|
Name |
Accession |
Description |
Interval |
E-value |
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
4-367 |
2.66e-172 |
|
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: 482.76 E-value: 2.66e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 4 FSLQTRLYSGLGSLKVLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSNRISIFSEITPDPTIQTVVKGIAQMQTLRPD 83
Cdd:cd08180 1 FSLKTKIYSGEDSLERLKELKGKRVFIVTDPFMVKSGMVDKVTDELDKSNEVEIFSDVVPDPSIEVVAKGLAKILEFKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 84 VVIGFGGGSALDAAKAIVWFSRQCAIEIE--TCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLV 161
Cdd:cd08180 81 TIIALGGGSAIDAAKAIIYFALKQKGNIKkpLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLPDIAILDPELV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 162 VSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFSQAGLG 241
Cdd:cd08180 161 KSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASCMAGIAFNNAGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 242 LNHAIAHQLGGQFHLPHGLANALLLTTVIRFnagdpraakryarlaktchlcpddandtaslnaLIQHIEQLKKACSMPT 321
Cdd:cd08180 241 INHSLAHALGGRFHIPHGRANAILLPYVIEF---------------------------------LIAAIRRLNKKLGIPS 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 447014174 322 LANALKDKKAEWSSRIPDMVRAALADATLRTNPRAADAIAIAEMLE 367
Cdd:cd08180 288 TLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-369 |
2.68e-144 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 413.75 E-value: 2.68e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 1 MNTFSLQTRLYSGLGSLK----VLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIA 75
Cdd:COG1454 2 MFTFRLPTRIVFGAGALAelgeELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGiEVVVFDDVEPNPTVETVEAGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 76 QMQTLRPDVVIGFGGGSALDAAKAIVWF------------SRQCAIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYP 143
Cdd:COG1454 82 AAREFGADVVIALGGGSAIDAAKAIALLatnpgdledylgIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 144 LFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGK 223
Cdd:COG1454 162 IADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 224 MHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLcPDDANDTASL 303
Cdd:COG1454 242 MALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNA--PAAPERYAEIARALGL-DVGLSDEEAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014174 304 NALIQHIEQLKKACSMPTlanALKD---KKAEwssrIPDMVRAALADATLRTNPRAADAIAIAEMLEEL 369
Cdd:COG1454 319 EALIEAIRELLRDLGIPT---RLSElgvTEED----LPELAELALADRCLANNPRPLTEEDIEAILRAA 380
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
26-355 |
2.80e-127 |
|
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: 371.13 E-value: 2.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 26 KHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKaIVW-- 102
Cdd:cd08178 24 KRAFIVTDRVLYKLGYVDKVLDVLEARGvETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAK-IMWlf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 103 -------FS--RQCAIEIE-------------TCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSL 160
Cdd:cd08178 103 yehpetkFEdlAQRFMDIRkrvykfpklgkkaKLVAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIVDPEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 161 VVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFSQAGL 240
Cdd:cd08178 183 VMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFANAFL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 241 GLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGD-------------PRAAKRYARLAKTCHLcpDDANDTASLNALI 307
Cdd:cd08178 263 GICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDpptkqaafpqykyYVAKERYAEIADLLGL--GGKTPEEKVESLI 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 447014174 308 QHIEQLKKACSMPTLANALKDKKAEWSSRIPDMVRAALADATLRTNPR 355
Cdd:cd08178 341 KAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPR 388
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
4-367 |
5.93e-127 |
|
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: 369.60 E-value: 5.93e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 4 FSLQTRLYSGLGSLKVLSRFTNKHIWIICDA-FLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLR 81
Cdd:cd08179 2 FFVPRDIYFGEGALEYLKTLKGKRAFIVTGGgSMKRNGFLDKVEDYLKEAGmEVKVFEGVEPDPSVETVEKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 82 PDVVIGFGGGSALDAAKAIVWF-------SRQCAIEIETC--------VAIPTTSGTGSEVTSACVISDPDKGIKYPLFD 146
Cdd:cd08179 82 PDWIIAIGGGSVIDAAKAMWVFyeypeltFEDALVPFPLPelrkkarfIAIPSTSGTGSEVTRASVITDTEKGIKYPLAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 147 NALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHN 226
Cdd:cd08179 162 FEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 227 ASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGDPRAAKRYARLAKtchlcpdDANDTASLNAL 306
Cdd:cd08179 242 ASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALLI-------GLTDEELVEDL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014174 307 IQHIEQLKKACSMP-TLANALKDKKaEWSSRIPDMVRAALADATLRTNPRAADAIAIAEMLE 367
Cdd:cd08179 315 IEAIEELNKKLGIPlSFKEAGIDED-EFFAKLDEMAENAMNDACTGTNPRKPTVEEMKELLK 375
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-362 |
1.72e-123 |
|
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: 360.61 E-value: 1.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 8 TRLYSGLGSLK----VLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRP 82
Cdd:cd08551 2 TRIVFGAGALArlgeELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGiEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 83 DVVIGFGGGSALDAAKAI------------VWFSRQCAIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALY 150
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIavlatnggsirdYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 151 PDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTL 230
Cdd:cd08551 162 PDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 231 AGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTASLNALIQHI 310
Cdd:cd08551 242 AGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNL--PACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 447014174 311 EQLKKACSMPTLANALKDKKaewsSRIPDMVRAALADATLRTN-PR---AADAIAI 362
Cdd:cd08551 320 RELLRDLGIPTSLSELGVTE----EDIPELAEDAMKSGRLLSNnPRpltEEDIREI 371
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
15-355 |
3.05e-119 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 364.89 E-value: 3.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 15 GSLKVLSR--FTNKHIWIICDAFLAGSPLIDTLCQSL-PDSNRI--SIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFG 89
Cdd:PRK13805 468 GSLPYLLDelDGKKRAFIVTDRFMVELGYVDKVTDVLkKRENGVeyEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALG 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 90 GGSALDAAKAIVWFSRQCAIEIE-----------------------TCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFD 146
Cdd:PRK13805 548 GGSPMDAAKIMWLFYEHPETDFEdlaqkfmdirkriykfpklgkkaKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLAD 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 147 NALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKG--DCLAtRGKM 224
Cdd:PRK13805 628 YELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGakDPEA-REKM 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 225 HNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGDP------------RAAKRYARLAKTCHL 292
Cdd:PRK13805 707 HNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPpkqaafpqyeypRADERYAEIARHLGL 786
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014174 293 CPDdaNDTASLNALIQHIEQLKKACSMPTlanALKD---KKAEWSSRIPDMVRAALADATLRTNPR 355
Cdd:PRK13805 787 PGS--TTEEKVESLIKAIEELKAELGIPM---SIKEagvDEADFLAKLDELAELAFDDQCTGANPR 847
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-362 |
8.42e-119 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 348.44 E-value: 8.42e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 8 TRLYSGLGSLKVLSRFT---NKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRPD 83
Cdd:pfam00465 2 TRIVFGAGALAELGEELkrlGARALIVTDPGSLKSGLLDKVLASLEEAGiEVVVFDGVEPEPTLEEVDEAAALAREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 84 VVIGFGGGSALDAAKAI------------VWFSRQCAIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYP 151
Cdd:pfam00465 82 VIIAVGGGSVIDTAKAIallltnpgdvwdYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 152 DIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLA 231
Cdd:pfam00465 162 DLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLASTLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 232 GMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDtaslNALIQHIE 311
Cdd:pfam00465 242 GLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNA--PAAPEKLAQLARALGEDSDEEAA----EEAIEALR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 447014174 312 QLKKACSMPTlanALKDKKAEwSSRIPDMVRAALADATLRTNPRAADAIAI 362
Cdd:pfam00465 316 ELLRELGLPT---TLSELGVT-EEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-348 |
6.56e-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: 6.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 7 QTRLYSGLGSL----KVLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLR 81
Cdd:cd08189 5 EPELFEGAGSLlqlpEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGiEYVVFDGVVPDPTIDNVEEGLALYKENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 82 PDVVIGFGGGSALDAAKAIvwfsrqcAI-------EIETCV-------------AIPTTSGTGSEVTSACVISDPDKGIK 141
Cdd:cd08189 85 CDAIIAIGGGSVIDCAKVI-------AAraanpkkSVRKLKgllkvrkklppliAVPTTAGTGSEATIAAVITDPETHEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 142 YPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATR 221
Cdd:cd08189 158 YAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 222 GKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTA 301
Cdd:cd08189 238 ENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYG--PAAEKRLAELADAAGLGDSGESDSE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 447014174 302 SLNALIQHIEQLKKACSMPTLANALKDKKaewssrIPDMVRAALADA 348
Cdd:cd08189 316 KAEAFIAAIRELNRRMGIPTTLEELKEED------IPEIAKRALKEA 356
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
11-367 |
2.45e-109 |
|
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: 324.85 E-value: 2.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 11 YSGLGSLK----VLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRPDVV 85
Cdd:cd08188 10 LFGPGCLKeigdELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGiEYVIFDGVQPNPTVTNVNEGLELFKENGCDFI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 86 IGFGGGSALDAAKAIvwfsrqcAI------EIET-------------CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFD 146
Cdd:cd08188 90 ISVGGGSAHDCAKAI-------GIlatnggEIEDyegvdkskkpglpLIAINTTAGTASEVTRFAVITDEERHVKMVIVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 147 NALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHN 226
Cdd:cd08188 163 WNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENMAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 227 ASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAK-----TCHLCPDDANDTA 301
Cdd:cd08188 243 AQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNL--PACPERFADIARalgenTEGLSDEEAAEAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014174 302 slnalIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPRAADAIAIAEMLE 367
Cdd:cd08188 321 -----IEAIRKLSRRVGIPSGLKELGVKEED----FPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-366 |
3.60e-106 |
|
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: 316.47 E-value: 3.60e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 1 MNTFSLQTRLYsGLGSLKVLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQT 79
Cdd:cd14862 1 MWYFSSPKIVF-GEDALSHLEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGfEVEVFDEVEPEPPLETVLKGAEAMRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 80 LRPDVVIGFGGGSALDAAKAIVWFSRQCAIEIETC--------------VAIPTTSGTGSEVTSACVISDPDKGIKYPLF 145
Cdd:cd14862 80 FEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIspldllglrkkaklIAIPTTSGTGSEATWAIVLTDTEEPRKIAVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 146 DNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMH 225
Cdd:cd14862 160 NPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAREKMH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 226 NASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdpRAAKRYARLAKTCHLCPDDANDTASlnA 305
Cdd:cd14862 240 NAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYA---KVTDERYDLLKLLGIEARDEEEALK--K 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014174 306 LIQHIEQLKKACSMPTLANALKDKKAEWSSRIPDMVRAALADATLRTNPRAADAIAIAEML 366
Cdd:cd14862 315 LVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-369 |
2.87e-100 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 301.76 E-value: 2.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 9 RLYSGLGSLK----VLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRPD 83
Cdd:cd08194 3 TIIIGGGALEelgeEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGiAYAVFDDVVSEPTDEMVEEGLALYKEGGCD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 84 VVIGFGGGSALDAAKAIVWFS------------RQCAIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYP 151
Cdd:cd08194 83 FIVALGGGSPIDTAKAIAVLAtnggpirdymgpRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 152 DIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLA 231
Cdd:cd08194 163 AVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAALEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 232 GMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGDprAAKRYARLAKTCHLCPDDANDTASLNALIQHIE 311
Cdd:cd08194 243 GIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPG--APERYAEIARAMGIATEGDSDEEAAEKLVEALE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014174 312 QLKKACSMPTLAnALKDKKAEWSSRIPDMVRAALADATLRTNPRAADAIAIAEMLEEL 369
Cdd:cd08194 321 RLCADLEIPTLR-EYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-369 |
2.04e-99 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 299.45 E-value: 2.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 3 TFSLQTRLYSGLGSL----KVLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSNRIS-IFSEITPDPTIQTVVKGIAQM 77
Cdd:cd14863 1 TYSQLTPVIFGAGAVeqigELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVvVFDDVEPDPPDEIVDEAAEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 78 QTLRPDVVIGFGGGSALDAAKAIVW----------FSRQCAIEIETC---VAIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:cd14863 81 REEGADGVIGIGGGSVLDTAKAIAVlltnpgpiidYALAGPPVPKPGiplIAIPTTAGTGSEVTPIAVITDEENGVKKSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 145 FDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKM 224
Cdd:cd14863 161 LGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 225 HNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTASLN 304
Cdd:cd14863 241 LLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNA--EAYPEKVKKIAKALGVSFPGESDEELGE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014174 305 ALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPRAADAIAIAEMLEEL 369
Cdd:cd14863 319 AVADAIREFMKELGIPSLFEDYGIDKED----LDKIAEAVLKDPFAMFNPRPITEEEVAEILEAI 379
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-368 |
8.26e-96 |
|
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: 290.21 E-value: 8.26e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 4 FSLQTRLYSGLGSL----KVLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSNRI-SIFSEITPDPTIQTVVKGIAQMQ 78
Cdd:cd14865 3 FFNPTKIVSGAGALenlpAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIvGVFDDVPPDSSVAVVNEAAARAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 79 TLRPDVVIGFGGGSALDAAKAI-VWFSRQCAIE-----IETC-------VAIPTTSGTGSEVTSACVISDPDKGIKYPLF 145
Cdd:cd14865 83 EAGADGIIAVGGGSVIDTAKGVnILLSEGGDDLddyggANRLtrplkplIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 146 DNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMH 225
Cdd:cd14865 163 SPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 226 NASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTAS--L 303
Cdd:cd14865 243 IAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNL--DAAAERYAELALALAYGVTPAGRRAEeaI 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014174 304 NALIQHIEQLKKACSMP-TLANALKDKKAewssrIPDMVRAALADATLRTNPRAADAIAIAEMLEE 368
Cdd:cd14865 321 EAAIDLVRRLHELCGLPtRLRDVGVPEEQ-----LEAIAELALNDGAILFNPREVDPEDILAILEA 381
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-366 |
4.95e-92 |
|
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: 280.23 E-value: 4.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 3 TFSLQTRLYSGLGSLK----VLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSNrISIFSEITPDPTIQTVVKGIAQMQ 78
Cdd:cd08196 2 SYYQPVKIIFGEGILKelpdIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRI-VAVFSDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 79 TLRPDVVIGFGGGSALDAAKAIVWFSrQCAIEIET--------------CVAIPTTSGTGSEVTSACVISDPDKGIKYPL 144
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLA-KTDGSIEDylegkkkipkkglpLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 145 FDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKM 224
Cdd:cd08196 160 VSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 225 HNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTChlcpddanDTASLN 304
Cdd:cd08196 240 ALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNA--EALPGRLDELAKQL--------GFKDAE 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014174 305 ALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPRAADAIAIAEML 366
Cdd:cd08196 310 ELADKIEELKKRIGLRTRLSELGITEED----LEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
2-362 |
2.55e-91 |
|
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: 278.66 E-value: 2.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 2 NTFSLQTRLYSGLGSLKVL----SRFTNKHIWIICDAFLAGSPLIDTLcQSLPDSNRI--SIFSEITPDPTIQTVVKGIA 75
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIgeeaKKRGFKKALIVTDKGLVKFGIVDKV-TDVLKEAGIayTVFDEVKPNPTIENVMAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 76 QMQTLRPDVVIGFGGGSALDAAKAI-----------VWFSRQCAIEIE--TCVAIPTTSGTGSEVTSACVISDPDKGIKY 142
Cdd:cd08176 80 AYKESGADGIIAVGGGSSIDTAKAIgiivanpgadvRSLEGVAPTKNPavPIIAVPTTAGTGSEVTINYVITDTEKKRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 143 PLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRG 222
Cdd:cd08176 160 VCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 223 KMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTAS 302
Cdd:cd08176 240 NMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNA--PATGEKYRDIARAMGVDTTGMSDEEA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014174 303 LNALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPRAA---DAIAI 362
Cdd:cd08176 318 AEAAVDAVKKLSKDVGIPQKLSELGVKEED----IEALAEDALNDVCTPGNPREAtkeDIIAL 376
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
30-370 |
2.30e-88 |
|
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: 270.92 E-value: 2.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 30 IICDAFLAGSPLIDTLCQSLPDSNRIS-IFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAIV------- 101
Cdd:cd14861 30 LVTDPGLAALGIVDRVLEALGAAGLSPaVFSDVPPNPTEADVEAGVAAYREGGCDGIIALGGGSAIDAAKAIAlmathpg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 102 ---WFSRQC----AIEIET--CVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANT 172
Cdd:cd14861 110 plwDYEDGEggpaAITPAVppLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAAT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 173 GMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFsQAGLGLNHAIAHQLGG 252
Cdd:cd14861 190 GMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMGAVAF-QKGLGAVHALAHALGA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 253 QFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDtaslnaLIQHIEQLKKACSMP-TLANALKDKka 331
Cdd:cd14861 269 LYGLHHGLLNAILLPYVLRFNR--PAVEDKLARLARALGLGLGGFDD------FIAWVEDLNERLGLPaTLSELGVTE-- 338
|
330 340 350
....*....|....*....|....*....|....*....
gi 447014174 332 ewsSRIPDMVRAALADATLRTNPRAADAIAIAEMLEELV 370
Cdd:cd14861 339 ---DDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-367 |
2.96e-87 |
|
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: 268.22 E-value: 2.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 8 TRLYSGLGSLK---VLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSNRISIFSEITPDPTIQTVVKGIAQMQTLRPDV 84
Cdd:cd08183 2 PRIVFGRGSLQelgELAAELGKRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 85 VIGFGGGSALDAAKAIvwfsrqCA------------------IEIET----CVAIPTTSGTGSEVTSACVISDPDKGIKY 142
Cdd:cd08183 82 VIAIGGGSVIDAAKAI------AAlltnegsvldylevvgkgRPLTEpplpFIAIPTTAGTGSEVTKNAVLSSPEHGVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 143 PLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRG 222
Cdd:cd08183 156 SLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEARE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 223 KMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFN-------AGDPRAAKRYARLAKTCHLCPD 295
Cdd:cd08183 236 DMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANlralrerEPDSPALARYRELAGILTGDPD 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014174 296 DANDtaslnALIQHIEQLKKACSMPTLaNALKDKKAEwssrIPDMVRAALADATLRTNPRAADAIAIAEMLE 367
Cdd:cd08183 316 AAAE-----DGVEWLEELCEELGIPRL-SEYGLTEED----FPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-367 |
3.40e-87 |
|
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: 268.21 E-value: 3.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 4 FSLQTRLYSGLGSLKVLSRFTNKH-----IwIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQM 77
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEALRPgkkalI-VTGKGSSKKTGLLDRVKKLLEKAGvEVVVFDKVEPNPLTTTVMEGAALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 78 QTLRPDVVIGFGGGSALDAAKAI---------VW---FSRQCAIEIETC----VAIPTTSGTGSEVTSACVISDPDKGIK 141
Cdd:cd08185 80 KEEGCDFVIGLGGGSSMDAAKAIafmatnpgdIWdyiFGGTGKGPPPEKalpiIAIPTTAGTGSEVDPWAVITNPETKEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 142 YPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATR 221
Cdd:cd08185 160 KGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 222 GKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQF-HLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDT 300
Cdd:cd08185 240 EKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTI--EKAPEKFAFVARAEASGLSDAKAA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014174 301 AslnALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAAL--ADATLRTNPRAADAIAIAEMLE 367
Cdd:cd08185 318 E---DFIEALRKLLKDIGLDDLLSDLGVTEED----IPWLAENAMetMGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-357 |
5.18e-86 |
|
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: 264.79 E-value: 5.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 13 GLGSLKV----LSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIG 87
Cdd:cd17814 10 GVGARKLagryAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGlEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 88 FGGGSALDAAKAI-VWFSRQCAI-EIETC----------VAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAV 155
Cdd:cd17814 90 VGGGSPIDCAKGIgIVVSNGGHIlDYEGVdkvrrplpplICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 156 LDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAF 235
Cdd:cd17814 170 IDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAGLAF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 236 SQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTASLNALIQHIEQLKK 315
Cdd:cd17814 250 SNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNF--PAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLRE 327
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 447014174 316 ACSMP-TLANALKDKkaewsSRIPDMVRAALADATLRTNPRAA 357
Cdd:cd17814 328 DLGIPeTLSELGVDE-----EDIPELAKRAMKDPCLVTNPRRP 365
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
1-365 |
5.36e-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: 249.66 E-value: 5.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 1 MNTFSLQTRLYSGLGSLKVL----SRFTNKHIWIICDAFLAGSPLIDTLCQSLpDSNRIS--IFSEITPDPTIQTVVKGI 74
Cdd:TIGR02638 1 SNRLILNETSYFGAGAIEDIvdevKRRGFKKALVVTDKDLIKFGVADKVTDLL-DEAGIAyeLFDEVKPNPTITVVKAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 75 AQMQTLRPDVVIGFGGGSALDAAKAI-----------------VWFSRQCAIEIetcVAIPTTSGTGSEVTSACVISDPD 137
Cdd:TIGR02638 80 AAFKASGADYLIAIGGGSPIDTAKAIgiisnnpefadvrslegVAPTKKPGVPI---IAIPTTAGTAAEVTINYVITDEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 138 KGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDC 217
Cdd:TIGR02638 157 NKRKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 218 LATRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDA 297
Cdd:TIGR02638 237 LEAREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNA--EFTGEKYREIAKAMGVKTEGM 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014174 298 NDTASLNALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPRAADAIAIAEM 365
Cdd:TIGR02638 315 SDEEARDAAVEAVKTLSKRVGIPEGLSELGVKEED----IPALAEAALADVCTGGNPRETTVEEIEEL 378
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
9-362 |
3.39e-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: 247.43 E-value: 3.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 9 RLYSGLGSL----KVLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRPD 83
Cdd:cd08193 6 RIICGAGAAarlgELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGiAVTVFDDVVADPPEAVVEAAVEQAREAGAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 84 VVIGFGGGSALDAAK--AIVWFSRQcaiEIETC-------------VAIPTTSGTGSEVTSACVISDPD---KGIKYPLf 145
Cdd:cd08193 86 GVIGFGGGSSMDVAKlvALLAGSDQ---PLDDIygvgkatgprlplILVPTTAGTGSEVTPISIVTTGEtekKGVVSPQ- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 146 dnaLYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDF-TDALAEKAVQIVFHYLPTAVNKGDCLATRGKM 224
Cdd:cd08193 162 ---LLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPiSDALAREALRLLGANLRRAVEDGSDLEAREAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 225 HNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAktCHLCPD--DANDTAS 302
Cdd:cd08193 239 LLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL--PAAEALYAELA--RALLPGlaFGSDAAA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014174 303 LNALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPR----AADAIAI 362
Cdd:cd08193 315 AEAFIDALEELVEASGLPTRLRDVGVTEED----LPMLAEDAMKQTRLLVNNPrevtEEDALAI 374
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
8-368 |
5.71e-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: 242.84 E-value: 5.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 8 TRLYSGLGSLK----VLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRP 82
Cdd:cd08190 2 SNIRFGPGATRelgmDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGiEVVVYDGVRVEPTDESFEEAIEFAKEGDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 83 DVVIGFGGGSALDAAKAIVWFS-----------------RQCAIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLF 145
Cdd:cd08190 82 DAFVAVGGGSVIDTAKAANLYAthpgdfldyvnapigkgKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGIS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 146 DNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVS--------PHASD----------FTDALAEKAVQIVFHY 207
Cdd:cd08190 162 SRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTArpynarprPANPDerpayqgsnpISDVWAEKAIELIGKY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 208 LPTAVNKGDCLATRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQ-------------FHLPHGLANALLLTTVIRFNA 274
Cdd:cd08190 242 LRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLSVALTAPAVFRFTA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 275 -GDPRAAKRYARL--AKTCHLCPDDANDtaslnALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALA-DATL 350
Cdd:cd08190 322 pACPERHLEAAELlgADTSGASDRDAGE-----VLADALIKLMRDIGIPNGLSALGYSEDD----IPALVEGTLPqQRLL 392
|
410
....*....|....*...
gi 447014174 351 RTNPRAADAIAIAEMLEE 368
Cdd:cd08190 393 KLNPRPVTEEDLEEIFED 410
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
30-367 |
1.32e-75 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 238.67 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 30 IICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAI-VWFSR-- 105
Cdd:cd08191 30 IVTDPRLASTPLVAELLAALTAAGvAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIGLGGGSNMDLAKVVaLLLAHgg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 106 -------QCAIEIETC--VAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDV 176
Cdd:cd08191 110 dprdyygEDRVPGPVLplIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 177 LTHALESYVS-PHASD--------------FTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFSQAGLG 241
Cdd:cd08191 190 LTHAIESYTArDFPPFprldpdpvyvgknpLTDLLALEAIRLIGRHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 242 LNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGDPRAakRYARLAKTCHLCPDDANDTASLNAlIQHIEQLKKACSMPT 321
Cdd:cd08191 270 AAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAA--ELAEIARALGVTTAGTSEEAADRA-IERVEELLARIGIPT 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 447014174 322 LANALKDKKAewssRIPDMVRAALADATL-RTNPRAADAIAIAEMLE 367
Cdd:cd08191 347 TLADLGVTEA----DLPGLAEKALSVTRLiANNPRPPTEEDLLRILR 389
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-367 |
1.36e-69 |
|
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: 222.49 E-value: 1.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 8 TRLYSGLGSLK----VLSRFTNKHIWIICD-AFLAGSPLIDTLCQSLPDSNrISIFSEITPDPTIQTVVKGIAQMQTLRP 82
Cdd:cd08182 2 VKIIFGPGALAelkdLLGGLGARRVLLVTGpSAVRESGAADILDALGGRIP-VVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 83 DVVIGFGGGSALDAAKAIvwfSRQCAIEIET-----------------CVAIPTTSGTGSEVTSACVISDPDKGIKYPLF 145
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAI---AALLGSPGENllllrtgekapeenalpLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 146 DNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMH 225
Cdd:cd08182 158 HPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 226 NASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAG--DPRAAKRYARLAKTCHLCPDDANdtasl 303
Cdd:cd08182 238 EASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGadDECDDDPRGREILLALGASDPAE----- 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014174 304 naLIQHIEQLKKACSMPTLANALKDKKAEWssriPDMVRAALADATLRTNPRAADAIAIAEMLE 367
Cdd:cd08182 313 --AAERLRALLESLGLPTRLSEYGVTAEDL----EALAASVNTPERLKNNPVRLSEEDLLRLLE 370
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
57-369 |
3.33e-66 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 214.09 E-value: 3.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 57 IFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAI-----------------VWFSRQCAIEIetcVAIPT 119
Cdd:PRK10624 63 IYDGVKPNPTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIgiisnnpefadvrslegVAPTKKPSVPI---IAIPT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 120 TSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEK 199
Cdd:PRK10624 140 TAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 200 AVQIVFHYLPTAVNkGDCLAtRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRA 279
Cdd:PRK10624 220 AIEIIAGALRGAVA-GDKEA-GEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA--DFT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 280 AKRYARLAKTCHLCPDDANDTASLNALIQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPRAADA 359
Cdd:PRK10624 296 GEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEED----IPALAQAAFDDVCTGGNPREATL 371
|
330
....*....|
gi 447014174 360 IAIAEMLEEL 369
Cdd:PRK10624 372 EDIVELYKKA 381
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
1-365 |
3.30e-65 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 212.20 E-value: 3.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 1 MNTFSLQTRLYSGLGSLKVLSRFTN----KHIWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIA 75
Cdd:PRK15454 21 VKTFSVPPVTLCGPGAVSSCGQQAQtrglKHLFVMADSFLHQAGMTAGLTRSLAVKGiAMTLWPCPVGEPCITDVCAAVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 76 QMQTLRPDVVIGFGGGSALDAAKAIVWF-----------SRQCAIEIE-TCVAIPTTSGTGSEVTSACVISDPDKGIKYP 143
Cdd:PRK15454 101 QLRESGCDGVIAFGGGSVLDAAKAVALLvtnpdstlaemSETSVLQPRlPLIAIPTTAGTGSETTNVTVIIDAVSGRKQV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 144 LFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGK 223
Cdd:PRK15454 181 LAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARES 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 224 MHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGDPRaaKRYARLAKTC-HLCPDDANDTAS 302
Cdd:PRK15454 261 MLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCR--ERFSQIGRALrTKKSDDRDAINA 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014174 303 LNALIQHIEQLKKACSmptlANALKDKKAEWSsripdmvRAALADATLRTNPRAADAIAIAEM 365
Cdd:PRK15454 339 VSELIAEVGIGKRLGD----VGATSAHYGAWA-------QAALEDICLRSNPRTASLEQIVGL 390
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
4-274 |
4.23e-64 |
|
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: 208.21 E-value: 4.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 4 FSLQTRLYSGLGSLKVLSRF-----------TNKHiwiicDAFLAGSplIDTLCQSLpDSNRIS--IFSEITPDPTIQTV 70
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADElaalgkkalivTGKH-----SAKKNGS--LDDVTEAL-EENGIEyfIFDEVEENPSIETV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 71 VKGIAQMQTLRPDVVIGFGGGSALDAAKAI-------VWFSRQCAIEIET----CVAIPTTSGTGSEVTSACVISDPDKG 139
Cdd:cd08181 73 EKGAELARKEGADFVIGIGGGSPLDAAKAIallaankDGDEDLFQNGKYNpplpIVAIPTTAGTGSEVTPYSILTDHEKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 140 IKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLA 219
Cdd:cd08181 153 TKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447014174 220 TRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNA 274
Cdd:cd08181 233 DREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCE 287
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
39-367 |
8.61e-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: 197.66 E-value: 8.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 39 SPLIDTLCQSLPDSNrISI--FSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAI---------VW--FSR 105
Cdd:cd08187 43 NGLYDRVVASLKEAG-IEVveFGGVEPNPRLETVREGIELAREENVDFILAVGGGSVIDAAKAIaagakydgdVWdfFTG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 106 QcaIEIETCV---AIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALE 182
Cdd:cd08187 122 K--APPEKALpvgTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 183 SYVS-PHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLA--GMafsqAGLGLN-----HAIAHQLGGQF 254
Cdd:cd08187 200 QYFTgTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAATLAlnGL----LGAGRGgdwatHAIEHELSALY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 255 HLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTASLNALIQHIEQLKKACSMPTLANALKDKKaews 334
Cdd:cd08187 276 DITHGAGLAIVFPAWMRYVL--KKKPERFAQFARRVFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDE---- 349
|
330 340 350
....*....|....*....|....*....|...
gi 447014174 335 SRIPDMVRAALADATLRTNPRAADAIAIAEMLE 367
Cdd:cd08187 350 EDIEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
16-357 |
1.19e-59 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 197.48 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 16 SLKVLSRFTNKHIWIICDAFLAGSPLIDTLCQSLPDSNRIS-IFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSAL 94
Cdd:PRK09860 22 AMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSvIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 95 DAAKAI---------------VWFSRQCAIEIetcVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPS 159
Cdd:PRK09860 102 DCAKGIalvaanggdirdyegVDRSAKPQLPM---IAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 160 LVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFSQAG 239
Cdd:PRK09860 179 LMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 240 LGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTASLNALIQHIEQLKKACSM 319
Cdd:PRK09860 259 LGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNS--KVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDI 336
|
330 340 350
....*....|....*....|....*....|....*...
gi 447014174 320 PTLANALKDKKAEwssrIPDMVRAALADATLRTNPRAA 357
Cdd:PRK09860 337 PAGLRDLNVKEED----FAVLATNALKDACGFTNPIQA 370
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-368 |
3.69e-51 |
|
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: 175.11 E-value: 3.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 9 RLYSGLGSL----KVLSRFTNKHIWIICDAFLAGSP-LIDTLCQSLPDsNRISIFSEITPDPTIQTVVKGIAQMQTLRPD 83
Cdd:cd14866 7 RLFSGRGALarlgRELDRLGARRALVVCGSSVGANPdLMDPVRAALGD-RLAGVFDGVRPHSPLETVEAAAEALREADAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 84 VVIGFGGGSALDAAKAIVW-------FSRQCAIEIET--------------CVAIPTTSgTGSEVTSACVISDPDKGIKY 142
Cdd:cd14866 86 AVVAVGGGSAIVTARAASIllaedrdVRELCTRRAEDglmvsprldapklpIFVVPTTP-TTADVKAGSAVTDPPAGQRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 143 PLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDClATRG 222
Cdd:cd14866 165 ALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDDDP-AARA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 223 KMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKtcHLCPDDANDTAS 302
Cdd:cd14866 244 DLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNA--PATDGRLDRLAE--ALGVADAGDEAS 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014174 303 LNALIQHIEQLKKACSMPTlanALKDKKAEwSSRIPDMVRAALADATLRTNPR-AADAIAIAEMLEE 368
Cdd:cd14866 320 AAAVVDAVEALLDALGVPT---RLRDLGVS-REDLPAIAEAAMDDWFMDNNPRpVPTAEELEALLEA 382
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
65-315 |
4.68e-49 |
|
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: 169.32 E-value: 4.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 65 PTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAIV---------WFSRQcaIEIE-TC--VAIPTTSGTGSEVTSACV 132
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLAlkgispvldLFDGK--IPLIkEKelIIVPTTCGTGSEVTNISI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 133 ISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFH-YLPTA 211
Cdd:cd14860 140 VELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEgYQEIA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 212 VNKGDCLATR-GKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRF---NAGDPRAAKRYARLA 287
Cdd:cd14860 220 EKGEEARFPLlGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNyqeKNPDGEIKKLNEFLA 299
|
250 260
....*....|....*....|....*...
gi 447014174 288 KTCHLCPDDANDTasLNALIQHIEQLKK 315
Cdd:cd14860 300 KILGCDEEDVYDE--LEELLNKILPKKP 325
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
7-366 |
2.32e-47 |
|
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: 165.11 E-value: 2.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 7 QTRLYSGLGS----LKVLSRFTNKHIWIICDAFLA-GSPLIDTLCQSLPDSNrISIFSEITPDPTIQTVVKGIAQMQTLR 81
Cdd:cd08192 1 LERVSYGPGAvealLHELATLGASRVFIVTSKSLAtKTDVIKRLEEALGDRH-VGVFSGVRQHTPREDVLEAARAVREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 82 PDVVIGFGGGSALDAAKAIVWFSRQCAIEIETC--------------------VAIPTT-SGtgSEVTSACVISDPDKGI 140
Cdd:cd08192 80 ADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLdaledgkridpnvtgptlphIAIPTTlSG--AEFTAGAGATDDDTGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 141 KYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLAT 220
Cdd:cd08192 158 KQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 221 RGKMHNASTLAGMAF-SQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGDPRAAKRYARLAKTcHLCPDDAND 299
Cdd:cd08192 238 RLKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALG-LVTGGLGRE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014174 300 TASLNaliQHIEQLKKACSMPTLANALKDKKAEwssrIPDMVRAALADATLRTNPR----AADAIAIAEML 366
Cdd:cd08192 317 AADAA---DAIDALIRELGLPRTLRDVGVGRDQ----LEKIAENALTDVWCRTNPRpitdKDDVLEILESA 380
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-367 |
1.38e-42 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 152.07 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 4 FSLQTRLYSGLGSLKVLSRFTNKH---IWIICDAFLAGSPLIDTLCQSLPDSN-RISIFSEITPDPTIQTVVKGIAQMQT 79
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYgsrFLLITDPVLKESGLADKIVSSLEKAGiSVIVFDEIPASATSDTIDEAAELARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 80 LRPDVVIGFGGGSALDAAKAI------------VWFSRQCAIEIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDN 147
Cdd:cd14864 81 AGADGIIAVGGGKVLDTAKAVailanndggaydFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 148 ALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNA 227
Cdd:cd14864 161 PGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 228 STLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgdPRAAKRYARLAKTCHLCPDDANDTASLNALI 307
Cdd:cd14864 241 GCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAA--TSAPDKYAKIARALGEDVEGASPEEAAIAAV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 308 QHIEQLKKACSMPTlanALKDKKAEWSsrIPDMVRAALADATLRTNPRAADAIAIAEMLE 367
Cdd:cd14864 319 EGVRRLIAQLNLPT---RLKDLDLASS--LEQLAAIAEDAPKLNGLPRSMSSDDIFDILK 373
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
38-367 |
6.88e-42 |
|
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: 149.19 E-value: 6.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 38 GSPLIDTLCQSLPDSNrISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAIvwfsrqcAIEIET-CVA 116
Cdd:cd08177 34 QRALAERVAALLGDRV-AGVFDGAVMHVPVEVAERALAAAREAGADGLVAIGGGSAIGLAKAI-------ALRTGLpIVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 117 IPTTSgTGSEVTSACVISDpdKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDAL 196
Cdd:cd08177 106 VPTTY-AGSEMTPIWGETE--DGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 197 AEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAgd 276
Cdd:cd08177 183 AEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNA-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 277 PRAAKRYARLAktchlcpdDANDTASLNALIQhieQLKKACSMPTlanALKD---KKAEwssrIPDMVRAALADATLrtN 353
Cdd:cd08177 261 PAAPDAMARLA--------RALGGGDAAGGLY---DLARRLGAPT---SLRDlgmPEDD----IDRAADLALANPYP--N 320
|
330
....*....|....
gi 447014174 354 PRAADAIAIAEMLE 367
Cdd:cd08177 321 PRPVERDALRALLE 334
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
41-346 |
2.67e-41 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 149.07 E-value: 2.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 41 LIDTLCQSLPDSNR-ISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAI---------VW--FSRQca 108
Cdd:COG1979 47 LYDQVKAALKEAGIeVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIaagakydgdPWdiLTGK-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 109 IEIETCV---AIPTTSGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYV 185
Cdd:COG1979 125 APVEKALplgTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 186 S-PHASDFTDALAEKAVQIVFHYLPTAVNKGDCLATRGKMHNASTLA--GMafsqAGLGLN-----HAIAHQLGGQFHLP 257
Cdd:COG1979 205 TyPVDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLAlnGL----IGAGVPqdwatHMIEHELSALYDID 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 258 HGLANALLLTTVIRFNAGDPRAakRYARLAKTC-HLCPDDANDTAslNALIQHIEQLKKACSMPTlanALKDKKAEwSSR 336
Cdd:COG1979 281 HGAGLAIVLPAWMRYVLEEKPE--KFAQYAERVwGITEGDDEERA--LEGIEATEEFFESLGLPT---RLSEYGID-EED 352
|
330
....*....|
gi 447014174 337 IPDMVRAALA 346
Cdd:COG1979 353 IEEMAEKATA 362
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
56-271 |
1.32e-39 |
|
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: 144.33 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 56 SIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAI-------------VWFSRQCAIEIETCVAIPTTSG 122
Cdd:cd08186 56 VVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDTAKSVavllayggktardLYGFRFAPERALPLVAINLTHG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 123 TGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQ 202
Cdd:cd08186 136 TGSEVDRFAVATIPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIR 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 203 IVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGG-QFHLPHGLANALLLTTVIR 271
Cdd:cd08186 216 LIAEYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGlKPELPHGLGLALLGPAVVK 285
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
8-262 |
1.42e-27 |
|
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: 111.21 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 8 TRLYSGLGSLKVLS-------RFTNKHIWIICDAFLAGSPLIDTLcqsLPDSNRISIFSEITPDPT---IQTVVKGIAQM 77
Cdd:cd08184 2 PKYLFGRGSFDQLGellaerrKSNNDYVVFFIDDVFKGKPLLDRL---PLQNGDLLIFVDTTDEPKtdqIDALRAQIRAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 78 QTLRPDVVIGFGGGSALDAAKAIV--------------W-FSRQCAIEIetcVAIPTTSGTGSEVTSACVISDPDK--GI 140
Cdd:cd08184 79 NDKLPAAVVGIGGGSTMDIAKAVSnmltnpgsaadyqgWdLVKNPGIYK---IGVPTLSGTGAEASRTAVLTGPEKklGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 141 K--YPLFDNalypdiAVLDPSLVVSVPAAITANTGMDVLTHALESYVSPHASDFTDALAEKAVQI---VFHYlptavNKG 215
Cdd:cd08184 156 NsdYTVFDQ------VILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELcrdVFLS-----DDM 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447014174 216 DCLATRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLAN 262
Cdd:cd08184 225 MSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
43-274 |
2.61e-25 |
|
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: 103.21 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 43 DTLCQSLPDSNRISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAIVwFSRQCAIEIetcVAIPTTSG 122
Cdd:cd07766 39 EKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKAVA-ALLNRGIPF---IIVPTTAS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 123 TGSEVTSACVISDPDKGIKYPLFdnALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALEsyvsphasdftdalaekavq 202
Cdd:cd07766 115 TDSEVSPKSVITDKGGKNKQVGP--HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE-------------------- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014174 203 ivfhylptavnkgdclatRGKMHNASTLAGMAFSQA-GLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNA 274
Cdd:cd07766 173 ------------------LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVAN 227
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
58-341 |
5.51e-16 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 78.68 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 58 FSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAIV-----------WFSRQC-AIEIETcvAIP-----TT 120
Cdd:PRK15138 62 FGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAaaanypenidpWHILETgGKEIKS--AIPmgsvlTL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 121 SGTGSEVTSACVISDPDKGIKYPLFDNALYPDIAVLDPSLVVSVPAAITANTGMDVLTHALESYVS-PHASDFTDALAEK 199
Cdd:PRK15138 140 PATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDAKIQDRFAEG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 200 AVQIVFHYLPTAVNKGDCLATRGKMHNASTLAGMAFSQAGLGLNHAiAHQLGGQFHLPHGLANALLLTTVIRFNAGDPRA 279
Cdd:PRK15138 220 ILLTLIEEGPKALKEPENYDVRANVMWAATQALNGLIGAGVPQDWA-THMLGHELTAMHGLDHAQTLAIVLPALWNEKRD 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014174 280 AKR-----YARLAKTCHLCPDDANDTASLNALIQHIEQLkkacSMPTlanALKDKKAEWSSrIPDMV 341
Cdd:PRK15138 299 TKRakllqYAERVWNITEGSDDERIDAAIAATRNFFEQM----GVPT---RLSDYGLDGSS-IPALL 357
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
18-292 |
2.21e-13 |
|
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: 70.58 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 18 KVLSRFtNKHIWIICDAF---LAGspliDTLCQSLPDSNRISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSAL 94
Cdd:COG0371 21 EYLADL-GKRALIITGPTalkAAG----DRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKEQGADVIIGVGGGKAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 95 DAAKAIvwfSRQCAIEIetcVAIPTTSGTGSEVTSACVISDPDKGIKYPLFDNAlYPDIAVLDPSLVVSVPAA-ITAntG 173
Cdd:COG0371 96 DTAKAV---AYRLGLPV---VSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAK-NPDLVLVDTDIIAKAPVRlLAA--G 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 174 M-DVL---------THALESYVSPHASDFTDALAEKAVQIVFHYLPTAVNKgdclATRGKMHNAS--------TLAGMAF 235
Cdd:COG0371 167 IgDALakwyeardwSLAHRDLAGEYYTEAAVALARLCAETLLEYGEAAIKA----VEAGVVTPALervveanlLLSGLAM 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014174 236 ----SQAGLGLNHAIAH---QLGGQFHLPHGL--ANALLLTTVIRfnaGDPRAAKRYARLAKTCHL 292
Cdd:COG0371 243 gigsSRPGSGAAHAIHNgltALPETHHALHGEkvAFGTLVQLVLE---GRPEEIEELLDFLRSVGL 305
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
18-259 |
3.10e-08 |
|
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: 54.72 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 18 KVLSRFTNKHIwIICDAFLAGSpLIDTLCQSLPDSNRISIFSEITPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAA 97
Cdd:cd08170 16 EYLAPLGKKAL-VIADPFVLDL-VGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADVVIGIGGGKTIDTA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 98 KAIvwfsrqcAIEIETCVAI-PTTSGTGSEVTSACVISDPDkGIkyplFDNALY----PDIAVLDPSLVVSVPAAITAnT 172
Cdd:cd08170 94 KAV-------ADYLGLPVVIvPTIASTDAPCSALSVIYTED-GE----FDEYLFlprnPDLVLVDTEIIAKAPVRFLV-A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 173 GM-DVLT---HALESYVSPHASDFTD-------ALAEKAVQIVFHYLPTAVnkgdcLATRGKMHN--------ASTL-AG 232
Cdd:cd08170 161 GMgDALAtyfEARACARSGAPNMAGGrptlaalALAELCYDTLLEYGVAAK-----AAVEAGVVTpaleavieANTLlSG 235
|
250 260 270
....*....|....*....|....*....|
gi 447014174 233 MAFSQAGLGLNHAIAH---QLGGQFHLPHG 259
Cdd:cd08170 236 LGFESGGLAAAHAIHNgltALPETHHLLHG 265
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
13-166 |
1.06e-07 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 53.28 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 13 GLGSLKVLSRFTN---KHIWIICDAFLAGSpLIDTLCQSLPDSN---RISIFSEITPDPTIQTVVKGIAQMQTlrpDVVI 86
Cdd:PRK09423 14 GKGALARLGEYLKplgKRALVIADEFVLGI-VGDRVEASLKEAGltvVFEVFNGECSDNEIDRLVAIAEENGC---DVVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 87 GFGGGSALDAAKAIvwfsrqcAIEIETCVAI-PTTSGTGSEVTSACVISDPDkGIkyplFDNALY----PDIAVLDPSLV 161
Cdd:PRK09423 90 GIGGGKTLDTAKAV-------ADYLGVPVVIvPTIASTDAPTSALSVIYTEE-GE----FERYLFlpknPDLVLVDTAII 157
|
....*
gi 447014174 162 VSVPA 166
Cdd:PRK09423 158 AKAPA 162
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
26-248 |
2.52e-05 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 45.60 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 26 KHIWIICDAF---LAGSPLIDTLCQslpdsNRISIFSEI-TPDPTIQTVVKGIAQMQTLRPDVVIGFGGGSALDAAKAIV 101
Cdd:cd08550 23 KKALIIGGKTaleAVGEKLEKSLEE-----AGIDYEVEVfGGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 102 WFSRQcaieieTCVAIPTTSGTGSEVTSACVISDPDKGIK-YPLFDNAlyPDIAVLDPSLVVSVPAAITAnTGM-DVLTH 179
Cdd:cd08550 98 DRLGL------PVVTVPTIAATCAAWSALSVLYDEEGEFLgYSLLKRS--PDLVLVDTDIIAAAPVRYLA-AGIgDTLAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 180 ALEsyVSPHASDFTD--------ALAEKAVQIVFHYLPTAVNKgdclATRGKMHNAST--------LAGMAFSQAGLGLN 243
Cdd:cd08550 169 WYE--ARPSSRGGPDdlalqaavQLAKLAYDLLLEYGVQAVED----VRQGKVTPALEdvvdaiilLAGLVGSLGGGGCR 242
|
....*
gi 447014174 244 HAIAH 248
Cdd:cd08550 243 TAAAH 247
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
43-98 |
2.30e-04 |
|
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: 42.51 E-value: 2.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 447014174 43 DTLCQSLPDSNRISIFSEITpDPTIQTVVKGIAQmqTLRPDVVIGFGGGSALDAAK 98
Cdd:cd08174 42 EDILESLEEAGEIVTVEENT-DNSAEELAEKAFS--LPKVDAIVGIGGGKVLDVAK 94
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
84-167 |
2.33e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 39.71 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 84 VVIGFGGGSALDAAKAIvwfSRQCAIEIetcVAIPTTSGTGSEVTSACV-ISDPDKGIKYPLFDNALYpdIAVLDPSLVV 162
Cdd:PRK10586 89 VVIGVGGGALLDTAKAL---ARRLGLPF---VAIPTIAATCAAWTPLSVwYNDAGQALHFEIFDDANF--LVLVEPRIIL 160
|
....*
gi 447014174 163 SVPAA 167
Cdd:PRK10586 161 NAPQE 165
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
75-167 |
2.58e-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: 341451 [Multi-domain] Cd Length: 346 Bit Score: 39.42 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014174 75 AQMQTLRPDVVIGFGGGSALDAAKAIvwfSRQCAIEietCVAIPTTSGTGSEVTSACVISDPD-KGIKYPLFDNAlyPDI 153
Cdd:cd08172 69 EEAKEHQADVIIGIGGGKVLDTAKAV---ADKLNIP---LILIPTLASNCAAWTPLSVIYDEDgEFIGYDYFPRS--AYL 140
|
90
....*....|....
gi 447014174 154 AVLDPSLVVSVPAA 167
Cdd:cd08172 141 VLVDPRLLLDSPKD 154
|
|
| |
