIPHGRTNAILLPHVIRYnakdpqKHTLFPKYdffradt 778
Cdd:cd08186 228 pKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGlKPELPHGLGLALLGPAVVKY------IYKAVPET------- 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545705897 779 dYADIAKFL--GLKGntTEELVEALANAVYDLGCSIGIDMNLKSQGVTEellhSTIDRMAELAFE 841
Cdd:cd08186 295 -LADILRPIvpGLKG--TPDEAEKAARGVEEFLFSVGFTEKLSDYGFTE----DDVDRLVELAFT 352
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
525-841 |
7.60e-43 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 160.62 E-value: 7.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 525 VEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAIWM--FFEHPETSFFGAKQKfldirkrtykiskPKNA-KFI 601
Cdd:COG1979 68 VEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIAAgaKYDGDPWDILTGKAP-------------VEKAlPLG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 602 CIPTTSGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSvmasdYTRG 681
Cdd:COG1979 135 TVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFT-----YPVD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 682 LSLQ-----AIKLTfdylkssVQENDKHSREKMHN---------ASTMAgmafANAFLGI-------SHSIAHKIGGEYG 740
Cdd:COG1979 210 APLQdrfaeGLLRT-------LIEEGPKALKDPEDydaranlmwAATLA----LNGLIGAgvpqdwaTHMIEHELSALYD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 741 IPHGRTNAILLPHVIRYNAKDpqkhtlfpkydffradtdyaDIAKFL-------GLKGNTTEELVEALANAVYDLGCSIG 813
Cdd:COG1979 279 IDHGAGLAIVLPAWMRYVLEE--------------------KPEKFAqyaervwGITEGDDEERALEGIEATEEFFESLG 338
|
330 340
....*....|....*....|....*...
gi 1545705897 814 IDMNLKSQGVTEEllhsTIDRMAELAFE 841
Cdd:COG1979 339 LPTRLSEYGIDEE----DIEEMAEKATA 362
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
464-865 |
3.27e-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: 158.62 E-value: 3.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 464 FKLPPKVYFEENSVM----YLTEMDNveRAMIVCDPGMVNIGYTDIVEQVLRRRenQPQIKVFNEVEPNPSTHTVYKGLE 539
Cdd:cd14864 1 FKIPPNIVFGADSLErigeEVKEYGS--RFLLITDPVLKESGLADKIVSSLEKA--GISVIVFDEIPASATSDTIDEAAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 540 MFMNFQPDTIIALGGGSAMDAAKAIWMFFEHPEtsffGAKQKFLDirkrtykiSKPKNA--KFICIPTTSGTGSEVTPFA 617
Cdd:cd14864 77 LARKAGADGIIAVGGGKVLDTAKAVAILANNDG----GAYDFLEG--------AKPKKKplPLIAVPTTPRSGFEFSDRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 618 VITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSS 697
Cdd:cd14864 145 PVVDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 698 VQE-NDKHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK-DPQKhtlfpkydffr 775
Cdd:cd14864 225 LADpKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATsAPDK----------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 776 adtdYADIAKFLGlkGNTTEELVEALANAVYDLGCSIGIDMNLKSQgVTEELLHSTIDRMAELAFEDQCTTANPKEPLIS 855
Cdd:cd14864 294 ----YAKIARALG--EDVEGASPEEAAIAAVEGVRRLIAQLNLPTR-LKDLDLASSLEQLAAIAEDAPKLNGLPRSMSSD 366
|
410
....*....|
gi 1545705897 856 ELKGIIERAY 865
Cdd:cd14864 367 DIFDILKAAF 376
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
467-865 |
3.37e-36 |
|
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: 139.95 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYLT-EMD--NVERAMIVCDPGMVNIGytDIVEQVLRRREnqpqIKVFNEVEPNPSTHTVYKGLEMFMN 543
Cdd:cd08177 1 PQRVVFGAGTLAELAeELErlGARRALVLSTPRQRALA--ERVAALLGDRV----AGVFDGAVMHVPVEVAERALAAARE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 544 FQPDTIIALGGGSAMDAAKAIwmffehpetsffgakqkfldiRKRTykiskpkNAKFICIPTTSgTGSEVTPFAVITdsE 623
Cdd:cd08177 75 AGADGLVAIGGGSAIGLAKAI---------------------ALRT-------GLPIVAVPTTY-AGSEMTPIWGET--E 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 624 THVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQAIKLTFDYLKSSVQE-ND 702
Cdd:cd08177 124 DGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADpSD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 703 KHSREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAKdpqkhtlfpkydffRADTDYAD 782
Cdd:cd08177 204 LEARSDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAP--------------AAPDAMAR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 783 IAKFLGlkgntteelVEALANAVYDLGCSIGIDMNLKSQGVTEEllhsTIDRMAELAFEDQctTANPkEPLISE-LKGII 861
Cdd:cd08177 270 LARALG---------GGDAAGGLYDLARRLGAPTSLRDLGMPED----DIDRAADLALANP--YPNP-RPVERDaLRALL 333
|
....
gi 1545705897 862 ERAY 865
Cdd:cd08177 334 ERAW 337
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
529-762 |
8.52e-36 |
|
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: 139.66 E-value: 8.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 529 PSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKaiwmffehpetsFFGAKQ--KFLDIRKRtyKISKPKNAKFICIPTT 606
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK------------LLALKGisPVLDLFDG--KIPLIKEKELIIVPTT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 607 SGTGSEVTPFAVITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVMASDYTRGLSLQA 686
Cdd:cd14860 128 CGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 687 IKLTFD-YLKssVQENDKHSREKMHN----ASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPHVIR-YNAK 760
Cdd:cd14860 208 IEMILEgYQE--IAEKGEEARFPLLGdfliASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKnYQEK 285
|
..
gi 1545705897 761 DP 762
Cdd:cd14860 286 NP 287
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
467-760 |
3.30e-33 |
|
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: 129.41 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 467 PPKVYFEENSVMYLTEM--DNVERAMIVCDPGmVNIGYTDIVEQVLRRRENqpqIKVFNEVEPNPSTHTVYKGLEMFMNF 544
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIkrRGFDRALVVSDEG-VVKGVGEKVADSLKKGLA---VAIFDFVGENPTFEEVKNAVERARAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 545 QPDTIIALGGGSAMDAAKAIwmffehpetsffgakqkfLDIRKRtykiskpkNAKFICIPTTSGTGSEVTPFAVITDSET 624
Cdd:cd07766 77 EADAVIAVGGGSTLDTAKAV------------------AALLNR--------GIPFIIVPTTASTDSEVSPKSVITDKGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 625 hvKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIEsyvsvmasdytrglslqaikltfdylkssvqendkh 704
Cdd:cd07766 131 --KNKQVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------ 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1545705897 705 sREKMHNASTMAGMAFANA-FLGISHSIAHKIGGEYGIPHGRTNAILLPHVIRYNAK 760
Cdd:cd07766 173 -LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVAND 228
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
61-415 |
4.21e-32 |
|
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: 128.89 E-value: 4.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 61 LAKLAYDETG--RGIYEDKAIKNLYASEYIWNSIKDNKTVGIIGEDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMI 138
Cdd:cd06534 36 LAALETLETGkpIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 139 AIKTGNPIIfaFHPSAQqsSKHAAKVILEAAIKAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSGMVKSAY--- 215
Cdd:cd06534 116 ALAAGNTVV--LKPSEL--TPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMkaa 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 216 -STGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEFKlhqTYFVNKNElqql 294
Cdd:cd06534 192 aENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV---TVLVDVDP---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 295 EDAIMNEdktavkpdivgksavniaklsgisvpektkllvaEIDGigkdyplsreklsPVLAMVTAKSTRHALQICEDTl 374
Cdd:cd06534 265 DMPIAQE----------------------------------EIFG-------------PVLPVIRFKDEEEAIALANDT- 296
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1545705897 375 kfgGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTPSAVGG 415
Cdd:cd06534 297 ---EYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG 334
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
521-806 |
5.90e-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: 104.27 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 521 VFNEVEPNPSTHTVYKGLEMFMNFQ---PDTIIALGGGSAMDAAKAIWMFFEHPETSffgAKQKFLDIRKR--TYKISkp 595
Cdd:cd08184 55 IFVDTTDEPKTDQIDALRAQIRAENdklPAAVVGIGGGSTMDIAKAVSNMLTNPGSA---ADYQGWDLVKNpgIYKIG-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 596 knakficIPTTSGTGSEVTPFAVITDSEthVKYPL-ADYALtPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSVM 674
Cdd:cd08184 130 -------VPTLSGTGAEASRTAVLTGPE--KKLGInSDYTV-FDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 675 ASDYTRGLSLQAIKLTFD-YLKSSVQENDKhsREKMHNASTMAGMAFANAFLGISHSIAHKIGGEYGIPHGRTNAILLPH 753
Cdd:cd08184 200 RNAFGDAYAEKALELCRDvFLSDDMMSPEN--REKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNV 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1545705897 754 VIRYnakdpqkhtlFPK-YDFFRADTDYADIAKFLGLKGNTTEELVEALANAVY 806
Cdd:cd08184 278 LEEF----------YPEgVKEFREMLEKQNITLPKGICKDLTDEQYEKMVAVTL 321
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
461-771 |
3.51e-16 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 81.38 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 461 MQWFKL--PPKVYFEENSVMYLT-EMDNVERAMIVCDPGMV-NIGYTDIVEQVLRRREnqpqIKVFNEVEPNPSTHTVYK 536
Cdd:PRK15138 1 MNNFNLhtPTRILFGKGAIAGLReQIPADARVLITYGGGSVkKTGVLDQVLDALKGMD----VLEFGGIEPNPTYETLMK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 537 GLEMFMNFQPDTIIALGGGSAMDAAKAIWMFFEHPETSffgAKQKFLDIRKRTYKISKPKNakfiCIPTTSGTGSEVTPF 616
Cdd:PRK15138 77 AVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENI---DPWHILETGGKEIKSAIPMG----SVLTLPATGSESNAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 617 AVITDSETHVKYPLADYALTPDIAIVDPQFVLSVPKDIAADTGMDVLTHAIESYVSV-----MASDYTRGLSLQAIKltf 691
Cdd:PRK15138 150 AVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYpvdakIQDRFAEGILLTLIE--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 692 DYLKSSVQENDKHSREKMHNASTMAgmafANAFLGI-------SHSIAHKIGGEYGIPHGRTNAILLPHVirYNAKDPQK 764
Cdd:PRK15138 227 EGPKALKEPENYDVRANVMWAATQA----LNGLIGAgvpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTK 300
|
....*..
gi 1545705897 765 HTLFPKY 771
Cdd:PRK15138 301 RAKLLQY 307
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
15-454 |
8.79e-15 |
|
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: 77.86 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 15 DEVTQMIDSlAEKGQEALKELSKKSQQEI-NDIVHQMSMatvdQHMHLAKLAYDETGRGIYE-----DKAIKNLYASEYI 88
Cdd:cd07094 21 ADAEEALAT-ARAGAENRRALPPHERMAIlERAADLLKK----RAEEFAKIIACEGGKPIKDarvevDRAIDTLRLAAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 89 WNSIKDNKTVGII--GEDKQKGLTyVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQQ--SSKHAAKV 164
Cdd:cd07094 96 AERIRGEEIPLDAtqGSDNRLAWT-IREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVV--LKPASKTplSALELAKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 165 ILEaaikAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGS--GMVKSAYSTGKP-ALGVGpGNVPTYIEKTAHIKR 241
Cdd:cd07094 173 LVE----AGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAavGEALRANAGGKRiALELG-GNAPVIVDRDADLDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 242 AVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEfklhqtyFVNKNELQQLEDAImnEDKTAVKPDIVGKSAVNI--- 318
Cdd:cd07094 248 AIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEA-------FVAAVKKLKVGDPL--DEDTDVGPLISEEAAERVerw 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 319 --------AKLSGISVPEKTKLLVAEIDGIGKDYPLSREK-LSPVLAMVTAKSTRHALQICEDTlkfgGLGHTAVIHTED 389
Cdd:cd07094 319 veeaveagARLLCGGERDGALFKPTVLEDVPRDTKLSTEEtFGPVVPIIRYDDFEEAIRIANST----DYGLQAGIFTRD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545705897 390 SQLQQKFGLKMKACRVLVNTPSAvggignMYNELIPSLTLGCGSYGRNSISHNVSavDLLNIKTI 454
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSA------FRTDWMPFGGVKESGVGREGVPYAME--EMTEEKTV 451
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
21-414 |
4.04e-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: 75.65 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 21 IDSLAEKGQEALKELSKKSQQEINDIVHQMSMAtVDQHMH-LAKLAYDETGRGIYE-----DKAIKNL-YASEYIwnsik 93
Cdd:pfam00171 31 VDAAIAAARAAFPAWRKTPAAERAAILRKAADL-LEERKDeLAELETLENGKPLAEargevDRAIDVLrYYAGLA----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 94 dNKTVG-IIGEDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFafHPSAQqsSKHAAKVILEAAIKA 172
Cdd:pfam00171 105 -RRLDGeTLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL--KPSEL--TPLTALLLAELFEEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 173 GAPKDCIQWIEIPSIEATKQLMNHKDIALVLATG----GSGMVKSAYSTGKPA---LGvgpGNVPTYIEKTAHIKRAVND 245
Cdd:pfam00171 180 GLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGstavGRHIAEAAAQNLKRVtleLG---GKNPLIVLEDADLDAAVEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 246 IIGSKTFDNGMICASEQVMVVDKEVYSDVVKEFK------------LHQTYF---VNKNELQQLEDAIMnedktavkpDI 310
Cdd:pfam00171 257 AVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVeaakklkvgdplDPDTDMgplISKAQLERVLKYVE---------DA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 311 VGKSAVniaKLSGISVPEKTKLLVAE--IDGIGKDYPLSREKL-SPVLAMVTAKSTRHALQICEDTlkfgGLGHTAVIHT 387
Cdd:pfam00171 328 KEEGAK---LLTGGEAGLDNGYFVEPtvLANVTPDMRIAQEEIfGPVLSVIRFKDEEEAIEIANDT----EYGLAAGVFT 400
|
410 420
....*....|....*....|....*..
gi 1545705897 388 EDSQLQQKFGLKMKACRVLVNTPSAVG 414
Cdd:pfam00171 401 SDLERALRVARRLEAGMVWINDYTTGD 427
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
12-418 |
4.06e-14 |
|
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: 75.46 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 12 SNKDEVTQMIDSlAEKGQEALKELSKKsqqEINDIVHQMSMATVDQHMHLAKLAYDETGRGIYE-----DKAIKNL-YAS 85
Cdd:cd07145 18 LSREEVREAIEV-AEKAKDVMSNLPAY---KRYKILMKVAELIERRKEELAKLLTIEVGKPIKQsrvevERTIRLFkLAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 86 EYIwnSIKDNKTVGIIG-EDKQKGLTY-VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFafHPSaqqsSKHAAK 163
Cdd:cd07145 94 EEA--KVLRGETIPVDAyEYNERRIAFtVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV--KPS----SNTPLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 164 VILEAAI--KAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATG----GSGMVKSAYSTGKP-ALGVGpGNVPTYIEKT 236
Cdd:cd07145 166 AIELAKIleEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKvALELG-GSDPMIVLKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 237 AHIKRAVNDIIGSKtFDN-GMICASEQVMVVDKEVYSDVVKEfklhqtyFVNKNELQQLEDAImnEDKTAVKPDIVGKSA 315
Cdd:cd07145 245 ADLERAVSIAVRGR-FENaGQVCNAVKRILVEEEVYDKFLKL-------LVEKVKKLKVGDPL--DESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 316 VNIAKLSGISVPEKTKLL--------------VAEIDgiGKDYPLSR-EKLSPVLAMVTAKSTRHALQICEDTlkfgGLG 380
Cdd:cd07145 315 ERMENLVNDAVEKGGKILyggkrdegsffpptVLEND--TPDMIVMKeEVFGPVLPIAKVKDDEEAVEIANST----EYG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1545705897 381 HTAVIHTEDSQLQQKFGLKMKACRVLVNTPSAV-------GGIGN 418
Cdd:cd07145 389 LQASVFTNDINRALKVARELEAGGVVINDSTRFrwdnlpfGGFKK 433
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-415 |
2.89e-13 |
|
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: 72.63 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 61 LAKLAYDETGRGIYE-----DKAIKNL-YASEYIwnsIKDNKTVGIIGEDKQKGLTyVAEPIGVICGVTPTTNPTSTTIF 134
Cdd:cd07078 40 LAALETLETGKPIEEalgevARAADTFrYYAGLA---RRLHGEVIPSPDPGELAIV-RREPLGVVGAITPWNFPLLLAAW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 135 KAMIAIKTGNPIIfaFHPSAQQSskHAAKVILEAAIKAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATG----GSGM 210
Cdd:cd07078 116 KLAPALAAGNTVV--LKPSELTP--LTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGstavGKAI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 211 VKSAYSTGKP---ALGvgpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEF-KLHQTYFV 286
Cdd:cd07078 192 MRAAAENLKRvtlELG---GKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLvERVKALKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 287 -NKNELQQLEDAIMNE---DKTavkpdivgKSAVNIAK------LSGISVPEKTKLLVAE---IDGIGKDYPLSREKL-S 352
Cdd:cd07078 269 gNPLDPDTDMGPLISAaqlDRV--------LAYIEDAKaegaklLCGGKRLEGGKGYFVPptvLTDVDPDMPIAQEEIfG 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1545705897 353 PVLAMVTAKSTRHALQICEDTlkFGGLghTAVIHTEDSQLQQKFGLKMKACRVLVNTPSAVGG 415
Cdd:cd07078 341 PVLPVIPFKDEEEAIELANDT--EYGL--AAGVFTRDLERALRVAERLEAGTVWINDYSVGAE 399
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
135-414 |
3.68e-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: 69.38 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 135 KAMIAIKTGNPIIFafHPSAQQSSkhAAKVILEAAIKAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATG----GSGM 210
Cdd:COG1012 161 KLAPALAAGNTVVL--KPAEQTPL--SALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGstavGRRI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 211 VKSAYSTGKPA---LGvgpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEFklhqtyfvn 287
Cdd:COG1012 237 AAAAAENLKRVtleLG---GKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERL--------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 288 KNELQQL-------EDAIMN--EDKTAVkpDIVgKSAVNIAK------LSGISVPEKTKLLVAE---IDGIGKDYPLSRE 349
Cdd:COG1012 305 VAAAKALkvgdpldPGTDMGplISEAQL--ERV-LAYIEDAVaegaelLTGGRRPDGEGGYFVEptvLADVTPDMRIARE 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1545705897 350 KL-SPVLAMVTAKSTRHALQICEDTLkfGGLghTAVIHTEDSQLQQKFGLKMKACRVLVNTPSAVG 414
Cdd:COG1012 382 EIfGPVLSVIPFDDEEEAIALANDTE--YGL--AASVFTRDLARARRVARRLEAGMVWINDGTTGA 443
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
479-744 |
5.32e-12 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 66.94 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 479 YLTEMDnVERAMIVCDPGMVNIgYTDIVEQVLRRRENQPQikVFNEVEPNPSTHTVYKGLEMFMNFQPDTIIALGGGSAM 558
Cdd:pfam13685 13 YLAELG-FRRVALVADANTYAA-AGRKVAESLKRAGIEVE--TRLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 559 DAAKAIwmffehpetsffgakqkfldirkrTYKISKPknakFICIPTTSGTGSEVTPFAVITdsETHVKYPLadYALTPD 638
Cdd:pfam13685 89 DLAKYA------------------------AFKLGKP----FISVPTAASNDGFASPGASLT--VDGKKRSI--PAAAPF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 639 IAIVDPQFVLSVPKD-IAADTGmDvlthAIESYVSVM------ASDYTRGLSLQAIKLTFDYLKSSVQenDKHSRE---K 708
Cdd:pfam13685 137 GVIADTDVIAAAPRRlLASGVG-D----LLAKITAVAdwelahAEEVAAPLALLSAAMVMNFADRPLR--DPGDIEalaE 209
|
250 260 270
....*....|....*....|....*....|....*...
gi 1545705897 709 MHNASTMAGMAFANAFLGISHSIAHKIGGEYGIP--HG 744
Cdd:pfam13685 210 LLSALAMGGAGSSRPASGSEHLISHALDMIAPKQalHG 247
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
115-251 |
5.66e-12 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 68.61 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 115 PIGVIcGVtpttnptsttIFK---------AMIAIKTGNPIIF-----AFHpsaqqSSKHAAKVILEAAIKAGAPKDCIQ 180
Cdd:cd07079 109 PLGVI-GI----------IYEsrpnvtvdaAALCLKSGNAVILrggseALH-----SNRALVEIIQEALEEAGLPEDAVQ 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1545705897 181 WIEIPSIEATKQLMN-HKDIALVLATGGSGMVKS-AYSTGKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKT 251
Cdd:cd07079 173 LIPDTDREAVQELLKlDDYIDLIIPRGGAGLIRFvVENATIPVIKHGDGNCHVYVDESADLEMAVRIVVNAKT 245
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
462-744 |
1.38e-09 |
|
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: 60.95 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 462 QWFKLPPKVYFEENSVMYLTEM--DNVERAMIVCDPGMVNIgYTDIVEQVLRRRENQPQIKVFNEvepNPSTHTVYKGLE 539
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYlaDLGKRALIITGPTALKA-AGDRLEESLEDAGIEVEVEVFGG---ECSEEEIERLAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 540 MFMNFQPDTIIALGGGSAMDAAKAIwmffehpetsffgAkqkfldirkrtYKISKPknakFICIPTTSGTGSEVTPFAVI 619
Cdd:COG0371 77 EAKEQGADVIIGVGGGKALDTAKAV-------------A-----------YRLGLP----VVSVPTIASTDAPASPLSVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 620 -TDSETHVKYPLadYALTPDIAIVDPQFVLSVPKD-IAAdtGM-DVLTHAIESYVSVMA---------SDYTRGLSLQAI 687
Cdd:COG0371 129 yTEDGAFDGYSF--LAKNPDLVLVDTDIIAKAPVRlLAA--GIgDALAKWYEARDWSLAhrdlageyyTEAAVALARLCA 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1545705897 688 KLTFDYLKSSVQENDKHSR----EKMHNAST-MAGMAFANAF----LGISHSIAH---KIGGEYGIPHG 744
Cdd:COG0371 205 ETLLEYGEAAIKAVEAGVVtpalERVVEANLlLSGLAMGIGSsrpgSGAAHAIHNgltALPETHHALHG 273
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
115-251 |
6.63e-09 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 58.93 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 115 PIGVIcGVtpttnptsttIFK---------AMIAIKTGNPIIF-----AFHpsaqqSSKHAAKVILEAAIKAGAPKDCIQ 180
Cdd:PRK00197 115 PLGVI-GV----------IYEsrpnvtvdaAALCLKSGNAVILrggseAIH-----SNRALVAVIQEALEEAGLPADAVQ 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545705897 181 WIEIPSIEATKQLMNHKD-IALVLATGGSGMVK--SAYSTgKPALGVGPGNVPTYIEKTAHIKRAVNDIIGSKT 251
Cdd:PRK00197 179 LVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRrvVENAT-VPVIEHGDGICHIYVDESADLDKALKIVLNAKT 251
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
114-279 |
3.81e-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: 56.89 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 114 EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSaqQSSKHAAKVILEAAIKAGAPKDCIQWIEIPSIEATKQL 193
Cdd:cd07088 132 VPIGVVAGILPWNFPFFLIARKLAPALVTGNTIV--IKPS--EETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDAL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 194 MNHKDIALVLATG--GSG---MVKSAYSTGKPALGVGpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDK 268
Cdd:cd07088 208 VAHPKVGMISLTGstEAGqkiMEAAAENITKVSLELG-GKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHE 286
|
170
....*....|.
gi 1545705897 269 EVYSDVVKEFK 279
Cdd:cd07088 287 DIYDEFMEKLV 297
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
219-408 |
7.08e-07 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 52.69 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 219 KPALGVGpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEFKLHqtyfvnkneLQQLEDAI 298
Cdd:cd07151 236 KVALELG-GNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVER---------VKALPYGD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 299 MNEDKTAVKPDIVGKSAVNIAKLSGISVPEKTKLLV-AEIDG----------IGKDYPLSREKL-SPVLAMVTAKSTRHA 366
Cdd:cd07151 306 PSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVgGEAEGnvleptvlsdVTNDMEIAREEIfGPVAPIIKADDEEEA 385
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1545705897 367 LQICEDTlkfgGLGHTAVIHTEDSQLQQKFGLKMKACRVLVN 408
Cdd:cd07151 386 LELANDT----EYGLSGAVFTSDLERGVQFARRIDAGMTHIN 423
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
112-418 |
1.52e-06 |
|
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: 51.56 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 112 VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEaaikAGAPKDCIQWIEIPSIEATK 191
Cdd:cd07150 116 VRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEE----AGLPKGVFNVVTGGGAEVGD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 192 QLMNHKDIALVLATGGSGM-----VKSAYSTGKPALGVGpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVV 266
Cdd:cd07150 192 ELVDDPRVRMVTFTGSTAVgreiaEKAGRHLKKITLELG-GKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 267 DKEVYSDVVKEfklhqtyFVNKNElqQLEDAIMNEDKTAVKPDIVGKSAVNIAKLSGISVPEKTKLLVAE---------- 336
Cdd:cd07150 271 EEPVYDEFVKK-------FVARAS--KLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGkydgnfyqpt 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 337 -IDGIGKDYPLSREK-LSPVLAMVTAKSTRHALQICEDTLkfggLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTPS--- 411
Cdd:cd07150 342 vLTDVTPDMRIFREEtFGPVTSVIPAKDAEEALELANDTE----YGLSAAILTNDLQRAFKLAERLESGMVHINDPTild 417
|
330
....*....|.
gi 1545705897 412 ----AVGGIGN 418
Cdd:cd07150 418 eahvPFGGVKA 428
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
102-279 |
1.76e-06 |
|
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: 51.44 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 102 GEDKQkGLTYvAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQqsSKHAAKVILEAAIKAGAPKDCIQW 181
Cdd:cd07149 112 GEGRI-GFTI-REPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV--LKPASQ--TPLSALKLAELLLEAGLPKGALNV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 182 IEIPSIEATKQLMNHKDIALVLATGGsgmvksaYSTG----------KPALGVGpGNVPTYIEKTAHIKRAVNDIIGSKT 251
Cdd:cd07149 186 VTGSGETVGDALVTDPRVRMISFTGS-------PAVGeaiarkaglkKVTLELG-SNAAVIVDADADLEKAVERCVSGAF 257
|
170 180
....*....|....*....|....*...
gi 1545705897 252 FDNGMICASEQVMVVDKEVYSDVVKEFK 279
Cdd:cd07149 258 ANAGQVCISVQRIFVHEDIYDEFLERFV 285
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
139-279 |
4.17e-06 |
|
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: 50.30 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 139 AIKTGNPIIFAfhPSaqQSSKHAAKVILEAaIKAGAPKDCIQWI--EIPsiEATKqLMNHK-DiaLVLATGgSGMV---- 211
Cdd:cd07135 132 AIAAGCTVVLK--PS--ELTPHTAALLAEL-VPKYLDPDAFQVVqgGVP--ETTA-LLEQKfD--KIFYTG-SGRVgrii 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 212 -KSAYSTGKP-ALGVGpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEFK 279
Cdd:cd07135 201 aEAAAKHLTPvTLELG-GKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELK 269
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
21-278 |
4.47e-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: 50.05 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 21 IDSLAEKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGRGI----YE-DKAIKNLYASEYIWNSIK-- 93
Cdd:cd07146 20 EEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLkdtrYEvGRAADVLRFAAAEALRDDge 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 94 ----DNKTVGiigeDKQKGLTyVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQqsSKHAAKVILEAA 169
Cdd:cd07146 100 sfscDLTANG----KARKIFT-LREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV--LKPSEK--TPLSAIYLADLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 170 IKAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSGMVKS-AYSTG--KPALGVGpGNVPTYIEKTAHIKRAVNDI 246
Cdd:cd07146 171 YEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAiAATAGykRQLLELG-GNDPLIVMDDADLERAATLA 249
|
250 260 270
....*....|....*....|....*....|..
gi 1545705897 247 IGSKTFDNGMICASEQVMVVDKEVYSDVVKEF 278
Cdd:cd07146 250 VAGSYANSGQRCTAVKRILVHESVADEFVDLL 281
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
133-412 |
2.07e-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: 48.01 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 133 IFKAMIAIKTGNPIIFAFHPSAQQSskhaAKVILEAAIKAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSGM-- 210
Cdd:cd07097 153 AWKIAPALAYGNTVVFKPAELTPAS----AWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVgr 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 211 ---VKSAYSTGKPALGVGPGNvPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKefKLHQtyfvn 287
Cdd:cd07097 229 riaAAAAARGARVQLEMGGKN-PLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVE--ALVE----- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 288 knELQQLE--DAImnEDKTAVKPdIVGK-------SAVNIAKLSGIS-------VPEKTK---LLVAEIDGIGKDYPLSR 348
Cdd:cd07097 301 --RTKALKvgDAL--DEGVDIGP-VVSErqlekdlRYIEIARSEGAKlvyggerLKRPDEgyyLAPALFAGVTNDMRIAR 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545705897 349 EKL-SPVLAMVTAKSTRHALQICEDTlKFgglGHTAVIHTEDSQLQQKFGLKMKACRVLVNTPSA 412
Cdd:cd07097 376 EEIfGPVAAVIRVRDYDEALAIANDT-EF---GLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTA 436
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
114-279 |
9.81e-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: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 114 EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFafhpsaqQSSKHAAKVIL---EAAIKAGAPKDCIQWIEiPSIEAT 190
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVI-------KPSEFTPLTLLrvaELAKEAGIPDGVLNVVN-GKGAVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 191 KQLMNHKDIALVLATG----GSGMVKSAYSTGKPA-LGVGPGNvPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMV 265
Cdd:cd07113 213 AQLISHPDVAKVSFTGsvatGKKIGRQAASDLTRVtLELGGKN-AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFY 291
|
170
....*....|....
gi 1545705897 266 VDKEVYSDVVKEFK 279
Cdd:cd07113 292 VHRSKFDELVTKLK 305
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
15-279 |
1.67e-04 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 45.28 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 15 DEVTQMIDSlAEKGQEALKELSKKSQQEINDIVHQMSMATVDQhmhLAKLAYDETGRGIYEDKAiKNLYASEYI-WNSIK 93
Cdd:PRK11241 48 DETRAAIDA-ANRALPAWRALTAKERANILRRWFNLMMEHQDD---LARLMTLEQGKPLAEAKG-EISYAASFIeWFAEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 94 DNKTVG--IIGEDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQqsSKHAAKVILEAAIK 171
Cdd:PRK11241 123 GKRIYGdtIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMV--LKPASQ--TPFSALALAELAIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 172 AGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSG-----MVKSAYSTGKPALGVGpGNVPTYIEKTAHIKRAVNDI 246
Cdd:PRK11241 199 AGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEigrqlMEQCAKDIKKVSLELG-GNAPFIVFDDADLDKAVEGA 277
|
250 260 270
....*....|....*....|....*....|...
gi 1545705897 247 IGSKTFDNGMICASEQVMVVDKEVYSDVVKEFK 279
Cdd:PRK11241 278 LASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQ 310
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
139-298 |
6.83e-04 |
|
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: 43.00 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 139 AIKTGNPIIFafHPSAQQSSkhAAKVILEAAIKAGAPKDCIQWIeIPSIEATKQLMNHKDIALVLATGGS-GMVKSAYST 217
Cdd:cd07102 140 ALLAGNAVIL--KHSPQTPL--CGERFAAAFAEAGLPEGVFQVL-HLSHETSAALIADPRIDHVSFTGSVaGGRAIQRAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 218 GKPALGVG---PGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSD-------VVKEFKL-----HQ 282
Cdd:cd07102 215 AGRFIKVGlelGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAfveafvaVVKGYKLgdpldPS 294
|
170 180
....*....|....*....|...
gi 1545705897 283 TYF---VNK----NELQQLEDAI 298
Cdd:cd07102 295 TTLgpvVSAraadFVRAQIADAI 317
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
133-276 |
7.33e-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: 42.95 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 133 IFKAMI--AIKTGNPIIFAfhPsAQQSSKHAAKVIlEAAIKAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGsgm 210
Cdd:cd07125 183 IFTGQIaaALAAGNTVIAK--P-AEQTPLIAARAV-ELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGS--- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 211 vksaYSTGKPALGVGPGN----VP----------TYIEKTAHIKRAVNDIIGSkTFDN-GMICASEQVMVVDKEVYSDVV 275
Cdd:cd07125 256 ----TETAKLINRALAERdgpiLPliaetggknaMIVDSTALPEQAVKDVVQS-AFGSaGQRCSALRLLYLQEEIAERFI 330
|
.
gi 1545705897 276 K 276
Cdd:cd07125 331 E 331
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
139-408 |
9.70e-04 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 42.56 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 139 AIKTGNPIIFAfhPSAQQSSKHAakVILEAAIKAGAPKDCIQWIEIPSIEATKQLMNHKDIALVLATGGSGM---VKSAY 215
Cdd:cd07082 165 ALIMGNTVVFK--PATQGVLLGI--PLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVgnrLKKQH 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 216 STGKPALGVGPGNvPTYIEKTAHIKRAVNDII-GSKTFdNGMICASEQVMVVDKEVYSDVVKEFklhqtyfvnKNELQQL 294
Cdd:cd07082 241 PMKRLVLELGGKD-PAIVLPDADLELAAKEIVkGALSY-SGQRCTAIKRVLVHESVADELVELL---------KEEVAKL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 295 EDAIMNEDKTAVKPDIVGKSAVNIAKLSGISVpEKTKLLVAEIDGIGKDY--PL------------SREKLSPVLAMVTA 360
Cdd:cd07082 310 KVGMPWDNGVDITPLIDPKSADFVEGLIDDAV-AKGATVLNGGGREGGNLiyPTlldpvtpdmrlaWEEPFGPVLPIIRV 388
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1545705897 361 KSTRHALQICEDTlKFgglGHTAVIHTEDSQLQQKFGLKMKACRVLVN 408
Cdd:cd07082 389 NDIEEAIELANKS-NY---GLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
30-420 |
1.18e-03 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 42.22 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 30 EALKELSKKSqqeiNDIVHqMSMATVDQHMHLAklayDETGRGIYEDKAIKNLYASEYIWNSIKDNKtvgiiGEDKQKGL 109
Cdd:cd07084 29 RIIQRLAAKS----YDIAA-GAVLVTGKGWMFA----ENICGDQVQLRARAFVIYSYRIPHEPGNHL-----GQGLKQQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 110 TYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAIKAGAPKDCIQWieipSIEA 189
Cdd:cd07084 95 HGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLING----DGKT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 190 TKQLMNHKDIALVLATGGSGMVKSAYSTGKPA-LGVGPGNV-PTYIEKTAHIKRAVND-IIGSKTFDNGMICASEQVMVV 266
Cdd:cd07084 171 MQALLLHPNPKMVLFTGSSRVAEKLALDAKQArIYLELAGFnWKVLGPDAQAVDYVAWqCVQDMTACSGQKCTAQSMLFV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 267 ----DKEVYSDVVKEfKLHQ--------TYFVNKNELQQLEdAIMNEDKTAVKPDivGKSAVNIAKLSGISVPEKTKLLV 334
Cdd:cd07084 251 penwSKTPLVEKLKA-LLARrkledlllGPVQTFTTLAMIA-HMENLLGSVLLFS--GKELKNHSIPSIYGACVASALFV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 335 AeIDGIGKDYPL-SREKLSPVLAMVTAKSTRHALQICEDTLKFGGLghTAVIH-TEDSQLQQKFGLKMKACRVLVNTPSA 412
Cdd:cd07084 327 P-IDEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSL--TAAIYsNDPIFLQELIGNLWVAGRTYAILRGR 403
|
....*...
gi 1545705897 413 VGGIGNMY 420
Cdd:cd07084 404 TGVAPNQN 411
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
109-413 |
1.19e-03 |
|
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: 42.43 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 109 LTY-VAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQQSSkhAAKVILEAAIKAGAPKDCIQWIEIPSI 187
Cdd:cd07115 110 LNYtVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVV--LKPAELTPL--SALRIAELMAEAGFPAGVLNVVTGFGE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 188 EATKQLMNHKDIALVLATG----GSGMVKSAYSTGKP-ALGVGpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQ 262
Cdd:cd07115 186 VAGAALVEHPDVDKITFTGstavGRKIMQGAAGNLKRvSLELG-GKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 263 VMVVDKEVYSDVVKEfklhqtyFVNKNELQQLEDAImnEDKTAVKPDIVGK------SAVNIAKLSGISV------PEKT 330
Cdd:cd07115 265 RLLVHESIYDEFLER-------FTSLARSLRPGDPL--DPKTQMGPLVSQAqfdrvlDYVDVGREEGARLltggkrPGAR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 331 KLLV--AEIDGIGKDYPLSREKL-SPVLAMVTAKSTRHALQICEDTLKfgGLGhtAVIHTEDSQLQQKFGLKMKACRVLV 407
Cdd:cd07115 336 GFFVepTIFAAVPPEMRIAQEEIfGPVVSVMRFRDEEEALRIANGTEY--GLA--AGVWTRDLGRAHRVAAALKAGTVWI 411
|
....*.
gi 1545705897 408 NTPSAV 413
Cdd:cd07115 412 NTYNRF 417
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
115-411 |
1.23e-03 |
|
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: 42.33 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 115 PIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSaqQSSKHAAKVILEAAIKAGAPKDCIQWIEIPSIEATKQLM 194
Cdd:cd07131 135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVV--FKPA--EDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 195 NHKDIALVLATG----GSGMVKSAYSTGKP-ALGVGPGNvPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKE 269
Cdd:cd07131 211 EHPDVDVVSFTGstevGERIGETCARPNKRvALEMGGKN-PIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHES 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 270 VYsdvvKEFKlhqTYFVNKNELQQLEDAimNEDKTAVKPDIVGKSA------VNIAKLSGISV-----------PEKTKL 332
Cdd:cd07131 290 VY----DEFL---KRFVERAKRLRVGDG--LDEETDMGPLINEAQLekvlnyNEIGKEEGATLllggerltgggYEKGYF 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 333 LVAEI-DGIGKDYPLSREKL-SPVLAMVTAKSTRHALQICEDTlkfgGLGHTAVIHTEDSQLQQKFGLKMKACRVLVNTP 410
Cdd:cd07131 361 VEPTVfTDVTPDMRIAQEEIfGPVVALIEVSSLEEAIEIANDT----EYGLSSAIYTEDVNKAFRARRDLEAGITYVNAP 436
|
.
gi 1545705897 411 S 411
Cdd:cd07131 437 T 437
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
79-304 |
1.31e-03 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 42.32 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 79 IKNLYAseyiWNSIKDNKTVGIIGEDKQkgltYVA-EPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIFAfhPSaqQS 157
Cdd:PTZ00381 80 LKHLDE----YLKPEKVDTVGVFGPGKS----YIIpEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLK--PS--EL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 158 SKHAAKVILEAAIKAgAPKDCIQWIEIPSIEATKQLMNHKDiaLVLATG----GSGMVKSAYSTGKPA---LGvgpGNVP 230
Cdd:PTZ00381 148 SPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLKEPFD--HIFFTGsprvGKLVMQAAAENLTPCtleLG---GKSP 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1545705897 231 TYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEFKLHQTYFVNKNELQQlED--AIMNEDKT 304
Cdd:PTZ00381 222 VIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKS-EDysRIVNEFHT 296
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
466-642 |
1.72e-03 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 41.38 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 466 LPPKVYFEENSV----MYLTEMDNVERAMIVCDPGMVNIgYTDIVEQVL------RRRENQPQIKVFNEVEpnpsthtvy 535
Cdd:cd08173 1 LPRNVVVGHGAInkigEVLKKLLLGKRALIITGPNTYKI-AGKRVEDLLessgveVVIVDIATIEEAAEVE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 536 KGLEMFMNFQPDTIIALGGGSAMDAAKAIwmffehpetsffgakqkfldirkrTYKISKPknakFICIPTTSGTGSEVTP 615
Cdd:cd08173 71 KVKKLIKESKADFIIGVGGGKVIDVAKYA------------------------AYKLNLP----FISIPTSASHDGIASP 122
|
170 180
....*....|....*....|....*..
gi 1545705897 616 FAVITDSETHVKYPladyALTPdIAIV 642
Cdd:cd08173 123 FASIKGGDKPYSIK----AKAP-IAII 144
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-279 |
3.87e-03 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 40.52 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 21 IDSLAEKGQEALKELSKKSQQEINDIVHQMSMATVDQHMHLAKLAYDETGRGIYEDKAIKNLYASE---YIWNSIK-DNK 96
Cdd:cd07117 40 VDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADhfrYFAGVIRaEEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 97 TVGIIgeDKQKGLTYVAEPIGVICGVTPTTNPTSTTIFKAMIAIKTGNPIIfaFHPSAQQSSKhaakvILEAA--IKAGA 174
Cdd:cd07117 120 SANMI--DEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVV--IKPSSTTSLS-----LLELAkiIQDVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 175 PKDCIQWIEIPSIEATKQLMNHKDIALVLATG----GSGMVKSAYSTGKPA---LGVGPGNVptyIEKTAHIKRAVNDII 247
Cdd:cd07117 191 PKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGstevGRDVAIAAAKKLIPAtleLGGKSANI---IFDDANWDKALEGAQ 267
|
250 260 270
....*....|....*....|....*....|..
gi 1545705897 248 GSKTFDNGMICASEQVMVVDKEVYSDVVKEFK 279
Cdd:cd07117 268 LGILFNQGQVCCAGSRIFVQEGIYDEFVAKLK 299
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
487-564 |
6.33e-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: 6.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1545705897 487 ERAMIVCDPGMVNIgYTDIVEQVLRRRENQPQIKVFN-EVepnpSTHTVYKGLEMFMNFQPDTIIALGGGSAMDAAKAI 564
Cdd:cd08170 23 KKALVIADPFVLDL-VGERLEESLEKAGLEVVFEVFGgEC----SREEIERLAAIARANGADVVIGIGGGKTIDTAKAV 96
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
135-279 |
6.45e-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: 39.85 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 135 KAMIAIKTGNPIIFAFHPSAQQSSKHAAKVILEAAIKAGAPKDCIQWIeIPSIEATKQLMNHKDIALVLATGGSGM---- 210
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV-TGGGDGGELLVHDPRVPLVSFTGSTEVgrrv 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705897 211 -VKSAYSTGKPALGVGpGNVPTYIEKTAHIKRAVNDIIGSKTFDNGMICASEQVMVVDKEVYSDVVKEFK 279
Cdd:cd07086 232 gETVARRFGRVLLELG-GNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLV 300
|
|
| |
