|
Name |
Accession |
Description |
Interval |
E-value |
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
4-367 |
4.66e-178 |
|
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: 497.40 E-value: 4.66e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 4 FSLQTRLYSGQGSLDVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADNRISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:cd08180 1 FSLKTKIYSGEDSLERLKELKGKRVFIVTDPFMVKSGMVDKVTDELDKSNEVEIFSDVVPDPSIEVVAKGLAKILEFKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAIVWFSRQF--GIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDMAILDPTLV 161
Cdd:cd08180 81 TIIALGGGSAIDAAKAIIYFALKQkgNIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLPDIAILDPELV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 162 VSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLAGMAFSQAGLG 241
Cdd:cd08180 161 KSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASCMAGIAFNNAGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 242 INHAIAHQLGGQFHLPHGLANALLLTHVIHFnardpraakryarfakachlcpdnandttalnaLIHHIELLKKQCALPA 321
Cdd:cd08180 241 INHSLAHALGGRFHIPHGRANAILLPYVIEF---------------------------------LIAAIRRLNKKLGIPS 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 851901932 322 FIDALKDEKHTWSQRIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08180 288 TLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-370 |
4.60e-149 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 425.69 E-value: 4.60e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 1 MKSFSLQTRLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIA 75
Cdd:COG1454 2 MFTFRLPTRIVFGAGALaelgEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGiEVVVFDDVEPNPTVETVEAGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 76 QMQSLQPDVVIGFGGGSALDAAKAIVWFSRQ-------FGIEIET-----CVAIPTTSGTGSEVTSACVISDPDKGIKYP 143
Cdd:COG1454 82 AAREFGADVVIALGGGSAIDAAKAIALLATNpgdledyLGIKKVPgpplpLIAIPTTAGTGSEVTPFAVITDPETGVKKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 144 LFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGK 223
Cdd:COG1454 162 IADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 224 MHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLcPDNANDTTAL 303
Cdd:COG1454 242 MALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNA--PAAPERYAEIARALGL-DVGLSDEEAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851901932 304 NALIHHIELLKKQCALPAFIDALK-DEKHtwsqrIPSMVQAALADVTLQTNPRVADASAIQELLEELL 370
Cdd:COG1454 319 EALIEAIRELLRDLGIPTRLSELGvTEED-----LPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
3-367 |
3.07e-135 |
|
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: 390.78 E-value: 3.07e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 3 SFSLQTRLYSGQGSLDVLKRFKNKHIWVICD-SFLARSPLIEKLRNTL-PADNRISIFSDITPDPTIGTVVQGIAQMQSL 80
Cdd:cd08179 1 RFFVPRDIYFGEGALEYLKTLKGKRAFIVTGgGSMKRNGFLDKVEDYLkEAGMEVKVFEGVEPDPSVETVEKGAEAMREF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 81 QPDVVIGFGGGSALDAAKAIVWF-----------SRQFGIEIET----CVAIPTTSGTGSEVTSACVISDPDKGIKYPLF 145
Cdd:cd08179 81 EPDWIIAIGGGSVIDAAKAMWVFyeypeltfedaLVPFPLPELRkkarFIAIPSTSGTGSEVTRASVITDTEKGIKYPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 146 NNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMH 225
Cdd:cd08179 161 SFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 226 NASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNARDPRAAKRYARFAKAchlcpdnANDTTALNA 305
Cdd:cd08179 241 NASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALLIG-------LTDEELVED 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851901932 306 LIHHIELLKKQCALP-AFIDALKDEKhTWSQRIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08179 314 LIEAIEELNKKLGIPlSFKEAGIDED-EFFAKLDEMAENAMNDACTGTNPRKPTVEEMKELLK 375
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-366 |
2.95e-129 |
|
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: 375.25 E-value: 2.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQP 82
Cdd:cd08551 2 TRIVFGAGALarlgEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGiEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 83 DVVIGFGGGSALDAAKAI------------VWFSRQFGIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALY 150
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIavlatnggsirdYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 151 PDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTL 230
Cdd:cd08551 162 PDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 231 AGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALNALIHHI 310
Cdd:cd08551 242 AGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNL--PACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 851901932 311 ELLKKQCALPAFIDALKDEKHtwsqRIPSMVQAALADVTLQTN-PRVADASAIQELL 366
Cdd:cd08551 320 RELLRDLGIPTSLSELGVTEE----DIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
26-367 |
4.65e-128 |
|
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: 373.06 E-value: 4.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 26 KHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQPDVVIGFGGGSALDAAKaIVWF- 103
Cdd:cd08178 24 KRAFIVTDRVLYKLGYVDKVLDVLEARGvETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAK-IMWLf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 104 ------------SRQFGI-----------EIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDMAILDPTL 160
Cdd:cd08178 103 yehpetkfedlaQRFMDIrkrvykfpklgKKAKLVAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIVDPEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 161 VVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLAGMAFSQAGL 240
Cdd:cd08178 183 VMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFANAFL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 241 GINHAIAHQLGGQFHLPHGLANALLLTHVIHFNARD-------------PRAAKRYARFAKACHLcpDNANDTTALNALI 307
Cdd:cd08178 263 GICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDpptkqaafpqykyYVAKERYAEIADLLGL--GGKTPEEKVESLI 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 308 HHIELLKKQCALPAFIDALKDEKHTWSQRIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08178 341 KAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISELKEILL 400
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-362 |
6.76e-121 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 353.45 E-value: 6.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSLDVLKRF---KNKHIWVICDSFLARSPLIEKLRNTL-PADNRISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:pfam00465 2 TRIVFGAGALAELGEElkrLGARALIVTDPGSLKSGLLDKVLASLeEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAIVWFSRQFGIEIETC------------VAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYP 151
Cdd:pfam00465 82 VIIAVGGGSVIDTAKAIALLLTNPGDVWDYLggkpltkpalplIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 152 DMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLA 231
Cdd:pfam00465 162 DLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLASTLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 232 GMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNAndttALNALIHHIE 311
Cdd:pfam00465 242 GLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNA--PAAPEKLAQLARALGEDSDEE----AAEEAIEALR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 851901932 312 LLKKQCALPAFIDALKDEKHtwsqRIPSMVQAALADVTLQTNPRVADASAI 362
Cdd:pfam00465 316 ELLRELGLPTTLSELGVTEE----DLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
1-367 |
1.11e-120 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 368.74 E-value: 1.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 1 MKSFSLQTRLYSGQGSLDVLKR--FKNKHIWVICDSFLARSPLIEKLRNTL---PADNRISIFSDITPDPTIGTVVQGIA 75
Cdd:PRK13805 454 MQWFKVPKKIYFERGSLPYLLDelDGKKRAFIVTDRFMVELGYVDKVTDVLkkrENGVEYEVFSEVEPDPTLSTVRKGAE 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 76 QMQSLQPDVVIGFGGGSALDAAKaIVWF-------------SRQFGIEIETC-----------VAIPTTSGTGSEVTSAC 131
Cdd:PRK13805 534 LMRSFKPDTIIALGGGSPMDAAK-IMWLfyehpetdfedlaQKFMDIRKRIYkfpklgkkaklVAIPTTSGTGSEVTPFA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 132 VISDPDKGIKYPLFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVA 211
Cdd:PRK13805 613 VITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRS 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 212 VSKG--DCLAtRGKMHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNARDP------------ 277
Cdd:PRK13805 693 YKNGakDPEA-REKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPpkqaafpqyeyp 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 278 RAAKRYARFAKACHLCPDnaNDTTALNALIHHIELLKKQCALPAFIDALKDEKHTWSQRIPSMVQAALADVTLQTNPRVA 357
Cdd:PRK13805 772 RADERYAEIARHLGLPGS--TTEEKVESLIKAIEELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYP 849
|
410
....*....|
gi 851901932 358 DASAIQELLE 367
Cdd:PRK13805 850 LISELKEILL 859
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-369 |
6.93e-111 |
|
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: 328.66 E-value: 6.93e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 7 QTRLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQ 81
Cdd:cd08189 5 EPELFEGAGSLlqlpEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGiEYVVFDGVVPDPTIDNVEEGLALYKENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 82 PDVVIGFGGGSALDAAKAI--------VWFSRQFGI-----EIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNA 148
Cdd:cd08189 85 CDAIIAIGGGSVIDCAKVIaaraanpkKSVRKLKGLlkvrkKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 149 LYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNAS 228
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLAS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 229 TLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALNALIH 308
Cdd:cd08189 245 YYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYG--PAAEKRLAELADAAGLGDSGESDSEKAEAFIA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851901932 309 HIELLKKQCALPAFIDALKDEKhtwsqrIPSMVQAALAdvtlQTN-----PRVADASAIQELLEEL 369
Cdd:cd08189 323 AIRELNRRMGIPTTLEELKEED------IPEIAKRALK----EANplypvPRIMDRKDCEELLRKV 378
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
11-367 |
5.35e-110 |
|
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: 326.39 E-value: 5.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 11 YSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQPDVV 85
Cdd:cd08188 10 LFGPGCLkeigDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGiEYVIFDGVQPNPTVTNVNEGLELFKENGCDFI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 86 IGFGGGSALDAAKAIvwfsrqfGI------EIET-------------CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFN 146
Cdd:cd08188 90 ISVGGGSAHDCAKAI-------GIlatnggEIEDyegvdkskkpglpLIAINTTAGTASEVTRFAVITDEERHVKMVIVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 147 NALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHN 226
Cdd:cd08188 163 WNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENMAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 227 ASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALNAL 306
Cdd:cd08188 243 AQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNL--PACPERFADIARALGENTEGLSDEEAAEAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851901932 307 IHHIELLKKQCALPAFIDAL--KDEKhtwsqrIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08188 321 IEAIRKLSRRVGIPSGLKELgvKEED------FPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-366 |
1.28e-108 |
|
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: 322.64 E-value: 1.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 9 RLYSGQGSLDVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQPDVVIG 87
Cdd:cd14862 8 KIVFGEDALSHLEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGfEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 88 FGGGSALDAAKAIVWFSRQFGIEIETC--------------VAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDM 153
Cdd:cd14862 88 LGGGSVMDAAKAAWVLYERPDLDPEDIspldllglrkkaklIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 154 AILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLAGM 233
Cdd:cd14862 168 AILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIAGL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 234 AFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNARdpRAAKRYARFAKACHLCPDNAndtTALNALIHHIELL 313
Cdd:cd14862 248 AFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAK--VTDERYDLLKLLGIEARDEE---EALKKLVEAIREL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 851901932 314 KKQCALPAFIDALKDEKHTWSQRIPSMVQAALADVTLQTNPRVADASAIQELL 366
Cdd:cd14862 323 YKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-370 |
4.21e-107 |
|
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: 319.10 E-value: 4.21e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 3 SFSLQTRLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLpADNRIS--IFSDITPDPTIGTVVQGIAQ 76
Cdd:cd14863 1 TYSQLTPVIFGAGAVeqigELLKELGCKKVLLVTDKGLKKAGIVDKIIDLL-EEAGIEvvVFDDVEPDPPDEIVDEAAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 77 MQSLQPDVVIGFGGGSALDAAKAIVW-------FSRQFGIEIE------TCVAIPTTSGTGSEVTSACVISDPDKGIKYP 143
Cdd:cd14863 80 AREEGADGVIGIGGGSVLDTAKAIAVlltnpgpIIDYALAGPPvpkpgiPLIAIPTTAGTGSEVTPIAVITDEENGVKKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 144 LFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGK 223
Cdd:cd14863 160 LLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEAREN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 224 MHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTAL 303
Cdd:cd14863 240 MLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNA--EAYPEKVKKIAKALGVSFPGESDEELG 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 851901932 304 NALIHHIELLKKQCALPafiDALKDEKHTWSQrIPSMVQAALADVTLQTNPRVADASAIQELLEELL 370
Cdd:cd14863 318 EAVADAIREFMKELGIP---SLFEDYGIDKED-LDKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-369 |
4.66e-103 |
|
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: 308.69 E-value: 4.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 9 RLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:cd08194 3 TIIIGGGALeelgEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGiAYAVFDDVVSEPTDEMVEEGLALYKEGGCD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAIVWFS------RQF-GIEIET-----CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYP 151
Cdd:cd08194 83 FIVALGGGSPIDTAKAIAVLAtnggpiRDYmGPRKVDkpglpLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 152 DMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLA 231
Cdd:cd08194 163 AVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAALEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 232 GMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNARDprAAKRYARFAKACHLCPDNANDTTALNALIHHIE 311
Cdd:cd08194 243 GIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPG--APERYAEIARAMGIATEGDSDEEAAEKLVEALE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 851901932 312 LLKKQCALPAfIDALKDEKHTWSQRIPSMVQAALADVTLQTNPRVADASAIQELLEEL 369
Cdd:cd08194 321 RLCADLEIPT-LREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-368 |
3.38e-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: 341487 [Multi-domain] Cd Length: 383 Bit Score: 288.67 E-value: 3.38e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 3 SFSLQTRLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADNRI-SIFSDITPDPTIGTVVQGIAQM 77
Cdd:cd14865 2 EFFNPTKIVSGAGALenlpAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIvGVFDDVPPDSSVAVVNEAAARA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 78 QSLQPDVVIGFGGGSALDAAKAI-VWFS------RQF-GIEIET-----CVAIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:cd14865 82 REAGADGIIAVGGGSVIDTAKGVnILLSeggddlDDYgGANRLTrplkpLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 145 FNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKM 224
Cdd:cd14865 162 VSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 225 HNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLC--PDNANDTTA 302
Cdd:cd14865 242 AIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNL--DAAAERYAELALALAYGvtPAGRRAEEA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851901932 303 LNALIHHIELLKKQCALPAfidALKDEKHTWSQrIPSMVQAALADVTLQTNPRVADASAIQELLEE 368
Cdd:cd14865 320 IEAAIDLVRRLHELCGLPT---RLRDVGVPEEQ-LEAIAELALNDGAILFNPREVDPEDILAILEA 381
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
2-367 |
8.52e-95 |
|
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: 287.52 E-value: 8.52e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 2 KSFSLQTRLYSGQGSLDVL----KRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQ 76
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIgeeaKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGiAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 77 MQSLQPDVVIGFGGGSALDAAKAI-VWFSRQFGIEIETC------------VAIPTTSGTGSEVTSACVISDPDKGIKYP 143
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIgIIVANPGADVRSLEgvaptknpavpiIAVPTTAGTGSEVTINYVITDTEKKRKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 144 LFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGK 223
Cdd:cd08176 161 CVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 224 MHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTAL 303
Cdd:cd08176 241 MALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNA--PATGEKYRDIARAMGVDTTGMSDEEAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851901932 304 NALIHHIELLKKQCALPAFIDALK-DEKHtwsqrIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08176 319 EAAVDAVKKLSKDVGIPQKLSELGvKEED-----IEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-367 |
7.77e-94 |
|
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: 285.16 E-value: 7.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSL----DVLKRFKNKHIWViCDSFLARSPLIEKLRNTLPADNRISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:cd08183 2 PRIVFGRGSLqelgELAAELGKRALLV-TGRSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAI---------------VwFSRqfGIEIET----CVAIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:cd08183 81 VVIAIGGGSVIDAAKAIaalltnegsvldyleV-VGK--GRPLTEpplpFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 145 FNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKM 224
Cdd:cd08183 158 RSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 225 HNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNAR-------DPRAAKRYARFAKACHLCPDna 297
Cdd:cd08183 238 ALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRalrerepDSPALARYRELAGILTGDPD-- 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901932 298 ndtTALNALIHHIELLKKQCALPAFID-ALKDEkhtwsqRIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08183 316 ---AAAEDGVEWLEELCEELGIPRLSEyGLTEE------DFPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
2-366 |
1.40e-91 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 279.08 E-value: 1.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 2 KSFSLQTRLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADNrISIFSDITPDPTIGTVVQGIAQM 77
Cdd:cd08196 1 WSYYQPVKIIFGEGILkelpDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRI-VAVFSDVEPNPTVENVDKCARLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 78 QSLQPDVVIGFGGGSALDAAKAIVWFS------RQFGIEIETCV-------AIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:cd08196 80 RENGADFVIAIGGGSVLDTAKAAACLAktdgsiEDYLEGKKKIPkkglpliAIPTTAGTGSEVTPVAVLTDKEKGKKAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 145 FNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKM 224
Cdd:cd08196 160 VSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 225 HNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKAChlcpdNANDTtalN 304
Cdd:cd08196 240 ALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNA--EALPGRLDELAKQL-----GFKDA---E 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901932 305 ALIHHIELLKKQCALPAFIDAL--KDEKhtwsqrIPSMVQAALADVTLQTNPRVADASAIQELL 366
Cdd:cd08196 310 ELADKIEELKKRIGLRTRLSELgiTEED------LEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
8-370 |
4.42e-91 |
|
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: 277.86 E-value: 4.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADNRIS-IFSDITPDPTIGTVVQGIAQMQSLQP 82
Cdd:cd14861 4 TRIRFGAGAIaelpEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPaVFSDVPPNPTEADVEAGVAAYREGGC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 83 DVVIGFGGGSALDAAKAIVWFSRQ-----------FGIEIET-----CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFN 146
Cdd:cd14861 84 DGIIALGGGSAIDAAKAIALMATHpgplwdyedgeGGPAAITpavppLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 147 NALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHN 226
Cdd:cd14861 164 PKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 227 ASTLAGMAFsQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDttalnaL 306
Cdd:cd14861 244 AALMGAVAF-QKGLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNR--PAVEDKLARLARALGLGLGGFDD------F 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901932 307 IHHIELLKKQCALPAfidALKDEKHTwSQRIPSMVQAALADVTLQTNPRVADASAIQELLEELL 370
Cdd:cd14861 315 IAWVEDLNERLGLPA---TLSELGVT-EDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-367 |
1.31e-90 |
|
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: 277.07 E-value: 1.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 4 FSLQTRLYSGQGSLDVL----KRFKNKHIWVICDSFLARSPLIEKLRNTLpADNRIS--IFSDITPDPTIGTVVQGIAQM 77
Cdd:cd08185 1 YYQPTRILFGAGKLNELgeeaLRPGKKALIVTGKGSSKKTGLLDRVKKLL-EKAGVEvvVFDKVEPNPLTTTVMEGAALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 78 QSLQPDVVIGFGGGSALDAAKAI---------VW---FSRQFGIEIETC----VAIPTTSGTGSEVTSACVISDPDKGIK 141
Cdd:cd08185 80 KEEGCDFVIGLGGGSSMDAAKAIafmatnpgdIWdyiFGGTGKGPPPEKalpiIAIPTTAGTGSEVDPWAVITNPETKEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 142 YPLFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATR 221
Cdd:cd08185 160 KGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 222 GKMHNASTLAGMAFSQAGLGINHAIAHQLGGQF-HLPHGLANALLLTHVIHFNARdpRAAKRYARFAKACHLCPDNANDT 300
Cdd:cd08185 240 EKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIE--KAPEKFAFVARAEASGLSDAKAA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901932 301 talNALIHHIELLKKQCALPafiDALKDEKHTWSQrIPSMVQAAL--ADVTLQTNPRVADASAIQELLE 367
Cdd:cd08185 318 ---EDFIEALRKLLKDIGLD---DLLSDLGVTEED-IPWLAENAMetMGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
20-365 |
4.22e-87 |
|
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: 267.87 E-value: 4.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 20 LKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQPDVVIGFGGGSALDAAK 98
Cdd:cd17814 21 AKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGlEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 99 AIvwfsrqfGI---------EIETC----------VAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDMAILDPT 159
Cdd:cd17814 101 GI-------GIvvsngghilDYEGVdkvrrplpplICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 160 LVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLAGMAFSQAG 239
Cdd:cd17814 174 TLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAGLAFSNAS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 240 LGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALNALIHHIELLKKQCAL 319
Cdd:cd17814 254 LGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNF--PAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGI 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 851901932 320 P---AFIDALKDEkhtwsqrIPSMVQAALADVTLQTNPRVADASAIQEL 365
Cdd:cd17814 332 PetlSELGVDEED-------IPELAKRAMKDPCLVTNPRRPTREDIEEI 373
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
11-365 |
4.28e-80 |
|
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: 250.05 E-value: 4.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 11 YSGQGSLDVL-KRFKNKHI---WVICDSFLARSPLIEKLRNTLPAdNRIS--IFSDITPDPTIGTVVQGIAQMQSLQPDV 84
Cdd:TIGR02638 11 YFGAGAIEDIvDEVKRRGFkkaLVVTDKDLIKFGVADKVTDLLDE-AGIAyeLFDEVKPNPTITVVKAGVAAFKASGADY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 85 VIGFGGGSALDAAKAI-----------------VWFSRQFGIEIetcVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNN 147
Cdd:TIGR02638 90 LIAIGGGSPIDTAKAIgiisnnpefadvrslegVAPTKKPGVPI---IAIPTTAGTAAEVTINYVITDEENKRKFVCVDP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 148 ALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNA 227
Cdd:TIGR02638 167 HDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAREQMALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 228 STLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALNALI 307
Cdd:TIGR02638 247 QYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNA--EFTGEKYREIAKAMGVKTEGMSDEEARDAAV 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 851901932 308 HHIELLKKQCALPAFIDALKDEKhtwsQRIPSMVQAALADVTLQTNPRVADASAIQEL 365
Cdd:TIGR02638 325 EAVKTLSKRVGIPEGLSELGVKE----EDIPALAEAALADVCTGGNPRETTVEEIEEL 378
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
9-362 |
1.20e-79 |
|
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: 248.58 E-value: 1.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 9 RLYSGQGSL----DVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:cd08193 6 RIICGAGAAarlgELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGiAVTVFDDVVADPPEAVVEAAVEQAREAGAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAK--AIVWFSRQ-----FGIEIET-----CVAIPTTSGTGSEVTSACVISDPD---KGIKYPLfnna 148
Cdd:cd08193 86 GVIGFGGGSSMDVAKlvALLAGSDQplddiYGVGKATgprlpLILVPTTAGTGSEVTPISIVTTGEtekKGVVSPQ---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 149 LYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVS-TKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNA 227
Cdd:cd08193 162 LLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 228 STLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALNALI 307
Cdd:cd08193 242 SMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL--PAAEALYAELARALLPGLAFGSDAAAAEAFI 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 851901932 308 HHIELLKKQCALPAFIDALKDEKhtwsQRIPSMVQAALA-DVTLQTNPRV---ADASAI 362
Cdd:cd08193 320 DALEELVEASGLPTRLRDVGVTE----EDLPMLAEDAMKqTRLLVNNPREvteEDALAI 374
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
8-368 |
4.18e-77 |
|
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: 243.22 E-value: 4.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSLD----VLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQSLQP 82
Cdd:cd08190 2 SNIRFGPGATRelgmDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGiEVVVYDGVRVEPTDESFEEAIEFAKEGDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 83 DVVIGFGGGSALDAAKAIVWFS-----------------RQFGIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLF 145
Cdd:cd08190 82 DAFVAVGGGSVIDTAKAANLYAthpgdfldyvnapigkgKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGIS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 146 NNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVS------TKASD------------FTDALAEKAAQIVFQY 207
Cdd:cd08190 162 SRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTArpynarPRPANpderpayqgsnpISDVWAEKAIELIGKY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 208 LPVAVSKGDCLATRGKMHNASTLAGMAFSQAGLGINHAIAHQLGGQ-------------FHLPHGLANALLLTHVIHFNA 274
Cdd:cd08190 242 LRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLSVALTAPAVFRFTA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 275 rdPRAAKRYARFAKACHLCPDNANDTTALNALIHHIELLKKQCALPAFIDALK-DEKHtwsqrIPSMVQAALADV-TLQT 352
Cdd:cd08190 322 --PACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGySEDD-----IPALVEGTLPQQrLLKL 394
|
410
....*....|....*.
gi 851901932 353 NPRVADASAIQELLEE 368
Cdd:cd08190 395 NPRPVTEEDLEEIFED 410
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-367 |
7.25e-77 |
|
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: 242.13 E-value: 7.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 4 FSLQTRLYSGQGSLD----VLKRFKNkHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIAQMQ 78
Cdd:cd08191 1 LRSPSRLLFGPGARRalgrVAARLGS-RVLIVTDPRLASTPLVAELLAALTAAGvAVEVFDGGQPELPVSTVADAAAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 79 SLQPDVVIGFGGGSALDAAKAI-VWFSRqfGIEIET-------------CVAIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVaLLLAH--GGDPRDyygedrvpgpvlpLIAVPTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 145 FNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDF---------------TDALAEKAAQIVFQYLP 209
Cdd:cd08191 158 SSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPFprldpdpvyvgknplTDLLALEAIRLIGRHLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 210 VAVSKGDCLATRGKMHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNaRDPRAAkRYARFAKA 289
Cdd:cd08191 238 RAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFN-RPARAA-ELAEIARA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 290 CHLCPDNANDTTALNAlIHHIELLKKQCALPAFIDAL--KDEkhtwsqRIPSMVQAALADVTL-QTNPRVADASAIQELL 366
Cdd:cd08191 316 LGVTTAGTSEEAADRA-IERVEELLARIGIPTTLADLgvTEA------DLPGLAEKALSVTRLiANNPRPPTEEDLLRIL 388
|
.
gi 851901932 367 E 367
Cdd:cd08191 389 R 389
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-367 |
5.17e-72 |
|
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: 229.03 E-value: 5.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSL----DVLKRFKNKHIWVICD-SFLARSPLIEKLRNTLPADNrISIFSDITPDPTIGTVVQGIAQMQSLQP 82
Cdd:cd08182 2 VKIIFGPGALaelkDLLGGLGARRVLLVTGpSAVRESGAADILDALGGRIP-VVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 83 DVVIGFGGGSALDAAKAIVWFSRQFGIEIET--------------CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNA 148
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLLLlrtgekapeenalpLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 149 LYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNAS 228
Cdd:cd08182 161 LYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 229 TLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNAR--DPRAAKRYARFAKACHLCPDNANdttalnaL 306
Cdd:cd08182 241 LLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGadDECDDDPRGREILLALGASDPAE-------A 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901932 307 IHHIELLKKQCALPAfidALKDEKHTWSQrIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08182 314 AERLRALLESLGLPT---RLSEYGVTAED-LEALAASVNTPERLKNNPVRLSEEDLLRLLE 370
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
1-365 |
2.60e-68 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 220.28 E-value: 2.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 1 MKSFSLQTRLYSGQGSLDVLKRFKN----KHIWVICDSFLARSPLIEKLRNTLPADN-RISIFSDITPDPTIGTVVQGIA 75
Cdd:PRK15454 21 VKTFSVPPVTLCGPGAVSSCGQQAQtrglKHLFVMADSFLHQAGMTAGLTRSLAVKGiAMTLWPCPVGEPCITDVCAAVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 76 QMQSLQPDVVIGFGGGSALDAAKAIVWF----SRQFGIEIETCV--------AIPTTSGTGSEVTSACVISDPDKGIKYP 143
Cdd:PRK15454 101 QLRESGCDGVIAFGGGSVLDAAKAVALLvtnpDSTLAEMSETSVlqprlpliAIPTTAGTGSETTNVTVIIDAVSGRKQV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 144 LFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGK 223
Cdd:PRK15454 181 LAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARES 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 224 MHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNARDPRaaKRYARFAKAchLCPDNANDTTAL 303
Cdd:PRK15454 261 MLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCR--ERFSQIGRA--LRTKKSDDRDAI 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 851901932 304 NA---LIHHIELLKKqcalpaFIDALKDEKH--TWSqripsmvQAALADVTLQTNPRVADASAIQEL 365
Cdd:PRK15454 337 NAvseLIAEVGIGKR------LGDVGATSAHygAWA-------QAALEDICLRSNPRTASLEQIVGL 390
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
11-370 |
1.30e-67 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 217.94 E-value: 1.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 11 YSGQGSLDVL----KRFKNKHIWVICDSFLARSPLIEKLRNTLPADNRI-SIFSDITPDPTIGTVVQGIAQMQSLQPDVV 85
Cdd:PRK10624 12 YFGRGAIGALtdevKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAyEIYDGVKPNPTIEVVKEGVEVFKASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 86 IGFGGGSALDAAKAIvwfsrqfGIEIET------------------CV---AIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:PRK10624 92 IAIGGGSPQDTCKAI-------GIISNNpefadvrslegvaptkkpSVpiiAIPTTAGTAAEVTINYVITDEEKRRKFVC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 145 FNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVsKGDCLAtRGKM 224
Cdd:PRK10624 165 VDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAV-AGDKEA-GEGM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 225 HNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALN 304
Cdd:PRK10624 243 ALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA--DFTGEKYRDIARAMGVKVEGMSLEEARN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851901932 305 ALIHHIELLKKQCALPAfidALKDEKHTwSQRIPSMVQAALADVTLQTNPRVADASAIQELLEELL 370
Cdd:PRK10624 321 AAVEAVKALNRDVGIPP---HLRDVGVK-EEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
56-274 |
3.03e-63 |
|
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: 205.90 E-value: 3.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 56 SIFSDITPDPTIGTVVQGIAQMQSLQPDVVIGFGGGSALDAAKAI-------VWFSRQFGIEIET----CVAIPTTSGTG 124
Cdd:cd08181 58 FIFDEVEENPSIETVEKGAELARKEGADFVIGIGGGSPLDAAKAIallaankDGDEDLFQNGKYNpplpIVAIPTTAGTG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 125 SEVTSACVISDPDKGIKYPLFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIV 204
Cdd:cd08181 138 SEVTPYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLI 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 205 FQYLPVAVSKGDCLATRGKMHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNA 274
Cdd:cd08181 218 GECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCE 287
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
16-365 |
5.71e-62 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 203.26 E-value: 5.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 16 SLDVLKRFKNKHIWVICDSFLARSPLIEKLRNTLPADNRISIFSDIT-PDPTIGTVVQGIAQMQSLQPDVVIGFGGGSAL 94
Cdd:PRK09860 22 AMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTqPNPTTENVAAGLKLLKENNCDSVISLGGGSPH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 95 DAAKAIVWFSRQFGiEIET-------------CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDMAILDPTLV 161
Cdd:PRK09860 102 DCAKGIALVAANGG-DIRDyegvdrsakpqlpMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 162 VSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLAGMAFSQAGLG 241
Cdd:PRK09860 181 IGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 242 INHAIAHQLGGQFHLPHGLANALLLTHVIHFNARdpRAAKRYARFAKACHLCPDNANDTTALNALIHHIELLKKQCALPA 321
Cdd:PRK09860 261 YVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK--VAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPA 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 851901932 322 FIDALKDEKhtwsQRIPSMVQAALADVTLQTNPRVADASAIQEL 365
Cdd:PRK09860 339 GLRDLNVKE----EDFAVLATNALKDACGFTNPIQATHEEIVAI 378
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
3-367 |
4.00e-60 |
|
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: 198.43 E-value: 4.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 3 SFSLQTRLYSGQGSLD----VLKRFKNKHIWVICDSFLARSPLIEKLRNTLpADNRISI--FSDITPDPTIGTVVQGIAQ 76
Cdd:cd08187 3 TFYNPTKIIFGKGAIEelgeEIKKYGKKVLLVYGGGSIKKNGLYDRVVASL-KEAGIEVveFGGVEPNPRLETVREGIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 77 MQSLQPDVVIGFGGGSALDAAKAI---------VW--FSRqfGIEIETCV---AIPTTSGTGSEVTSACVISDPDKGIKY 142
Cdd:cd08187 82 AREENVDFILAVGGGSVIDAAKAIaagakydgdVWdfFTG--KAPPEKALpvgTVLTLAATGSEMNGGAVITNEETKEKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 143 PLFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVS-TKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATR 221
Cdd:cd08187 160 GFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 222 GKMHNASTLA--GMafsqAGLGIN-----HAIAHQLGGQFHLPHGLANALLLTHVIHFNARdpRAAKRYARFAKACHLCP 294
Cdd:cd08187 240 ANLMWAATLAlnGL----LGAGRGgdwatHAIEHELSALYDITHGAGLAIVFPAWMRYVLK--KKPERFAQFARRVFGID 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901932 295 DNANDTTALNALIHHIELLKKQCALPAFIDALK-DEKHtwsqrIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd08187 314 PGGDDEETALEGIEALEEFFKSIGLPTTLSELGiDEED-----IEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-368 |
7.31e-50 |
|
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: 171.65 E-value: 7.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 9 RLYSGQGSL----DVLKRFKNKHIWVICDSFLARSP-LIEKLRNTLpADNRISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:cd14866 7 RLFSGRGALarlgRELDRLGARRALVVCGSSVGANPdLMDPVRAAL-GDRLAGVFDGVRPHSPLETVEAAAEALREADAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAIVWFSRQFGIEIETC---------------------VAIPTTSgTGSEVTSACVISDPDKGIKY 142
Cdd:cd14866 86 AVVAVGGGSAIVTARAASILLAEDRDVRELCtrraedglmvsprldapklpiFVVPTTP-TTADVKAGSAVTDPPAGQRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 143 PLFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDClATRG 222
Cdd:cd14866 165 ALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDDDP-AARA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 223 KMHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKAchLCPDNANDTTA 302
Cdd:cd14866 244 DLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNA--PATDGRLDRLAEA--LGVADAGDEAS 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 303 LNALIHHIELLKKQCALPAF---IDALKDEkhtwsqrIPSMVQAALADVTLQTNPR-VADASAIQELLEE 368
Cdd:cd14866 320 AAAVVDAVEALLDALGVPTRlrdLGVSRED-------LPAIAEAAMDDWFMDNNPRpVPTAEELEALLEA 382
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
7-369 |
3.86e-49 |
|
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: 169.74 E-value: 3.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 7 QTRLYSGQGSLD----VLKRFKNKHIWVICDSFLAR-SPLIEKLRNTLpADNRISIFSDITPDPTIGTVVQGIAQMQSLQ 81
Cdd:cd08192 1 LERVSYGPGAVEallhELATLGASRVFIVTSKSLATkTDVIKRLEEAL-GDRHVGVFSGVRQHTPREDVLEAARAVREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 82 PDVVIGFGGGSALDAAKAIVWFSRQFGIEIETC--------------------VAIPTT-SGtgSEVTSACVISDPDKGI 140
Cdd:cd08192 80 ADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLdaledgkridpnvtgptlphIAIPTTlSG--AEFTAGAGATDDDTGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 141 KYPLFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLAT 220
Cdd:cd08192 158 KQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 221 RGKMHNASTLAGMAF-SQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNARDPRAAKRyARFAKACHLCPDNAND 299
Cdd:cd08192 238 RLKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQR-LIARALGLVTGGLGRE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851901932 300 TTALNALIHhiellkkqcalpAFIDALK-----DEKHTWSQRIPSMVQAALADVTLQTNPR-VADASAIQELLEEL 369
Cdd:cd08192 317 AADAADAID------------ALIRELGlprtlRDVGVGRDQLEKIAENALTDVWCRTNPRpITDKDDVLEILESA 380
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
1-269 |
1.08e-45 |
|
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: 160.46 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 1 MKSFSLQTRLYSGQGSLDVLKRFK-NKHIWVICDSFLARsPLIEKLrnTLPADNrisIFSD--ITPDPTIGTVVQGIAQM 77
Cdd:cd14860 1 MKEFRIKPEIYQFDTCKEFAEEFKlGKDDLVLTNEYIYE-PYFEPL--NLDCAV---IFQEkyGTGEPSDEMVEAIYKDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 78 QSLQPDVVIGFGGGSALDAAKAIV---------WFSRQFGIEIET-CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNN 147
Cdd:cd14860 75 KKYGYKRVIAIGGGTVIDIAKLLAlkgispvldLFDGKIPLIKEKeLIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 148 ALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGdcLATRGKMHN- 226
Cdd:cd14860 155 ELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEIAEKG--EEARFPLLGd 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 851901932 227 ---ASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHV 269
Cdd:cd14860 233 fliASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGV 278
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-288 |
3.26e-42 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 151.38 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 1 MKSFSLQ--TRLYSGQGSL----DVLKRFKNK--------HIwvicdsflARSPLIEKLRNTLPADNR-ISIFSDITPDP 65
Cdd:COG1979 1 MNNFTFYnpTKIIFGKGQIaklgEEIPKYGKKvllvygggSI--------KKNGLYDQVKAALKEAGIeVVEFGGVEPNP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 66 TIGTVVQGIAQMQSLQPDVVIGFGGGSALDAAKAI---------VW--FSRqfGIEIETCV---AIPTTSGTGSEVTSAC 131
Cdd:COG1979 73 RLETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIaagakydgdPWdiLTG--KAPVEKALplgTVLTLPATGSEMNSGS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 132 VISDPDKGIKYPLFNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVS-TKASDFTDALAEKAAQIVFQYLPV 210
Cdd:COG1979 151 VITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTyPVDAPLQDRFAEGLLRTLIEEGPK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 211 AVSKGDCLATRGKMHNASTLA--GMafsqAGLGIN-----HAIAHQLGGQFHLPHGLANALLLTHVIHFNARDPRAakRY 283
Cdd:COG1979 231 ALKDPEDYDARANLMWAATLAlnGL----IGAGVPqdwatHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPE--KF 304
|
....*
gi 851901932 284 ARFAK 288
Cdd:COG1979 305 AQYAE 309
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
8-270 |
3.47e-42 |
|
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: 151.26 E-value: 3.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSL----DVLKRFKNKHIWVICDSFLAR-SPLIEKLRNTLpADNRIS--IFSDITPDPTIGTVVQGIAQMQSL 80
Cdd:cd08186 2 TTLYFGVGAIakikDILKDLGIDKVIIVTGRSSYKkSGAWDDVEKAL-EENGIEyvVYDKVTPNPTVDQADEAAKLARDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 81 QPDVVIGFGGGSALDAAKAI-------------VWFSRQFGIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNN 147
Cdd:cd08186 81 GADAVIAIGGGSPIDTAKSVavllayggktardLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 148 ALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNA 227
Cdd:cd08186 161 CIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 851901932 228 STLAGMAFSQAGLGINHAIAHQLGG-QFHLPHGLANALLLTHVI 270
Cdd:cd08186 241 SMIAGIAIDNGLLHLTHALEHPLSGlKPELPHGLGLALLGPAVV 284
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-367 |
7.30e-41 |
|
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: 147.83 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 4 FSLQTRLYSGQGSLD----VLKRFKNKhIWVICDSFLARSPLIEKLRNTLpADNRIS--IFSDITPDPTIgTVVQGIAQM 77
Cdd:cd14864 1 FKIPPNIVFGADSLErigeEVKEYGSR-FLLITDPVLKESGLADKIVSSL-EKAGISviVFDEIPASATS-DTIDEAAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 78 -QSLQPDVVIGFGGGSALDAAK--AIVWFSRQFGIEIET----------CVAIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:cd14864 78 aRKAGADGIIAVGGGKVLDTAKavAILANNDGGAYDFLEgakpkkkplpLIAVPTTPRSGFEFSDRFPVVDSRSREVKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 145 FNNALYPDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKM 224
Cdd:cd14864 158 KAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 225 HNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKACHLCPDNANDTTALN 304
Cdd:cd14864 238 AQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAA--TSAPDKYAKIARALGEDVEGASPEEAAI 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851901932 305 ALIHHIELLKKQCALPAfidALKDEKHTWSqrIPSMVQAALADVTLQTNPRVADASAIQELLE 367
Cdd:cd14864 316 AAVEGVRRLIAQLNLPT---RLKDLDLASS--LEQLAAIAEDAPKLNGLPRSMSSDDIFDILK 373
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
8-367 |
1.27e-40 |
|
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: 146.11 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSL----DVLKRFKNKHIWVICDSflARSPLIEKLRNTLPaDNRISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:cd08177 2 QRVVFGAGTLaelaEELERLGARRALVLSTP--RQRALAERVAALLG-DRVAGVFDGAVMHVPVEVAERALAAAREAGAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAIvwfSRQFGIEIetcVAIPTTSgTGSEVTSACVISDpdKGIKYPLFNNALYPDMAILDPTLVVS 163
Cdd:cd08177 79 GLVAIGGGSAIGLAKAI---ALRTGLPI---VAVPTTY-AGSEMTPIWGETE--DGVKTTGRDPRVLPRTVIYDPDLTLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 164 VPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLAGMAFSQAGLGIN 243
Cdd:cd08177 150 LPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGMGLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 244 HAIAHQLGGQFHLPHGLANALLLTHVIHFNArdPRAAKRYARFAKAChlcpdNAND-TTALNALIHhiellkkQCALPAf 322
Cdd:cd08177 230 HKLCHVLGGTFDLPHAETHAVVLPHVLAYNA--PAAPDAMARLARAL-----GGGDaAGGLYDLAR-------RLGAPT- 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 851901932 323 idALKD----EKHtwsqrIPSMVQAALADVTLqtNPRVADASAIQELLE 367
Cdd:cd08177 295 --SLRDlgmpEDD-----IDRAADLALANPYP--NPRPVERDALRALLE 334
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
8-286 |
6.04e-31 |
|
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: 120.45 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSLD----VLKRFKNKH----IWVIcDSFLARSPLIEKLRNtlpADNRISIFSDITPDPT---IGTVVQGIAQ 76
Cdd:cd08184 2 PKYLFGRGSFDqlgeLLAERRKSNndyvVFFI-DDVFKGKPLLDRLPL---QNGDLLIFVDTTDEPKtdqIDALRAQIRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 77 MQSLQPDVVIGFGGGSALDAAKAIVWF------SRQF---------GIEIetcVAIPTTSGTGSEVTSACVISDPDK--G 139
Cdd:cd08184 78 ENDKLPAAVVGIGGGSTMDIAKAVSNMltnpgsAADYqgwdlvknpGIYK---IGVPTLSGTGAEASRTAVLTGPEKklG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 140 IK--YPLFnnalypDMAILDPTLVVSVPPAITANTGMDVLTHALEAYVSTKASDFTDALAEKAAQIVFQYLpvavSKGD- 216
Cdd:cd08184 155 INsdYTVF------DQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVF----LSDDm 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901932 217 -CLATRGKMHNASTLAGMAFSQAGLGINHAIAHQLGGQFHLPHGLANAlllthvIHFNARDPRAAKRYARF 286
Cdd:cd08184 225 mSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANC------IVFNVLEEFYPEGVKEF 289
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-282 |
6.92e-26 |
|
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: 104.75 E-value: 6.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 8 TRLYSGQGSL----DVLKRFKNKHIwVICDSFLARSpLIEKLRNTLPADNRISIFSDITPDPTIGTVVQGIAQMQSLQPD 83
Cdd:cd07766 2 TRIVFGEGAIaklgEIKRRGFDRAL-VVSDEGVVKG-VGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAIVwFSRQFGIEIetcVAIPTTSGTGSEVTSACVISDPDKGIKYPLFnnALYPDMAILDPTLVVS 163
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVA-ALLNRGIPF---IIVPTTASTDSEVSPKSVITDKGGKNKQVGP--HYNPDVVFVDTDITKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 164 VPPAITANTGMDVLTHALEayvstkasdftdalaekaaqivfqylpvavskgdclatRGKMHNASTLAGMAFSQA-GLGI 242
Cdd:cd07766 154 LPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAATLAGMGLFESpGLGL 195
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 851901932 243 NHAIAHQLGGQFHLPHGLANALLLTHVIHFNARDPRAAKR 282
Cdd:cd07766 196 AHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEA 235
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
2-299 |
1.24e-15 |
|
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: 77.13 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 2 KSFSLQTRLYSGQGSLD----VLKRFKnKHIWVICDSFlARSPLIEKLRNTLPADNRISIFSDITPDPTIGTVVQGIAQM 77
Cdd:COG0371 1 RVIILPRRYVQGEGALDelgeYLADLG-KRALIITGPT-ALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 78 QSLQPDVVIGFGGGSALDAAKAIvwfSRQFGIEIetcVAIPTTSGTGSEVTSACVISDPD-KGIKYPLFNNAlyPDMAIL 156
Cdd:COG0371 79 KEQGADVIIGVGGGKALDTAKAV---AYRLGLPV---VSVPTIASTDAPASPLSVIYTEDgAFDGYSFLAKN--PDLVLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 157 DPTLVVSVPPA-ITAntGM-DVLTHALEAYVSTKASD------FTD---ALAEKAAQIVFQYLPVAVSKgdclATRGKMH 225
Cdd:COG0371 151 DTDIIAKAPVRlLAA--GIgDALAKWYEARDWSLAHRdlageyYTEaavALARLCAETLLEYGEAAIKA----VEAGVVT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 226 NAS--------TLAGMAF----SQAGLGINHAIAH---QLGGQFHLPHGL--ANALLLTHVIHfnaRDPRAAKRYARFAK 288
Cdd:COG0371 225 PALervveanlLLSGLAMgigsSRPGSGAAHAIHNgltALPETHHALHGEkvAFGTLVQLVLE---GRPEEIEELLDFLR 301
|
330
....*....|.
gi 851901932 289 ACHLcPDNAND 299
Cdd:COG0371 302 SVGL-PTTLAD 311
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
42-282 |
1.27e-15 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 77.53 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 42 IEKLRNTLPADNRISI---------------------------FSDITPDPTIGTVVQGIAQMQSLQPDVVIGFGGGSAL 94
Cdd:PRK15138 19 IAGLREQIPADARVLItygggsvkktgvldqvldalkgmdvleFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 95 DAAKAIV-----------WFSRQ-FGIEIETcvAIP-----TTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDMAILD 157
Cdd:PRK15138 99 DGTKFIAaaanypenidpWHILEtGGKEIKS--AIPmgsvlTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 158 PTLVVSVPPAITANTGMDVLTHALEAYVsTKASD--FTDALAEKAAQIVFQYLPVAVSKGDCLATRGKMHNASTLAGMAF 235
Cdd:PRK15138 177 PVYTYTLPPRQVANGVVDAFVHTVEQYV-TYPVDakIQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNGL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 851901932 236 SQAGLGINHAiAHQLGGQFHLPHGLANALLLTHVIHFNARDPRAAKR 282
Cdd:PRK15138 256 IGAGVPQDWA-THMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKR 301
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
13-292 |
6.52e-10 |
|
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: 59.73 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 13 GQGSLD----VLKRFKNKHIwVICDSFlARSPLIEKLRNTLPADN---RISIFSDITPDPTIGTVVqgiAQMQSLQPDVV 85
Cdd:cd08170 7 GPGALDrlgeYLAPLGKKAL-VIADPF-VLDLVGERLEESLEKAGlevVFEVFGGECSREEIERLA---AIARANGADVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 86 IGFGGGSALDAAKAIvwfsrqfGIEIETCVAI-PTTSGTGSEVTSACVISDPDkGIkyplFNNALY----PDMAILDPTL 160
Cdd:cd08170 82 IGIGGGKTIDTAKAV-------ADYLGLPVVIvPTIASTDAPCSALSVIYTED-GE----FDEYLFlprnPDLVLVDTEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 161 VVSVPPAITAnTGM-DVLTHALEA----------YVSTKASDFTDALAEKAAQIVFQYLPVAVskgdcLATRGKMHN--- 226
Cdd:cd08170 150 IAKAPVRFLV-AGMgDALATYFEAracarsgapnMAGGRPTLAALALAELCYDTLLEYGVAAK-----AAVEAGVVTpal 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851901932 227 -----ASTL-AGMAFSQAGLGINHAIAH---QLGGQFHLPHGLANAL-LLTHVIHFNaRDPRAAKRYARFAKACHL 292
Cdd:cd08170 224 eavieANTLlSGLGFESGGLAAAHAIHNgltALPETHHLLHGEKVAFgTLVQLVLEG-RPDEEIEEVIRFCRSVGL 298
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
71-292 |
5.66e-08 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 54.08 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 71 VQGIAQM-QSLQPDVVIGFGGGSALDAAKAIVWfsrQFGIeieTCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNAL 149
Cdd:cd08550 66 IERLAEKaKEEGADVIIGIGGGKVLDTAKAVAD---RLGL---PVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 150 yPDMAILDPTLVVSVPP------------------AITANTGMDVLTHAleayvSTKASDFT-DALAEKAAQIVFQylpv 210
Cdd:cd08550 140 -PDLVLVDTDIIAAAPVrylaagigdtlakwyearPSSRGGPDDLALQA-----AVQLAKLAyDLLLEYGVQAVED---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 211 avskgdclATRGKMHNAST--------LAGMAFSQAGLGINHAIAH-------QLGGQFHLPHGLANAL-LLTHVIhFNA 274
Cdd:cd08550 210 --------VRQGKVTPALEdvvdaiilLAGLVGSLGGGGCRTAAAHaihngltKLPETHGTLHGEKVAFgLLVQLA-LEG 280
|
250
....*....|....*...
gi 851901932 275 RDPRAAKRYARFAKACHL 292
Cdd:cd08550 281 RSEEEIEELIEFLRRLGL 298
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
81-259 |
9.05e-07 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 50.20 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 81 QPDVVIGFGGGSALDAAKAIvwfsrqfGIEIETCVAI-PTTSGTGSEVTSACVISDPDkGIkyplFNNALY----PDMAI 155
Cdd:PRK09423 84 GCDVVIGIGGGKTLDTAKAV-------ADYLGVPVVIvPTIASTDAPTSALSVIYTEE-GE----FERYLFlpknPDLVL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 156 LDPTLVVSVPPAITAnTGM-DVLTHALEA----------YVSTKASDFTDALAEKAAQIVFQYLPVAvskgdCLATRgkm 224
Cdd:PRK09423 152 VDTAIIAKAPARFLA-AGIgDALATWFEAracsrsggttMAGGKPTLAALALAELCYETLLEDGLKA-----KLAVE--- 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 851901932 225 HNAST------------LAGMAFSQAGLGINHAIaH----QLGGQFHLPHG 259
Cdd:PRK09423 223 AKVVTpalenvieantlLSGLGFESGGLAAAHAI-HngltALEDTHHLTHG 272
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
75-165 |
2.71e-05 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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: 341451 [Multi-domain] Cd Length: 346 Bit Score: 45.59 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 75 AQMQSLQPDVVIGFGGGSALDAAKAIvwfSRQFGIEietCVAIPTTSGTGSEVTSACVISDPD-KGIKYPLFNNAlyPDM 153
Cdd:cd08172 69 EEAKEHQADVIIGIGGGKVLDTAKAV---ADKLNIP---LILIPTLASNCAAWTPLSVIYDEDgEFIGYDYFPRS--AYL 140
|
90
....*....|..
gi 851901932 154 AILDPTLVVSVP 165
Cdd:cd08172 141 VLVDPRLLLDSP 152
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
84-185 |
5.83e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 41.63 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901932 84 VVIGFGGGSALDAAKAIvwfSRQFGIEIetcVAIPTTSGTGSEVTSACV-ISDPDKGIKYPLFNNALYpdMAILDPTLVV 162
Cdd:PRK10586 89 VVIGVGGGALLDTAKAL---ARRLGLPF---VAIPTIAATCAAWTPLSVwYNDAGQALHFEIFDDANF--LVLVEPRIIL 160
|
90 100
....*....|....*....|....
gi 851901932 163 SVPPA-ITANTGmDVLTHALEAYV 185
Cdd:PRK10586 161 NAPQEyLLAGIG-DTLAKWYEAVV 183
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
43-120 |
1.08e-03 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 40.58 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851901932 43 EKLRNTLPADNRISIFSDITpDPTIGTVVQGIAQmqSLQPDVVIGFGGGSALDAAKaIVWFSRQFGieietCVAIPTT 120
Cdd:cd08174 42 EDILESLEEAGEIVTVEENT-DNSAEELAEKAFS--LPKVDAIVGIGGGKVLDVAK-YAAFLSKLP-----FISVPTS 110
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| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
71-145 |
7.10e-03 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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: 341450 Cd Length: 345 Bit Score: 37.89 E-value: 7.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851901932 71 VQGIAQMQSLQ-PDVVIGFGGGSALDAAKAIvwfSRQFGIEIETcvaIPTTSGTGSEVTSACVISDPDKGIKYPLF 145
Cdd:cd08171 67 VEKLKANPEVQeADMIFAVGGGKAIDTVKVL---ADRLNKPVFT---FPTIASNCAAVTAVSVMYNPDGSFKEYYF 136
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