|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
11-378 |
1.03e-176 |
|
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: 496.20 E-value: 1.03e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHD 88
Cdd:cd08551 3 RIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAgiEVEVFDDVEPNPTVETVEAAAELAREEGAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 89 GLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLP 168
Cdd:cd08551 83 LVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 169 DVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMA 248
Cdd:cd08551 163 DVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 249 GMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVEAMTRL 328
Cdd:cd08551 243 GIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVREL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 504533071 329 CAAVEIPSGLRSFGVPEDAIPAMASEAAGIERLMRNNPRKLSAADIEKIY 378
Cdd:cd08551 323 LRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREIY 372
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
5-382 |
1.77e-172 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 485.78 E-value: 1.77e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 5 SFKIAHKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAY 82
Cdd:COG1454 4 TFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAgiEVVVFDDVEPNPTVETVEAGAAAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 83 REGGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIV 162
Cdd:COG1454 84 REFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKGIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 163 SDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMA 242
Cdd:COG1454 164 DPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREKMA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 243 TASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIaGLSVNDAADQAV 322
Cdd:COG1454 244 LASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAEALI 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 323 EAMTRLCAAVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:COG1454 323 EAIRELLRDLGIPTRLSELGVTEEDLPELA-ELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
13-379 |
5.03e-144 |
|
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: 413.45 E-value: 5.03e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 13 LTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHDGL 90
Cdd:cd08188 10 LFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAgiEYVIFDGVQPNPTVTNVNEGLELFKENGCDFI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 91 IGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLPDV 170
Cdd:cd08188 90 ISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNVTPTI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 171 ALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMAGM 250
Cdd:cd08188 170 AVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENMAYAQFLAGM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 251 AFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVEAMTRLCA 330
Cdd:cd08188 250 AFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSR 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 504533071 331 AVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKLSAADIEKIYR 379
Cdd:cd08188 330 RVGIPSGLKELGVKEEDFPLLA-ENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-382 |
9.89e-139 |
|
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: 399.98 E-value: 9.89e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGD--RAYEIFDRVLPDPEIAIVEDCMRAYREGGHD 88
Cdd:cd08194 3 TIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEagIAYAVFDDVVSEPTDEMVEEGLALYKEGGCD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 89 GLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLP 168
Cdd:cd08194 83 FIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 169 DVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMA 248
Cdd:cd08194 163 AVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAALEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 249 GMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVEAMTRL 328
Cdd:cd08194 243 GIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 329 CAAVEIPSgLRSFGVPED----AIPAMASEA--AGierLMRNNPRKLSAADIEKIYRAAY 382
Cdd:cd08194 323 CADLEIPT-LREYGIDEEefeaALDKMAEDAlaSG---SPANNPRVPTKEEIIELYREAW 378
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
11-374 |
1.62e-136 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 393.89 E-value: 1.62e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDVdNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHD 88
Cdd:pfam00465 3 RIVFGAGALAELGEELKRLGA-RALIVTDPGSLKSGLLDKVLASLEEAgiEVVVFDGVEPEPTLEEVDEAAALAREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 89 GLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLP 168
Cdd:pfam00465 82 VIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 169 DVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMA 248
Cdd:pfam00465 162 DLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLASTLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 249 GMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNiaglSVNDAADQAVEAMTRL 328
Cdd:pfam00465 242 GLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED----SDEEAAEEAIEALREL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 504533071 329 CAAVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKLSAADI 374
Cdd:pfam00465 318 LRELGLPTTLSELGVTEEDLDALA-EAALRDRSLANNPRPLTAEDI 362
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
6-382 |
3.43e-135 |
|
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: 391.11 E-value: 3.43e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 6 FKIAHKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYR 83
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAgiAVTVFDDVVADPPEAVVEAAVEQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 84 EGGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQlKKGIVS 163
Cdd:cd08193 81 EAGADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGETE-KKGVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 164 DYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHA-SPITDALAIGAIRLIASALPKAYANPANLQARDDMA 242
Cdd:cd08193 160 PQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKkNPISDALAREALRLLGANLRRAVEDGSDLEAREAML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 243 TASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAV 322
Cdd:cd08193 240 LGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 323 EAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGIERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:cd08193 320 DALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPREVTEEDALAIYQAAL 379
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
15-382 |
1.40e-133 |
|
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: 388.06 E-value: 1.40e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIG 92
Cdd:cd08190 7 GPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAgiEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 93 VGGGSAIDIAKSVAAYAGYHGA-LADLFGVD----QVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLL 167
Cdd:cd08190 87 VGGGSVIDTAKAANLYATHPGDfLDYVNAPIgkgkPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 168 PDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLH------------------ASPITDALAIGAIRLIASALPKAY 229
Cdd:cd08190 167 PTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNPISDVWAEKAIELIGKYLRRAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 230 ANPANLQARDDMATASLMAGMAFGNAGVGAVHALAYPLGGRFN-------------IAHGVSNALLLPYVMHWNKLACVE 296
Cdd:cd08190 247 NDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKdyrppgypvdhphVPHGLSVALTAPAVFRFTAPACPE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 297 RMQDIAQAMGVNIAGLSVNDAADQAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGIERLMRNNPRKLSAADIEK 376
Cdd:cd08190 327 RHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEE 406
|
....*.
gi 504533071 377 IYRAAY 382
Cdd:cd08190 407 IFEDAL 412
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-382 |
2.33e-130 |
|
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: 378.81 E-value: 2.33e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 5 SFKIAHKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGD--RAYEIFDRVLPDPEIAIVEDCMRAY 82
Cdd:cd14865 2 EFFNPTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDaiEIVGVFDDVPPDSSVAVVNEAAARA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 83 REGGHDGLIGVGGGSAIDIAKSVAAYAGYHG-ALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGI 161
Cdd:cd14865 82 REAGADGIIAVGGGSVIDTAKGVNILLSEGGdDLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 162 VSDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDM 241
Cdd:cd14865 162 VSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 242 ATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAM--GVNIAGLSVNDAAD 319
Cdd:cd14865 242 AIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAGRRAEEAIE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533071 320 QAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:cd14865 322 AAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIA-ELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
15-379 |
2.35e-129 |
|
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: 376.12 E-value: 2.35e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIG 92
Cdd:cd08176 12 GWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAgiAYTVFDEVKPNPTIENVMAGVAAYKESGADGIIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 93 VGGGSAIDIAKSVAAYAGYHGA-LADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLPDVA 171
Cdd:cd08176 92 VGGGSSIDTAKAIGIIVANPGAdVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFVCVDPHDIPTVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 172 LISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMAGMA 251
Cdd:cd08176 172 IVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARENMALAQYIAGMA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 252 FGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVEAMTRLCAA 331
Cdd:cd08176 252 FSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKD 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504533071 332 VEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKLSAADIEKIYR 379
Cdd:cd08176 332 VGIPQKLSELGVKEEDIEALA-EDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-382 |
4.85e-128 |
|
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: 373.49 E-value: 4.85e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 12 LLTGAGAIEQLAAELTRLDvDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHDG 89
Cdd:cd08191 7 LLFGPGARRALGRVAARLG-SRVLIVTDPRLASTPLVAELLAALTAAgvAVEVFDGGQPELPVSTVADAAAAARAFDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 90 LIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLPD 169
Cdd:cd08191 86 VIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 170 VALISPQMTLTCPRGVTAASGVDALVHAIESYLSLH---------------ASPITDALAIGAIRLIASALPKAYANPAN 234
Cdd:cd08191 166 VAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAIRLIGRHLPRAVRDGDD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 235 LQARDDMATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSv 314
Cdd:cd08191 246 LEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAGTS- 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533071 315 NDAADQAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGIERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:cd08191 325 EEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-378 |
1.90e-127 |
|
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: 371.11 E-value: 1.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 14 TGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDRA--YEIFDRVLPDPEIAIVEDCMRAYREGGHDGLI 91
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGleYVVFSDVTPNPRDFEVMEGAELYREEGCDGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 92 GVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLPDVA 171
Cdd:cd17814 89 AVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 172 LISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMAGMA 251
Cdd:cd17814 169 LIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAGLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 252 FGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVEAMTRLCAA 331
Cdd:cd17814 249 FSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLRED 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504533071 332 VEIPSGLRSFGVPEDAIPAMASEAAgIERLMRNNPRKLSAADIEKIY 378
Cdd:cd17814 329 LGIPETLSELGVDEEDIPELAKRAM-KDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-382 |
3.56e-124 |
|
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: 363.01 E-value: 3.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 5 SFKIAHKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGD--RAYEIFDRVLPDPEIAIVEDCMRAY 82
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEagIEVVVFDDVEPDPPDEIVDEAAEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 83 REGGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFG-VDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGI 161
Cdd:cd14863 81 REEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALaGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 162 VSDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDM 241
Cdd:cd14863 161 LGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 242 ATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQA 321
Cdd:cd14863 241 LLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504533071 322 VEAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGiERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:cd14863 321 ADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLK-DPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-380 |
1.49e-120 |
|
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: 353.70 E-value: 1.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 10 HKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGH 87
Cdd:cd08189 6 PELFEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAgiEYVVFDGVVPDPTIDNVEEGLALYKENGC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 88 DGLIGVGGGSAIDIAKSVAAYAGYHGA-LADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYL 166
Cdd:cd08189 86 DAIIAIGGGSVIDCAKVIAARAANPKKsVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 167 LPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASL 246
Cdd:cd08189 166 IPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLASY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 247 MAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVEAMT 326
Cdd:cd08189 246 YAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIR 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533071 327 RLCAAVEIPSGLRSFgvPEDAIPAMAS----EAagierlmrnN-----PRKLSAADIEKIYRA 380
Cdd:cd08189 326 ELNRRMGIPTTLEEL--KEEDIPEIAKralkEA---------NplypvPRIMDRKDCEELLRK 377
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-378 |
1.01e-118 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 348.80 E-value: 1.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 5 SFKIAHKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDRAYEIFDRVLPDPEIAIVEDCMRAYRE 84
Cdd:cd08196 2 SYYQPVKIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAVFSDVEPNPTVENVDKCARLARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 85 GGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLF-GVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVS 163
Cdd:cd08196 82 NGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLeGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 164 DYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMAT 243
Cdd:cd08196 162 PGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKMAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 244 ASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNiaglSVNDAADqAVE 323
Cdd:cd08196 242 ASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFK----DAEELAD-KIE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504533071 324 AMTRlcaAVEIPSGLRSFGVPEDAIPAMASEAAGIERlMRNNPRKLSAADIEKIY 378
Cdd:cd08196 317 ELKK---RIGLRTRLSELGITEEDLEEIVEESFHPNR-ANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-377 |
1.31e-118 |
|
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: 348.72 E-value: 1.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDvDNPLIVTDAALVQSGTVALALEHL--GDRAYEIFDRVlPDPEIAIVEDCMRAYREGGHD 88
Cdd:cd08183 3 RIVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALeaAGIEVALFSVS-GEPTVETVDAAVALAREAGCD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 89 GLIGVGGGSAIDIAKSVAAYAGYHGALAD-LFGV-DQVPRKGPPL--IAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSD 164
Cdd:cd08183 81 VVIAIGGGSVIDAAKAIAALLTNEGSVLDyLEVVgKGRPLTEPPLpfIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 165 YLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATA 244
Cdd:cd08183 161 SMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 245 SLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIA----QAMGVNIAGLSVNDAADQ 320
Cdd:cd08183 241 SLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSPalarYRELAGILTGDPDAAAED 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 504533071 321 AVEAMTRLCAAVEIPsGLRSFGVPEDAIPAMASEAAGIERlMRNNPRKLSAADIEKI 377
Cdd:cd08183 321 GVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSS-MKGNPIELSDEELLEI 375
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
15-381 |
1.59e-118 |
|
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: 348.35 E-value: 1.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGD--RAYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIG 92
Cdd:cd14861 9 GAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAagLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 93 VGGGSAIDIAKSVAAYAGYHGALAD----LFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLP 168
Cdd:cd14861 89 LGGGSAIDAAKAIALMATHPGPLWDyedgEGGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 169 DVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMA 248
Cdd:cd14861 169 KVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 249 GMAFGNaGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGlsvndaADQAVEAMTRL 328
Cdd:cd14861 249 AVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGG------FDDFIAWVEDL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 504533071 329 CAAVEIPSGLRSFGVPEDAIPAMASEAAGiERLMRNNPRKLSAADIEKIYRAA 381
Cdd:cd14861 322 NERLGLPATLSELGVTEDDLDELAELALA-DPCHATNPRPVTAEDYRALLREA 373
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
6-379 |
1.34e-106 |
|
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: 316.74 E-value: 1.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 6 FKIAHKLLTGAGAIEQLAaeltRLDVDNPLIVTDAALVQSGTVALALEHLGDRA-YEIFDRVLPDPEIAIVEDCMRAYRE 84
Cdd:cd08180 1 FSLKTKIYSGEDSLERLK----ELKGKRVFIVTDPFMVKSGMVDKVTDELDKSNeVEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 85 GGHDGLIGVGGGSAIDIAKSVAAYAGYHgaladlfgvdQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSD 164
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAKAIIYFALKQ----------KGNIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 165 YLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATA 244
Cdd:cd08180 147 SMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 245 SLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVmhwnklacvermqdiaqamgvnIAGLsvndaadqaVEA 324
Cdd:cd08180 227 SCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYV----------------------IEFL---------IAA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 504533071 325 MTRLCAAVEIPSGLRSFGVPED----AIPAMAsEAAGIERLMRNNPRKLSAADIEKIYR 379
Cdd:cd08180 276 IRRLNKKLGIPSTLKELGIDEEefekAIDEMA-EAALADRCTATNPRKPTAEDLIELLR 333
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
15-382 |
1.68e-105 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 315.40 E-value: 1.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIG 92
Cdd:PRK10624 14 GRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAglAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 93 VGGGSAIDIAKSVAAYAGyHGALAD---LFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLPD 169
Cdd:PRK10624 94 IGGGSPQDTCKAIGIISN-NPEFADvrsLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 170 VALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPAnlQARDDMATASLMAG 249
Cdd:PRK10624 173 VAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGDK--EAGEGMALGQYIAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 250 MAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVEAMTRLC 329
Cdd:PRK10624 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALN 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 504533071 330 AAVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:PRK10624 331 RDVGIPPHLRDVGVKEEDIPALA-QAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
11-382 |
7.69e-97 |
|
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: 293.33 E-value: 7.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLaaelTRLDVDNPLIVTDA-ALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGH 87
Cdd:cd08179 7 DIYFGEGALEYL----KTLKGKRAFIVTGGgSMKRNGFLDKVEDYLKEAgmEVKVFEGVEPDPSVETVEKGAEAMREFEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 88 DGLIGVGGGSAIDIAKSVAAYAGY-HGALADLFGVDQVP--RKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSD 164
Cdd:cd08179 83 DWIIAIGGGSVIDAAKAMWVFYEYpELTFEDALVPFPLPelRKKARFIAIPSTSGTGSEVTRASVITDTEKGIKYPLASF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 165 YLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATA 244
Cdd:cd08179 163 EITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHNA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 245 SLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQamgvnIAGLSVNDAADQAVEA 324
Cdd:cd08179 243 SCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAAL-----LIGLTDEELVEDLIEA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504533071 325 MTRLCAAVEIPSGLRSFGVPEDA----IPAMAsEAAGIERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:cd08179 318 IEELNKKLGIPLSFKEAGIDEDEffakLDEMA-ENAMNDACTGTNPRKPTVEEMKELLKAAY 378
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-379 |
2.83e-95 |
|
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: 289.40 E-value: 2.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAaELTRLDVDNPLIVTDA-ALVQSGT---VALALEHLGdRAYEIFDRVLPDPEIAIVEDCMRAYREGG 86
Cdd:cd08185 6 RILFGAGKLNELG-EEALRPGKKALIVTGKgSSKKTGLldrVKKLLEKAG-VEVVVFDKVEPNPLTTTVMEGAALAKEEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 87 HDGLIGVGGGSAIDIAKSVAAYAGYHGALAD-LF---GVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIV 162
Cdd:cd08185 84 CDFVIGLGGGSSMDAAKAIAFMATNPGDIWDyIFggtGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 163 SDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMA 242
Cdd:cd08185 164 HPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKMA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 243 TASLMAGMAFGNAGVGAVHALAYPLGGRF-NIAHGVSNALLLPYVMHWNKLACVERMQDIAQAmgvNIAGLSVNDAADQA 321
Cdd:cd08185 244 WASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA---EASGLSDAKAAEDF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 504533071 322 VEAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGI-ERLMRNNPRKLSAADIEKIYR 379
Cdd:cd08185 321 IEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMETmGGLFANNPVELTEEDIVEIYE 379
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
17-379 |
1.66e-91 |
|
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: 280.23 E-value: 1.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 17 GAIEQLAAELtrLDVDNPLIVTDAALVQSGTVALALEHLGDR--AYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIGVG 94
Cdd:cd08178 11 GCLPYLLLEL--PGVKRAFIVTDRVLYKLGYVDKVLDVLEARgvETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 95 GGSAIDIAKSVaaYAGYHGALADLFGVDQV---PRK----GPP------LIAIPTTAGTGSEVTNVAILSDKAAQlKKGI 161
Cdd:cd08178 89 GGSAMDAAKIM--WLFYEHPETKFEDLAQRfmdIRKrvykFPKlgkkakLVAIPTTSGTGSEVTPFAVITDDKTG-KKYP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 162 VSDY-LLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDD 240
Cdd:cd08178 166 LADYaLTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 241 MATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWN------KLAC---------VERMQDIAQAM 305
Cdd:cd08178 246 MHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNatdpptKQAAfpqykyyvaKERYAEIADLL 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533071 306 GVNiaGLSVNDAADQAVEAMTRLCAAVEIPSGLRSFGVPED----AIPAMASEAAGiERLMRNNPRKLSAADIEKIYR 379
Cdd:cd08178 326 GLG--GKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEAdflaAVDKLAEDAFD-DQCTGANPRYPLISELKEILL 400
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
11-379 |
1.93e-91 |
|
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: 279.11 E-value: 1.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDRA-YEIFDRVLPDPEIAIVEDCMRAYREGGHDG 89
Cdd:cd08182 3 KIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGRIpVVVFSDFSPNPDLEDLERGIELFRESGPDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 90 LIGVGGGSAIDIAKSVAAYAGY-HGALADLFGVDQVPR-KGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLL 167
Cdd:cd08182 83 IIAVGGGSVIDTAKAIAALLGSpGENLLLLRTGEKAPEeNALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 168 PDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLM 247
Cdd:cd08182 163 PDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 248 AGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVM--HWNKLA---CVERMQDIAQAMGVNiaglsvndAADQAV 322
Cdd:cd08182 243 AGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLryNAGADDecdDDPRGREILLALGAS--------DPAEAA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 504533071 323 EAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGIERlMRNNPRKLSAADIEKIYR 379
Cdd:cd08182 315 ERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPER-LKNNPVRLSEEDLLRLLE 370
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-378 |
8.90e-89 |
|
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: 272.56 E-value: 8.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAaeltRLDVDNPLIVTDAALVQSGTVALALEHL--GDRAYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIG 92
Cdd:cd14862 12 GEDALSHLE----QLSGKRALIVTDKVLVKLGLLKKVLKRLlqAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 93 VGGGSAIDIAKsvAAYAGYHGALADLFGVDQVP----RKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLP 168
Cdd:cd14862 88 LGGGSVMDAAK--AAWVLYERPDLDPEDISPLDllglRKKAKLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 169 DVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMA 248
Cdd:cd14862 166 DVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 249 GMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERmqdIAQAMGVNIAGLSVNDAADQAVEAMTRL 328
Cdd:cd14862 246 GLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDER---YDLLKLLGIEARDEEEALKKLVEAIREL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504533071 329 CAAVEIPSGLRSFGVPED----AIPAMASEAAG-IERLMrnNPRKLSAADIEKIY 378
Cdd:cd14862 323 YKEVGQPLSIKDLGISEEefeeKLDELVEYAMEdSCTIT--SPRPPSEEDLKKLF 375
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
1-381 |
1.08e-85 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 264.89 E-value: 1.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 1 MSTSSFKIAHKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDRAYE--IFDRVLPDPEIAIVEDC 78
Cdd:PRK09860 1 MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFsvIYDGTQPNPTTENVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 79 MRAYREGGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLK 158
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 159 KGIVSDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQAR 238
Cdd:PRK09860 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 239 DDMATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAA 318
Cdd:PRK09860 241 EAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533071 319 DQAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGiERLMRNNPRKLSAADIEKIYRAA 381
Cdd:PRK09860 321 EACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALK-DACGFTNPIQATHEEIVAIYRAA 382
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
6-382 |
4.48e-84 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 273.21 E-value: 4.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 6 FKIAHKLLTGAGAIEQLAAELtrLDVDNPLIVTDAALVQSGTVALALEHLGDR----AYEIFDRVLPDPEIAIVEDCMRA 81
Cdd:PRK13805 457 FKVPKKIYFERGSLPYLLDEL--DGKKRAFIVTDRFMVELGYVDKVTDVLKKRengvEYEVFSEVEPDPTLSTVRKGAEL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 82 YREGGHDGLIGVGGGSAIDIAKsvAAYAGYHGALADLFGVDQV---PRKG----PP------LIAIPTTAGTGSEVTNVA 148
Cdd:PRK13805 535 MRSFKPDTIIALGGGSPMDAAK--IMWLFYEHPETDFEDLAQKfmdIRKRiykfPKlgkkakLVAIPTTSGTGSEVTPFA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 149 ILSDKAAQLKKGIVsDY-LLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPK 227
Cdd:PRK13805 613 VITDDKTGVKYPLA-DYeLTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPR 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 228 AYANPA-NLQARDDMATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWN-----KLA-------- 293
Cdd:PRK13805 692 SYKNGAkDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNatdppKQAafpqyeyp 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 294 -CVERMQDIAQAMGvnIAGLSVNDAADQAVEAMTRLCAAVEIPSGLRSFGVPED----AIPAMASEA-------Agierl 361
Cdd:PRK13805 772 rADERYAEIARHLG--LPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEAdflaKLDELAELAfddqctgA----- 844
|
410 420
....*....|....*....|.
gi 504533071 362 mrnNPRKLSAADIEKIYRAAY 382
Cdd:PRK13805 845 ---NPRYPLISELKEILLDAY 862
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-379 |
9.10e-82 |
|
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: 254.05 E-value: 9.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 6 FKIAHKLLTGAGAIEQLAAELTRLDvDNPLIVTDA-------ALvqsGTVALALEHLGDrAYEIFDRVLPDPEIAIVEDC 78
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALG-KKALIVTGKhsakkngSL---DDVTEALEENGI-EYFIFDEVEENPSIETVEKG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 79 MRAYREGGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFgVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLK 158
Cdd:cd08181 76 AELARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLF-QNGKYNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 159 KGIVSDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQAR 238
Cdd:cd08181 155 KSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 239 DDMATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNiaglSVNDAA 318
Cdd:cd08181 235 EKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFG----SIEEFQ 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504533071 319 DQaveaMTRLCAAVEIpsglrsfgVPEDAIPAMASEAAGIERlMRNNPRKLSAADIEKIYR 379
Cdd:cd08181 311 KF----LNRLLGKKEE--------LSEEELEKYADEAMKAKN-KKNTPGNVTKEDILRIYR 358
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
11-379 |
2.41e-73 |
|
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: 233.09 E-value: 2.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDvDNPLIVTD-AALVQSGTVALALEHLGDRAYEI--FDRVLPDPEIAIVEDCMRAYREGGH 87
Cdd:cd08187 9 KIIFGKGAIEELGEEIKKYG-KKVLLVYGgGSIKKNGLYDRVVASLKEAGIEVveFGGVEPNPRLETVREGIELAREENV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 88 DGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLL 167
Cdd:cd08187 88 DFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 168 PDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSL-HASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASL 246
Cdd:cd08187 168 PKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGtEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAAT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 247 MA--GM-AFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERmqdIAQaMGVNI----AGLSVNDAAD 319
Cdd:cd08187 248 LAlnGLlGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPER---FAQ-FARRVfgidPGGDDEETAL 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 320 QAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMASEAAGIERLMRNNpRKLSAADIEKIYR 379
Cdd:cd08187 324 EGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGF-KPLTREDIEEILK 382
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
70-382 |
8.21e-73 |
|
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: 231.34 E-value: 8.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 70 PEIAIVEDCMRAYREGGHDGLIGVGGGSAIDIAKSVAAyaGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAI 149
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLAL--KGISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 150 LSDKAAQLKKGIVSDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPK-- 227
Cdd:cd14860 140 VELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEia 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 228 AYANPANLQARDDMATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHW----NKLACVERMQDIaq 303
Cdd:cd14860 220 EKGEEARFPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNyqekNPDGEIKKLNEF-- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 304 amgvnIAGLsVNDAADQAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMA-SEAAGIERLMRNNPRKLSAADIEKIYRAAY 382
Cdd:cd14860 298 -----LAKI-LGCDEEDVYDELEELLNKILPKKPLHEYGMKEEEIDEFAdSVMENQQRLLANNYVPLDREDVAEIYKELY 371
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
5-381 |
1.98e-66 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 215.66 E-value: 1.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 5 SFKIAHKLLTGAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEHLGDRAYEIFDRVLPDPEIAIVEDC--MRAY 82
Cdd:PRK15454 23 TFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCaaVAQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 83 REGGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIV 162
Cdd:PRK15454 103 RESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 163 SDYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMA 242
Cdd:PRK15454 183 HASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESML 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 243 TASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMgvniaglsVNDAAD--Q 320
Cdd:PRK15454 263 LASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL--------RTKKSDdrD 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504533071 321 AVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKLSAADIEKIYRAA 381
Cdd:PRK15454 335 AINAVSELIAEVGIGKRLGDVGATSAHYGAWA-QAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
15-382 |
2.38e-66 |
|
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: 213.52 E-value: 2.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAAlvQSGTVALALEHLGDRAYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIGVG 94
Cdd:cd08177 7 GAGTLAELAEELERLGARRALVLSTPR--QRALAERVAALLGDRVAGVFDGAVMHVPVEVAERALAAAREAGADGLVAIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 95 GGSAIDIAKSVAAyagyhgaladlfgvdqvpRKGPPLIAIPTTAgTGSEVTNvaILSDKAAQLKKGIVSDYLLPDVALIS 174
Cdd:cd08177 85 GGSAIGLAKAIAL------------------RTGLPIVAVPTTY-AGSEMTP--IWGETEDGVKTTGRDPRVLPRTVIYD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 175 PQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMAGMAFGN 254
Cdd:cd08177 144 PDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 255 AGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGvniaglsvndaADQAVEAMTRLCAAVEI 334
Cdd:cd08177 224 VGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALG-----------GGDAAGGLYDLARRLGA 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504533071 335 PSGLRSFGVPEDAIPAMASEAAGIErlmRNNPRKLSAADIEKIYRAAY 382
Cdd:cd08177 293 PTSLRDLGMPEDDIDRAADLALANP---YPNPRPVERDALRALLERAW 337
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-381 |
8.03e-66 |
|
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: 213.63 E-value: 8.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALALEH-LGDRAYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIGV 93
Cdd:cd14866 11 GRGALARLGRELDRLGARRALVVCGSSVGANPDLMDPVRAaLGDRLAGVFDGVRPHSPLETVEAAAEALREADADAVVAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 94 GGGSAIDIAKSVAAYAGYHGALADL---------FGVDQVPRKGPPLIAIPTTAgTGSEVTNVAILSDKAAQLKKGIVSD 164
Cdd:cd14866 91 GGGSAIVTARAASILLAEDRDVRELctrraedglMVSPRLDAPKLPIFVVPTTP-TTADVKAGSAVTDPPAGQRLALFDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 165 YLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAyANPANLQARDDMATA 244
Cdd:cd14866 170 KTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRL-ADDDDPAARADLVLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 245 SLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVniAGLSVNDAADQAVEA 324
Cdd:cd14866 249 AVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGV--ADAGDEASAAAVVDA 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 504533071 325 MTRLCAAVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKL-SAADIEKIYRAA 381
Cdd:cd14866 327 VEALLDALGVPTRLRDLGVSREDLPAIA-EAAMDDWFMDNNPRPVpTAEELEALLEAA 383
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
15-381 |
4.81e-63 |
|
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: 206.35 E-value: 4.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTD-AALVQSG---TVALALEHLGdRAYEIFDRVLPDPEIAIVEDCMRAYREGGHDGL 90
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGrSSYKKSGawdDVEKALEENG-IEYVVYDKVTPNPTVDQADEAAKLARDFGADAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 91 IGVGGGSAIDIAKSVAAYAGYHGALA-DLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYLLPD 169
Cdd:cd08186 86 IAIGGGSPIDTAKSVAVLLAYGGKTArDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 170 VALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATASLMAG 249
Cdd:cd08186 166 YAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 250 MAFGNAGVGAVHALAYPLGG-RFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSvnDAADQAVEAMTRL 328
Cdd:cd08186 246 IAIDNGLLHLTHALEHPLSGlKPELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGTP--DEAEKAARGVEEF 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 504533071 329 CAAVEIPSGLRSFGVPEDAIPAMASEAA---GIERLMRNNPRKLSAADIEKIYRAA 381
Cdd:cd08186 324 LFSVGFTEKLSDYGFTEDDVDRLVELAFttpSLDLLLSLAPVEVTEEVVREIYEES 379
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-382 |
1.60e-62 |
|
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: 204.84 E-value: 1.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 6 FKIAHKLLTGAGAIEQLAAELtRLDVDNPLIVTDAALVQSGTVALALEHLGDRAYE--IFDRVLPDPEIAIVEDCMRAYR 83
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEV-KEYGSRFLLITDPVLKESGLADKIVSSLEKAGISviVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 84 EGGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVS 163
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 164 DYLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMAT 243
Cdd:cd14864 160 QPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 244 ASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVNDAADQAVE 323
Cdd:cd14864 240 AGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504533071 324 AMTRLCAAVEIPSGLRSFGV--PEDAIPAMASEAAGIErlmrNNPRKLSAADIEKIYRAAY 382
Cdd:cd14864 320 GVRRLIAQLNLPTRLKDLDLasSLEQLAAIAEDAPKLN----GLPRSMSSDDIFDILKAAF 376
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
15-381 |
6.04e-62 |
|
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: 203.63 E-value: 6.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAAL-VQSGTVALALEHLGDRAYEIFDRVLPDPEIAIVEDCMRAYREGGHDGLIGV 93
Cdd:cd08192 7 GPGAVEALLHELATLGASRVFIVTSKSLaTKTDVIKRLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAGADLLVSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 94 GGGSAIDIAKSVA-AYAGYHGALADLFGVDQVPRKGP-------PLIAIPTTAgTGSEVTNVAILSDKAAQLKKGIVSDY 165
Cdd:cd08192 87 GGGSPIDAAKAVAlALAEDVTDVDQLDALEDGKRIDPnvtgptlPHIAIPTTL-SGAEFTAGAGATDDDTGHKQGFAHPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 166 LLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAYANPANLQARDDMATAS 245
Cdd:cd08192 166 LGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEARLKCQLAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 246 LMAGMAFGN-AGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMQDIAQAMGVNIAGLSVndAADQAVEA 324
Cdd:cd08192 246 WLSLFGLGSgVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGGLGR--EAADAADA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 504533071 325 MTRLCAAVEIPSGLRSFGVPEDAIPAMAsEAAGIERLMRNNPRKL-SAADIEKIYRAA 381
Cdd:cd08192 324 IDALIRELGLPRTLRDVGVGRDQLEKIA-ENALTDVWCRTNPRPItDKDDVLEILESA 380
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
11-382 |
6.07e-61 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 201.07 E-value: 6.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELtRLDVDNPLIVTDA-ALVQSGT---VALALEHLGdRAYEIFDRVLPDPEIAIVEDCMRAYREGG 86
Cdd:COG1979 11 KIIFGKGQIAKLGEEI-PKYGKKVLLVYGGgSIKKNGLydqVKAALKEAG-IEVVEFGGVEPNPRLETVRKGVELCKEEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 87 HDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDYL 166
Cdd:COG1979 89 IDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 167 LPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHA-SPITDALAIGAIR-LIASAlPKAYANPANLQARDDMATA 244
Cdd:COG1979 169 FPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVdAPLQDRFAEGLLRtLIEEG-PKALKDPEDYDARANLMWA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 245 SLMA--GMAfgNAGVG---AVHALAYPLGGRFNIAHGVSNALLLPYVMHWNKLACVERMqdiAQaMGVNIAGL---SVND 316
Cdd:COG1979 248 ATLAlnGLI--GAGVPqdwATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKF---AQ-YAERVWGItegDDEE 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504533071 317 AADQAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMAseaagiERLMRN------NPRKLSAADIEKIYRAAY 382
Cdd:COG1979 322 RALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMA------EKATAHgmtalgEFKDLTPEDVREILELAL 387
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
11-279 |
1.01e-34 |
|
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: 130.85 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLA---AELTRLDVDNPLIVTDAALVQSGTVALALEHLGDraYEIFDRVLPDP---EIAIVEDCMRAYRE 84
Cdd:cd08184 3 KYLFGRGSFDQLGellAERRKSNNDYVVFFIDDVFKGKPLLDRLPLQNGD--LLIFVDTTDEPktdQIDALRAQIRAEND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 85 GGHDGLIGVGGGSAIDIAKSVAAYAGYHGALADLFGVDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKaaQLKKGIVSD 164
Cdd:cd08184 81 KLPAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGP--EKKLGINSD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 165 YLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHASPITDALAIGAIRLIASALPKAyaNPANLQARDDMATA 244
Cdd:cd08184 159 YTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLSD--DMMSPENREKLMVA 236
|
250 260 270
....*....|....*....|....*....|....*
gi 504533071 245 SLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSN 279
Cdd:cd08184 237 SYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
11-355 |
1.84e-28 |
|
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: 112.07 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDvDNPLIVTDAALVQsGTVALALEHLGDR-AYEIFDRVLPDPEIAIVEDCMRAYREGGHDG 89
Cdd:cd07766 3 RIVFGEGAIAKLGEIKRRGF-DRALVVSDEGVVK-GVGEKVADSLKKGlAVAIFDFVGENPTFEEVKNAVERARAAEADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 90 LIGVGGGSAIDIAKSVAAYAgyhgaladlfgvdqvpRKGPPLIAIPTTAGTGSEVTNVAILSDKaaQLKKGIVSDYLLPD 169
Cdd:cd07766 81 VIAVGGGSTLDTAKAVAALL----------------NRGIPFIIVPTTASTDSEVSPKSVITDK--GGKNKQVGPHYNPD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 170 VALISPQMTLTCPRGVTAASGVDALVHAIEsylslhaspitdalaigairliasalpkayanpanlqaRDDMATASLMAG 249
Cdd:cd07766 143 VVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAATLAG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 250 MAFGNA-GVGAVHALAYPLGGRFNIAHGVSNALLLPYVmhwnkLACVERMqdiaqamgvniaglsvNDAADQAVEAMTRL 328
Cdd:cd07766 185 MGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYV-----LKVANDM----------------NPEPEAAIEAVFKF 243
|
330 340
....*....|....*....|....*..
gi 504533071 329 CAAVEIPSGLRSFGVPEDAIPAMASEA 355
Cdd:cd07766 244 LEDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
11-381 |
1.09e-25 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 106.80 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRldvDNPLIVT--DAALVQSGTVALALEHLGDRAYEIFDRVLPDPEIAIVEDCMRAYREGGHD 88
Cdd:PRK15138 11 RILFGKGAIAGLREQIPA---DARVLITygGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPTYETLMKAVKLVREEKIT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 89 GLIGVGGGSAIDIAKSVAAYAGYHGAlADLFGVDQVP----RKGPPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSD 164
Cdd:PRK15138 88 FLLAVGGGSVLDGTKFIAAAANYPEN-IDPWHILETGgkeiKSAIPMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 165 YLLPDVALISPQMTLTCPRGVTAASGVDALVHAIESYLSLHA-SPITDALAIGAIRLIASALPKAYANPANLQARDDMAT 243
Cdd:PRK15138 167 HVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVdAKIQDRFAEGILLTLIEEGPKALKEPENYDVRANVMW 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 244 ASLMAGMAFGNAGVG---AVHALAYPLGGRFNIAHGVSNALLLPYVmhWNKLACVERMQDIAQAMGV-NIAGLSVNDAAD 319
Cdd:PRK15138 247 AATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQYAERVwNITEGSDDERID 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533071 320 QAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAMAS--EAAGIERLMRNnpRKLSAADIEKIYRAA 381
Cdd:PRK15138 325 AAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKklEEHGMTQLGEH--HDITLDVSRRIYEAA 386
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
15-261 |
2.90e-15 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 74.65 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTDAALVQSGTVALAlEHLGDRAYE--IFDRVLPDPEIAIVEDCMRAYREGGHDGLIG 92
Cdd:pfam13685 3 GPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVA-ESLKRAGIEveTRLEVAGNADMETAEKLVGALRERDADAVVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 93 VGGGSAIDIAKSVAAyagyhgaladlfgvdqvpRKGPPLIAIPTTA---GTGSevTNVAILSDKA-----AQLKKGIVSD 164
Cdd:pfam13685 82 VGGGTVIDLAKYAAF------------------KLGKPFISVPTAAsndGFAS--PGASLTVDGKkrsipAAAPFGVIAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 165 yllpdvalisPQMTLTCPRGVTaASGVDALVHAI----ESYLSlHASPITDALAIGAIRLIASALPKAYANPANLQARDD 240
Cdd:pfam13685 142 ----------TDVIAAAPRRLL-ASGVGDLLAKItavaDWELA-HAEEVAAPLALLSAAMVMNFADRPLRDPGDIEALAE 209
|
250 260
....*....|....*....|.
gi 504533071 241 MATASLMAGMAFGNAGVGAVH 261
Cdd:pfam13685 210 LLSALAMGGAGSSRPASGSEH 230
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
5-381 |
2.52e-11 |
|
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: 64.42 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 5 SFKIAHKLLTGAGAIEQLAAELTRLDvDNPLIVTDAAlvqsgtvalALEHLGDRAYEIFDRVLPDPEIAI---------V 75
Cdd:COG0371 2 VIILPRRYVQGEGALDELGEYLADLG-KRALIITGPT---------ALKAAGDRLEESLEDAGIEVEVEVfggecseeeI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 76 EDCMRAYREGGHDGLIGVGGGSAIDIAKSVAAYAGYhgaladlfgvdqvprkgpPLIAIPTTAGTGSEVTNVAILSDKAa 155
Cdd:COG0371 72 ERLAEEAKEQGADVIIGVGGGKALDTAKAVAYRLGL------------------PVVSVPTIASTDAPASPLSVIYTED- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 156 qlkkGIVSDYLL----PDVALISPQMTLTCPRGVTAASGVDAL-----VHAIESYLSLHASPITDALAIGAIRLIASAL- 225
Cdd:COG0371 133 ----GAFDGYSFlaknPDLVLVDTDIIAKAPVRLLAAGIGDALakwyeARDWSLAHRDLAGEYYTEAAVALARLCAETLl 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 226 ---PKAYANPANLQARDD----MATASLMAGMAFG----NAGVGAvhalayplggrfniAHGVSNAL-LLPY---VMHWN 290
Cdd:COG0371 209 eygEAAIKAVEAGVVTPAlervVEANLLLSGLAMGigssRPGSGA--------------AHAIHNGLtALPEthhALHGE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 291 KLA----CVERMQDiaqamgvniaglsvndaADQAVEAMTRLCAAVEIPSGLRSFGVPEDAIPAM--ASEAAGIER-LMR 363
Cdd:COG0371 275 KVAfgtlVQLVLEG-----------------RPEEIEELLDFLRSVGLPTTLADLGLDDETEEELltVAEAARPERyTIL 337
|
410
....*....|....*...
gi 504533071 364 NNPRKLSAADIEKIYRAA 381
Cdd:COG0371 338 NLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
15-263 |
7.35e-10 |
|
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: 59.86 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLdVDNPLIVTDAAlvqsgtvalALEHLGDRAYEIFDRVLPDPEIAI---------VEDCMRAYREG 85
Cdd:cd08550 7 EPGILAKAGEYIAPL-GKKALIIGGKT---------ALEAVGEKLEKSLEEAGIDYEVEVfggecteenIERLAEKAKEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 86 GHDGLIGVGGGSAIDIAKsvaayagyhgALADLFGVdqvprkgpPLIAIPTTAGTGSEVTNVAILSDKAAQLKKGIVSDY 165
Cdd:cd08550 77 GADVIIGIGGGKVLDTAK----------AVADRLGL--------PVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 166 lLPDVALISPQMTLTCPRGVTAASGVDALVHAIEsylslhASPITDALAIGAIRLIASAL------------PKAYANPA 233
Cdd:cd08550 139 -SPDLVLVDTDIIAAAPVRYLAAGIGDTLAKWYE------ARPSSRGGPDDLALQAAVQLaklaydllleygVQAVEDVR 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 504533071 234 N---LQARDDMATASLM-AGMAFG----NAGVGAVHAL 263
Cdd:cd08550 212 QgkvTPALEDVVDAIILlAGLVGSlgggGCRTAAAHAI 249
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
12-326 |
5.20e-09 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with 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. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 57.19 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 12 LLTGAGAIEQLAAELTRLDVDNPLIVTDaalvqSGTVALALEHLGDRAYEIFDrVLPDPEIAIVEDCMRAYreGGHDGLI 91
Cdd:cd08549 4 TIVGDGAINKIEEILKKLNLKRVLIITG-----KNTKAKYCRFFYDQLKTVCD-IVYYDNIDNLEDELKKY--TFYDCVI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 92 GVGGGSAIDIAKsVAAYagyhgaladlfgvdqvpRKGPPLIAIPTTA---GTGSEVTNVAILSDKA---AQLKKGIVSDy 165
Cdd:cd08549 76 GIGGGRSIDTGK-YLAY-----------------KLKIPFISVPTSAsndGIASPIVSLRIPGVKKtfmADAPIAIIAD- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 166 llPDVALISPQMTLtcprgvtaASGVDALVHAIESYLS------LHASPITDALAIGAIRLIASALPKAYANPANLQARD 239
Cdd:cd08549 137 --TEIIKKSPRRLL--------SAGIGDLVSNITAVLDwklahkEKGEKYSEFAAILSKTSAKELVSYVLKASDLEEYHR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 240 DMATASLMAGMAFGNAG-----VGAVHALAYPLGGRF------NIAHGVSNAL---LLPYV---MHWNKLACVERMQDIA 302
Cdd:cd08549 207 VLVKALVGSGIAMAIAGssrpaSGSEHLFSHALDKLKeeylniNVLHGEQVGVgtiIMSYLhekENKKLSGLHERIKMIL 286
|
330 340
....*....|....*....|....
gi 504533071 303 QAMGVNIAGLSVNDAADQAVEAMT 326
Cdd:cd08549 287 KKVGAPTTAKQLGIDEDLIIEALT 310
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
15-140 |
8.07e-09 |
|
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: 56.65 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDvDNPLIVTDAAlvqsgtvalALEHLGDRAYEIFDRVLPDPEIAI---------VEDCMRAYREG 85
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPF---------VLDLVGERLEESLEKAGLEVVFEVfggecsreeIERLAAIARAN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504533071 86 GHDGLIGVGGGSAIDIAKSVAAYAGYhgaladlfgvdqvprkgpPLIAIPTTAGT 140
Cdd:cd08170 77 GADVVIGIGGGKTIDTAKAVADYLGL------------------PVVIVPTIAST 113
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
10-173 |
3.91e-07 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 51.35 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 10 HKLLTGAGAIEQLAAELTRLDvDNPLIVTDAA---LVQSGTVALALEHLGDRAYEIFDRVLPDPEIAIVEDcmrAYREGG 86
Cdd:PRK09423 9 SKYVQGKGALARLGEYLKPLG-KRALVIADEFvlgIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVA---IAEENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 87 HDGLIGVGGGSAIDIAKSVAAYAGYhgaladlfgvdqvprkgpPLIAIPTTAGTGSEVTNVAILSDKAaqlkkGIVSDYL 166
Cdd:PRK09423 85 CDVVIGIGGGKTLDTAKAVADYLGV------------------PVVIVPTIASTDAPTSALSVIYTEE-----GEFERYL 141
|
170
....*....|.
gi 504533071 167 L----PDVALI 173
Cdd:PRK09423 142 FlpknPDLVLV 152
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
10-138 |
4.30e-07 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 51.40 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 10 HKLLTGAGAIEQLAAELTRLDVD-NPLIVTDAALVQS--GTVALALEHLGDRAYEIfDRVLPDpEIAIVEDCMRAYREGG 86
Cdd:cd08173 3 RNVVVGHGAINKIGEVLKKLLLGkRALIITGPNTYKIagKRVEDLLESSGVEVVIV-DIATIE-EAAEVEKVKKLIKESK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 504533071 87 HDGLIGVGGGSAIDIAKsVAAYagyhgaladlfgvdqvpRKGPPLIAIPTTA 138
Cdd:cd08173 81 ADFIIGVGGGKVIDVAK-YAAY-----------------KLNLPFISIPTSA 114
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
11-138 |
7.75e-07 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 50.66 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 11 KLLTGAGAIEQLAAELTRLDV-DNPLIVTdaalvqSGTValaLEHLGDRAYEIFDRVlPDPEIAIVED--------CMRA 81
Cdd:PRK00843 13 DVVVGHGVLDDIGDVCSDLKLtGRALIVT------GPTT---KKIAGDRVEENLEDA-GDVEVVIVDEatmeevekVEEK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504533071 82 YREGGHDGLIGVGGGSAIDIAKsVAAYagyhgaladlfgvdqvpRKGPPLIAIPTTA 138
Cdd:PRK00843 83 AKDVNAGFLIGVGGGKVIDVAK-LAAY-----------------RLGIPFISVPTAA 121
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
15-140 |
1.06e-05 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 47.13 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDVDNPLIVTdaalvqsgtvalalehlGDRAYEIFDRVLPD-----------------PEIA-IVE 76
Cdd:cd08172 7 EEGALKELPELLSEFGIKRPLIIH-----------------GEKSWQAAKPYLPKlfeieypvlrydgecsyEEIDrLAE 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533071 77 DCmrayREGGHDGLIGVGGGSAIDIAKSVAAYAGYhgaladlfgvdqvprkgpPLIAIPTTAGT 140
Cdd:cd08172 70 EA----KEHQADVIIGIGGGKVLDTAKAVADKLNI------------------PLILIPTLASN 111
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
15-138 |
2.02e-05 |
|
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: 45.97 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 15 GAGAIEQLAAELTRLDV--DNPLIVTDaalvqsgtvalalEHLGDRAYEIFDRVLPDP-EIAIVEDCM---------RAY 82
Cdd:cd08174 7 EEGALEHLGKYLADRNQgfGKVAIVTG-------------EGIDELLGEDILESLEEAgEIVTVEENTdnsaeelaeKAF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504533071 83 REGGHDGLIGVGGGSAIDIAKsvaaYAGYhgaladlfgvdqvpRKGPPLIAIPTTA 138
Cdd:cd08174 74 SLPKVDAIVGIGGGKVLDVAK----YAAF--------------LSKLPFISVPTSL 111
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
40-150 |
9.67e-04 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 40.97 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533071 40 AALVQSGTVALALEHLGDRA-YEIFDRVLPDPEIAivedcmRAyregghDGLIGVGGGSAIDIAKSVAAyagyhgaladl 118
Cdd:cd08171 43 AALEGSGLEITDFIWYGGEAtYENVEKLKANPEVQ------EA------DMIFAVGGGKAIDTVKVLAD----------- 99
|
90 100 110
....*....|....*....|....*....|..
gi 504533071 119 fgvdqvpRKGPPLIAIPTTAGTGSEVTNVAIL 150
Cdd:cd08171 100 -------RLNKPVFTFPTIASNCAAVTAVSVM 124
|
|
| |
