|
Name |
Accession |
Description |
Interval |
E-value |
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
8-359 |
1.37e-156 |
|
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: 443.39 E-value: 1.37e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQfKKIGIIYDPAIEGPILDKVTISLNQSNLDFISYKFPGECTYETIERLSHIMEQHDID 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLG-KKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 88 SIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEKTKRNPDIVLVDLDTIVQAPARFFA 167
Cdd:cd08170 80 VVIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 168 AGIGDAISKMFEVNQCKNAHGLNSFSTPPLETALLLANNTYSNLITWGKMAYEDVKQHHITPSVERVVESTVLLSGLGFE 247
Cdd:cd08170 160 AGMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 248 SGGLSLAHALIRGLTAIPELATNLHGELVAYGTVVQAVLENRKHIFIIELINFLKSVDLPTTIAELGYHqEISDSMLETI 327
Cdd:cd08170 240 SGGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLE-DVTDEELRKV 318
|
330 340 350
....*....|....*....|....*....|...
gi 262259464 328 IMHTLQNDYSKNFEP-PLNKENLKQAIIKTNHY 359
Cdd:cd08170 319 AEAACAPGETIHNMPfPVTPEDVVDAILAADAL 351
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
1-359 |
9.33e-133 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 383.40 E-value: 9.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 1 MLKIMGFPGEYIQGEHALRNISDIATRHQfKKIGIIYDPAIEGPILDKVTISLNQSNLDFISYKFPGECTYETIERLSHI 80
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLG-KRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 81 MEQHDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEKTKRNPDIVLVDLDTIVQ 160
Cdd:PRK09423 80 AEENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 161 APARFFAAGIGDAISKMFEVNQCKNAHGLNSFSTPPLETALLLANNTYSNLITWGKMAYEDVKQHHITPSVERVVESTVL 240
Cdd:PRK09423 160 APARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 241 LSGLGFESGGLSLAHALIRGLTAIPELATNLHGELVAYGTVVQAVLENRKHIFIIELINFLKSVDLPTTIAELGYHQEIS 320
Cdd:PRK09423 240 LSGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSD 319
|
330 340 350
....*....|....*....|....*....|....*....
gi 262259464 321 DSMLETIIMHTLQNDYSKNFEPPLNKENLKQAIIKTNHY 359
Cdd:PRK09423 320 EELRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAY 358
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-356 |
2.50e-118 |
|
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: 346.38 E-value: 2.50e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 3 KIMGFPGEYIQGEHALRNISDIATRHqFKKIGIIYDPAIEGPILDKVTISLNQSNLDFISYKFPGECTYETIERLSHIME 82
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADL-GKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 83 QHDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEKTKRNPDIVLVDLDTIVQAP 162
Cdd:COG0371 80 EQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 163 ARFFAAGIGDAISKMFEVNQCKNAHGLNsFSTPPLETALLLANNTYSNLITWGKMAYEDVKQHHITPSVERVVESTVLLS 242
Cdd:COG0371 160 VRLLAAGIGDALAKWYEARDWSLAHRDL-AGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 243 GLGF----ESGGLSLAHALIRGLTAIPELATNLHGELVAYGTVVQAVLENRkHIFIIELINFLKSVDLPTTIAELGYhQE 318
Cdd:COG0371 239 GLAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGR-PEEIEELLDFLRSVGLPTTLADLGL-DD 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 262259464 319 ISDSMLETIIMHTLQNDYS-KNFEPPLNKENLKQAIIKT 356
Cdd:COG0371 317 ETEEELLTVAEAARPERYTiLNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-356 |
3.77e-96 |
|
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: 289.44 E-value: 3.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHqFKKIGIIYDP----AIEGPILDkvtiSLNQSNLDFISYKFPGECTYETIERLSHIMEQ 83
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPL-GKKALIIGGKtaleAVGEKLEK----SLEEAGIDYEVEVFGGECTEENIERLAEKAKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 84 HDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEKTKRNPDIVLVDLDTIVQAPA 163
Cdd:cd08550 76 EGADVIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 164 RFFAAGIGDAISKMFE--VNQCKNAHGLnsfstpPLETALLLANNTYSNLITWGKMAYEDVKQHHITPSVERVVESTVLL 241
Cdd:cd08550 156 RYLAAGIGDTLAKWYEarPSSRGGPDDL------ALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 242 SGLGFESGG----LSLAHALIRGLTAIPELATNLHGELVAYGTVVQAVLENRKHIFIIELINFLKSVDLPTTIAELGyhQ 317
Cdd:cd08550 230 AGLVGSLGGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLG--L 307
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 262259464 318 EISDSMLETIIMHTLQNDYSKNFEP-PLNKENLKQAIIKT 356
Cdd:cd08550 308 ELTEEELRKIAEYACDPPDMAHMLPfPVTPEMLAEAILAA 347
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
8-355 |
4.68e-75 |
|
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: 235.49 E-value: 4.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQFKKIGIIYDP----AIEgPILDKvtisLNQSNLDFISYKfpGECTYETIERLSHIMEQ 83
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFGIKRPLIIHGEkswqAAK-PYLPK----LFEIEYPVLRYD--GECSYEEIDRLAEEAKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 84 HDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEKTKRNPDIVLVDLDTIVQAPA 163
Cdd:cd08172 74 HQADVIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 164 RFFAAGIGDAISKMFEVN-QCKNAHGLnsfsTPPLETALLLANNTYSNLITWGKMAYEDVKQHHITPSVERVVESTVLLS 242
Cdd:cd08172 154 DYFVAGIGDTLAKWYEADaILRQLEEL----PAFLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 243 GL--GF--ESGGLSLAHALIRGLTAIPELATNLHGELVAYGTVVQAVLENRKHIfIIELINFLKSVDLPTTIAELGYhQE 318
Cdd:cd08172 230 GMvgGFgdEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGKWDE-IKKLLPFYRRLGLPTSLADLGL-TD 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 262259464 319 ISDSMLETIIMHTLQNDYSKNFEPP-LNKENLKQAIIK 355
Cdd:cd08172 308 DTEEALQKIAAFAASPEESIHLLPPdVTAEEVLQAIEK 345
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
7-356 |
1.45e-67 |
|
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: 216.23 E-value: 1.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 7 FPGEYIqGEHALRNISDIATRHQfKKIGIIYDP-AIEGpILDKVTISLNQSNL---DFISYkfPGECTYETIERLSHIME 82
Cdd:cd08171 1 LPSYTI-GEDAYDAIPKICSPYG-KKVVVIGGKkALAA-AKPKLRAALEGSGLeitDFIWY--GGEATYENVEKLKANPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 83 QHDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEKTKRNPDIVLVDLDTIVQAP 162
Cdd:cd08171 76 VQEADMIFAVGGGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 163 ARFFAAGIGDAISKMFEVN-QCKNAHgLNSFSTppleTALLLANNTYSNLITWGKMAYEDVKQHHITPSVERVVE----S 237
Cdd:cd08171 156 EKYLWAGIGDTLAKYYEVEfSARGDE-LDHTNA----LGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLdiivT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 238 TVLLSGL---GFESgglSLAHALIRGLTAIPELATN-LHGELVAYGTVVQAVLENRKHIFiIELINFLKSVDLPTTIAEL 313
Cdd:cd08171 231 TGLVSNLvepDYNS---SLAHALYYGLTTLPQIEEEhLHGEVVSYGVLVLLTVDGQFEEL-EKVYAFNKSIGLPTCLADL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 262259464 314 GyhqeISDSMLETIIMHTLQNDYSKNFEPPLNKENLKQAIIKT 356
Cdd:cd08171 307 G----LTVEDLEKVLDKALKTKDLRHSPYPITKEMFEEAIKDL 345
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-349 |
1.60e-53 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 180.49 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQfKKIGIIYDP-AIEGPILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQHD 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLG-ARALIVTDPgSLKSGLLDKVLASLEEAGIEVVVFdGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 86 IDSIIALGGGKAIDTTKGIS------------------KKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQ-GVEKTKR 146
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIAllltnpgdvwdylggkplTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKlGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 147 NPDIVLVDLDTIVQAPARFFAAGIGDAISKMFEVNQCKNAhglNSFSTPPLETALLLanntysnLITWGKMAYEDVKQhh 226
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGA---NPLTDALALEAIRL-------IAENLPRAVADGED-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 227 iTPSVERVVESTvLLSGLGFESGGLSLAHALIRGLTAIPELATNL-HGELVAYGT-----------------VVQAVLEN 288
Cdd:pfam00465 228 -LEARENMLLAS-TLAGLAFSNAGLGAAHALAHALGGRYGIPHGLaNAILLPYVLrfnapaapeklaqlaraLGEDSDEE 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262259464 289 RKHIFIIELINFLKSVDLPTTIAELGyhqeISDSMLETIIMHTLQNDYSKNFEPPLNKENL 349
Cdd:pfam00465 306 AAEEAIEALRELLRELGLPTTLSELG----VTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-352 |
1.04e-32 |
|
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: 124.56 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIAT--RHQFKKIGIIYDPAIEGPILDKVTISLNQSNLDFISYkfpgECTYETIErlsHIMEQ----HDID 87
Cdd:cd08174 7 EEGALEHLGKYLAdrNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVE----ENTDNSAE---ELAEKafslPKVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 88 SIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDA---PTSRLIIvydENHKV-QGVektkRNPDIVLVDLDTIVQAPA 163
Cdd:cd08174 80 AIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGiasPVAVLKV---DGKRKsLGA----KMPYGVIVDLDVIKSAPR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 164 RFFAAGIGDAISKM-------FEVNQCKNAHglNSFstppletALLLANNTYSNLITWGKMAYEDvkqhhiTPSVERVVE 236
Cdd:cd08174 153 RLILAGIGDLISNItalydwkLAEEKGGEPV--DDF-------AYLLSRTAADSLLNTPGKDIKD------DEFLKELAE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 237 STVlLSGLGFESGGLS---------LAHALirgltaiPELA--TNLHGELVAYGTVVQAVLENRKHIFIIElinFLKSVD 305
Cdd:cd08174 218 SLV-LSGIAMEIAGSSrpasgsehlISHAL-------DKLFpgPALHGIQVGLGTYFMSFLQGQRYEEIRD---VLKRTG 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 262259464 306 LPTTIAELGYHQEisdsMLETIIMHTLQ---NDYSKNFEPPLNKENLKQA 352
Cdd:cd08174 287 FPLNPSDLGLTKE----EFIEAVKLAPStrpGRYTILEELDLSEERLKEI 332
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
7-336 |
1.17e-32 |
|
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: 124.59 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 7 FPGEYIQGEHALRNISDIATRHQF-KKIGIIYDPAIEGPILDKVTISLNQSNLDFISYKFPGECTYETIERLSHIMEQHD 85
Cdd:cd08173 1 LPRNVVVGHGAINKIGEVLKKLLLgKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 86 IDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRL--IIVYDENHKVQGVEktkrnPDIVLVDLDTIVQAPA 163
Cdd:cd08173 81 ADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFasIKGGDKPYSIKAKA-----PIAIIADTEIISKAPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 164 RFFAAGIGDAISKMFEVNQCKNAHGLN--SFStpplETALLLANNTySNLItwgkMAYEDVKQHHITPSVERVVESTVlL 241
Cdd:cd08173 156 RLLAAGCGDLISNITAVKDWRLAHRLKgeYYS----EYAASLALMS-AKLI----IENADLIKPGLEEGVRTVVKALI-S 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 242 SGLGFE--------SGGLSL-AHALIRgLTAIPelatNLHGELVAYGTVVQAVLENRKHIFIIELinfLKSVDLPTTIAE 312
Cdd:cd08173 226 SGVAMSiagssrpaSGSEHLfSHALDK-LAPGP----ALHGEQCGVGTIMMAYLHGGDWKEIREA---LKKIGAPTTAKE 297
|
330 340
....*....|....*....|....*
gi 262259464 313 LGYHQEIsdsMLETIIM-HTLQNDY 336
Cdd:cd08173 298 LGLDKEI---IIEALTIaHKIRPER 319
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
3-328 |
1.04e-28 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 113.83 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 3 KIMGFPGEYIQGEHALRNISDIATRHQFKK-IGIIYDPAIEGPILDKVTISLNqsnlDFISYKF--PGECTYETIERLSH 79
Cdd:PRK00843 6 HWIQLPRDVVVGHGVLDDIGDVCSDLKLTGrALIVTGPTTKKIAGDRVEENLE----DAGDVEVviVDEATMEEVEKVEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 80 IMEQHDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRL--IIVYDENHKVQGVEktkrnPDIVLVDLDT 157
Cdd:PRK00843 82 KAKDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRasIKGGGKPVSVKAKP-----PLAVIADTEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 158 IVQAPARFFAAGIGDAISKMFEVNQCKNAHGLN--SFStpplETALLLAnntysnLITwGKMAYEDVKQhhITPSVE--- 232
Cdd:PRK00843 157 IAKAPYRLLAAGCGDIISNYTAVKDWRLAHRLRgeYYS----EYAAALS------LMT-AKMLIENADI--IKPGLEesa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 233 RVVESTVLLSGLGFE--------SGGLSL-AHALIRgltAIPELAtnLHGELVAYGTVVQAVL--ENRKHIFiieliNFL 301
Cdd:PRK00843 224 RLVVKALISSGVAMSiagssrpaSGSEHLfSHALDR---LAPGPA--LHGEQCGVGTIIMMYLhgGDWRKIR-----DAL 293
|
330 340
....*....|....*....|....*..
gi 262259464 302 KSVDLPTTIAELGyhqeISDsmlETII 328
Cdd:PRK00843 294 KKIGAPTTAKELG----IDD---EYII 313
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
64-359 |
5.61e-28 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 112.13 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 64 KFPGECTYETIERLSHiMEQHDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEK 143
Cdd:PRK10586 66 LFRGHCSESDVAQLAA-ASGDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 144 TKRNPDIVLVDLDTIVQAPARFFAAGIGDAISKMFE-VNQCKNAHGLNSFSTPPLETALLLANNtysnLITWGKMAYEDV 222
Cdd:PRK10586 145 FDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEaVVLAPQPETLPLTVRLGINNALAIRDV----LLNSSEQALADQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 223 KQHHITPSVERVVESTV----LLSGLGFESGGLSLAHALIRGLTAIPELATNLHGELVAYGTVVQAVLENRKHIfIIELI 298
Cdd:PRK10586 221 QNGQLTQDFCDVVDAIIagggMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDV-LAQLI 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262259464 299 NFLKSVDLPTTIAELGYhqEISD-SMLETIIMHTLQNDYSKNFEP-PLNKENLKQAIIKTNHY 359
Cdd:PRK10586 300 GAYQRFHLPTTLAELDV--DINNqAEIDRVIAHTLRPVESIHYLPvTLTPDTLRAAFEKVESF 360
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
14-277 |
2.15e-27 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 108.16 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDPAIEGPILDKVTISLNQSNLDFISykFPGECTYETIERLSHIMEQH---DIDSII 90
Cdd:pfam13685 3 GPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVAESLKRAGIEVET--RLEVAGNADMETAEKLVGALrerDADAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 91 ALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVydenhKVQGVEKT--KRNPDIVLVDLDTIVQAPARFFAA 168
Cdd:pfam13685 81 GVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASL-----TVDGKKRSipAAAPFGVIADTDVIAAAPRRLLAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 169 GIGDAISKMFEVNQCKNAHgLNSFSTPpleTALLLANNTYSNLitwgKMAYEDvkqHHITPSVERVVEStVLLSGLGFE- 247
Cdd:pfam13685 156 GVGDLLAKITAVADWELAH-AEEVAAP---LALLSAAMVMNFA----DRPLRD---PGDIEALAELLSA-LAMGGAGSSr 223
|
250 260 270
....*....|....*....|....*....|...
gi 262259464 248 --SGGLSL-AHALirGLTAIPELatnLHGELVA 277
Cdd:pfam13685 224 paSGSEHLiSHAL--DMIAPKQA---LHGEQVG 251
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-351 |
3.65e-22 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 96.34 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 1 MLKIMGFPGEYIQGEHALRNISDIATRHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISY-KFPGECTYETIERLS 78
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKlGLLDRVLDALEAAGIEVVVFdDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 79 HIMEQHDIDSIIALGGGKAIDTTKGIS------------------KKLNIPIIICPTVAS--SDApTSRLIIVYDENHkv 138
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIAllatnpgdledylgikkvPGPPLPLIAIPTTAGtgSEV-TPFAVITDPETG-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 139 qgvekTKRN-------PDIVLVDLDTIVQAPARFFAA-GIgDAIskmfevnqcknAHGLNSF----STPP-----LETAL 201
Cdd:COG1454 158 -----VKKGiadpellPDVAILDPELTLTLPPSLTAAtGM-DAL-----------THAIEAYvskgANPLtdalaLEAIR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 202 LLANN---TY---SNLITWGKMAYedvkqhhitpsvervvesTVLLSGLGFESGGLSLAHALIRGLTAIPELAtnlHGEL 275
Cdd:COG1454 221 LIARNlprAVadgDDLEAREKMAL------------------ASLLAGMAFANAGLGAVHALAHPLGGLFHVP---HGLA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 276 VAygTVVQAVLE-NRKHI-------------------------FIIELINFLKSVDLPTTIAELGyhqeISDSMLETIIM 329
Cdd:COG1454 280 NA--ILLPHVLRfNAPAAperyaeiaralgldvglsdeeaaeaLIEAIRELLRDLGIPTRLSELG----VTEEDLPELAE 353
|
410 420
....*....|....*....|..
gi 262259464 330 HTLQNDYSKNFEPPLNKENLKQ 351
Cdd:COG1454 354 LALADRCLANNPRPLTEEDIEA 375
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-351 |
3.65e-20 |
|
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: 90.67 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQHDIDSIIA 91
Cdd:cd14863 11 GAGAVEQIGELLKELGCKKVLLVTDKGLKKaGIVDKIIDLLEEAGIEVVVFdDVEPDPPDEIVDEAAEIAREEGADGVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 92 LGGGKAIDTTKGIS-------------------KKLNIPIIICPTVASSDAPTSRLIIVYDE-NHKVQGVEKTKRNPDIV 151
Cdd:cd14863 91 IGGGSVLDTAKAIAvlltnpgpiidyalagppvPKPGIPLIAIPTTAGTGSEVTPIAVITDEeNGVKKSLLGPFLVPDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 152 LVDLDTIVQAPARFFAA-GIgDAISkmfevnqcknaHGLNSFSTPpletalllANNTYSNLItwgkmAYEDVKqhHITPS 230
Cdd:cd14863 171 ILDPELTVGLPPSLTAAtGM-DALS-----------HAIEAYTSK--------LANPMTDAL-----ALQAIR--LIVKN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 231 VERVVE--------------STvlLSGLGFESGGLSLAHALIRGLTA---IPelatnlHGELVAYGTVVqaVLEN----- 288
Cdd:cd14863 224 LPRAVKdgdnlearenmllaSN--LAGIAFNNAGTHIGHAIAHALGAlyhIP------HGLACALALPV--VLEFnaeay 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 289 ----------------------RKHIFIIELINFLKSVDLPTTIAELGyhqeISDSMLETIImHTLQNDYSKNFEP-PLN 345
Cdd:cd14863 294 pekvkkiakalgvsfpgesdeeLGEAVADAIREFMKELGIPSLFEDYG----IDKEDLDKIA-EAVLKDPFAMFNPrPIT 368
|
....*.
gi 262259464 346 KENLKQ 351
Cdd:cd14863 369 EEEVAE 374
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
8-335 |
5.12e-20 |
|
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: 89.55 E-value: 5.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQFKKIGIIYDPAIEGPILDKVTISLNQsNLDFISYKfpgECTYETIERLSHIMeqhdID 87
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKKLNLKRVLIITGKNTKAKYCRFFYDQLKT-VCDIVYYD---NIDNLEDELKKYTF----YD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 88 SIIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSRLIIVydenhKVQGVEKTK--RNPDIVLVDLDTIVQAPARF 165
Cdd:cd08549 73 CVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSL-----RIPGVKKTFmaDAPIAIIADTEIIKKSPRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 166 FAAGIGDAISKMFEVNQCKNAHGLNsfSTPPLETALLLANNTYSNLITWGKMAYEDVKQHhitpsveRVVESTVLLSGLG 245
Cdd:cd08549 148 LSAGIGDLVSNITAVLDWKLAHKEK--GEKYSEFAAILSKTSAKELVSYVLKASDLEEYH-------RVLVKALVGSGIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 246 FESGGLS---------LAHALIRGLTAIPELATnLHGELVAYGTVVQAVL---ENRKHIFIIELIN-FLKSVDLPTTIAE 312
Cdd:cd08549 219 MAIAGSSrpasgsehlFSHALDKLKEEYLNINV-LHGEQVGVGTIIMSYLhekENKKLSGLHERIKmILKKVGAPTTAKQ 297
|
330 340
....*....|....*....|...
gi 262259464 313 LGYHQEISDSMLETiiMHTLQND 335
Cdd:cd08549 298 LGIDEDLIIEALTE--AHKIRPR 318
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-351 |
8.70e-19 |
|
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: 86.35 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQHD 85
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKaGLLDKVLESLKAAGIEVEVFdDVEPNPTVETVEAAAELAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 86 IDSIIALGGGKAIDTTKGIS------------------KKLNIPIIICPTVASSDAPTSRLIIVYDEnhkvqgVEKTKRN 147
Cdd:cd08551 81 ADLVIAVGGGSVLDTAKAIAvlatnggsirdyegigkvPKPGLPLIAIPTTAGTGSEVTPNAVITDP------ETGRKMG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 148 -------PDIVLVDLDTIVQAPARFFAA-GIgDAIskmfevnqcknAHGLNSFStppletalllanNTYSNLITWGkMAY 219
Cdd:cd08551 155 ivspyllPDVAILDPELTLSLPPSVTAAtGM-DAL-----------THAIEAYT------------SKKANPISDA-LAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 220 EDVKqhHITPSVERVVE--------------STvlLSGLGFESGGLSLAHALIRGLTA---IPelatnlHGELVA----- 277
Cdd:cd08551 210 EAIR--LIGKNLRRAVAdgsdleareamllaSL--LAGIAFGNAGLGAVHALAYPLGGryhIP------HGVANAillpy 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 278 ------------YGTVVQAVLENRK--------HIFIIELINFLKSVDLPTTIAELGyhqeISDSMLETIIMHTLQNDYS 337
Cdd:cd08551 280 vmefnlpacpekYAEIAEALGEDVEglsdeeaaEAAVEAVRELLRDLGIPTSLSELG----VTEEDIPELAEDAMKSGRL 355
|
410
....*....|....*
gi 262259464 338 KNFEP-PLNKENLKQ 351
Cdd:cd08551 356 LSNNPrPLTEEDIRE 370
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
14-331 |
6.44e-16 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) 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 a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 77.55 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDI-ATRHQFKKIGIIYDPAIEGPILDKVTISLNQSNLDFISYKFPGE----CTYETIERLShIMEQHDIDS 88
Cdd:cd08175 7 GEGALKKLPEYlKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEgdliADEAAVGKVL-LELEKDTDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 89 IIALGGGKAIDTTKGISKKLNIPIIICPTVASSDAPTSR--LIIVYdenhkvqGVEKT--KRNPDIVLVDLDTIVQAPAR 164
Cdd:cd08175 86 IIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSgaPIIVD-------GVKKTfpAHAPKAIFADLDVLANAPQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 165 FFAAGIGDAISKMfevnqcknahglnsfstppleTALL------LANNTYSNLITWGKMAY--EDVKQHH--ITP----S 230
Cdd:cd08175 159 MIAAGFGDLLGKY---------------------TALAdwklshLLGGEYYCPEVADLVQEalEKCLDNAegIAArdpeA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 231 VERVVEStVLLSGLGFESGGLS---------LAH-----ALIRGLTAIpelatnLHGELVAYGTVVQAvlenrkHIFII- 295
Cdd:cd08175 218 IEALMEA-LILSGLAMQLVGNSrpasgaehhLSHywemeFLRLGKPPV------LHGEKVGVGTLLIA------ALYILe 284
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 262259464 296 ------ELINFLKSVDLPTTIAELGyhqeISDSMLETIIMHT 331
Cdd:cd08175 285 qlpppeELRELLRKAGAPTTPEDLG----IDRDLLRDSLRLA 322
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-314 |
3.09e-14 |
|
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: 73.10 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 5 MGFPGEYIQGEHALRNISDIATRHqFKKIGIIYDPA-IEGPILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIME 82
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEY-GSRFLLITDPVlKESGLADKIVSSLEKAGISVIVFdEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 83 QHDIDSIIALGGGKAIDTTKGISKKLN------------------IPIIICPTVASSDAP-TSRLIIVYDENHKVQGVEK 143
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANndggaydflegakpkkkpLPLIAVPTTPRSGFEfSDRFPVVDSRSREVKLLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 144 TKRNPDIVLVDLDTIVQAPARFFAAGIGDAISKMFEVNQCKNAhglNSFSTPPLETAL-LLANNTYSnlitwgkmAYEDV 222
Cdd:cd14864 160 QPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKS---NFFSDALALKAIeLVSENLDG--------ALADP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 223 KQhhiTPSVERVVESTVlLSGLGFESGGLSLAHALIRGLTAI-------------PELATNLH--------------GEL 275
Cdd:cd14864 229 KN---TPAEELLAQAGC-LAGLAASSSSPGLATALALAVNSRykvskslvasillPHVIEYAAtsapdkyakiaralGED 304
|
330 340 350
....*....|....*....|....*....|....*....
gi 262259464 276 VAYGTVVQAVLEnrkhiFIIELINFLKSVDLPTTIAELG 314
Cdd:cd14864 305 VEGASPEEAAIA-----AVEGVRRLIAQLNLPTRLKDLD 338
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-173 |
5.07e-14 |
|
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: 72.56 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQHD 85
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKlGLVDKVTQLLAEAGIAYAVFdDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 86 IDSIIALGGGKAIDTTKGIS------------------KKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEKTKR- 146
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAvlatnggpirdymgprkvDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPAl 160
|
170 180
....*....|....*....|....*...
gi 262259464 147 NPDIVLVDLDTIVQAPARFFAA-GIgDA 173
Cdd:cd08194 161 LPAVAIVDPELTLSMPPRVTAAtGI-DA 187
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-328 |
3.37e-11 |
|
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: 63.79 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQFKKIgIIYDPAIEG-PILDKVTISLNQSNLDFISY-----KFPGECTYETIERLShim 81
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARLGSRVL-IVTDPRLAStPLVAELLAALTAAGVAVEVFdggqpELPVSTVADAAAAAR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 82 eQHDIDSIIALGGGKAIDTTKGISKKLN------------------IPIIICPTVASSDAPTSRLIIVYD-ENHKVQGVE 142
Cdd:cd08191 80 -AFDPDVVIGLGGGSNMDLAKVVALLLAhggdprdyygedrvpgpvLPLIAVPTTAGTGSEVTPVAVLTDpARGMKVGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 143 KTKRNPDIVLVDLDTIVQAPARFFA-AGIgDAISkmfevnqcknaHGLNSF-STPPLETALLLANNTY--SNLITwGKMA 218
Cdd:cd08191 159 SPYLRPAVAIVDPELTLTCPPGVTAdSGI-DALT-----------HAIESYtARDFPPFPRLDPDPVYvgKNPLT-DLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 219 YEDVKqhHITPSVERVVES------------TVLLSGLGFESGGLSLAHAL---IRGLTAIPELATNlhGELVAYgtVVQ 283
Cdd:cd08191 226 LEAIR--LIGRHLPRAVRDgddlearsgmalAALLAGLAFGTAGTAAAHALqypIGALTHTSHGVGN--GLLLPY--VMR 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262259464 284 AVLENRKHIF----------------------IIELINFLKSVDLPTTIAELGyhqeISDSMLETII 328
Cdd:cd08191 300 FNRPARAAELaeiaralgvttagtseeaadraIERVEELLARIGIPTTLADLG----VTEADLPGLA 362
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-154 |
9.21e-11 |
|
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: 62.60 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDP-AIEGPILDKVTISLNQSNLDFISyKFPGECTYETIERLSHIMEQHDIDSIIAL 92
Cdd:cd08196 12 GEGILKELPDIIKELGGKRGLLVTDPsFIKSGLAKRIVESLKGRIVAVFS-DVEPNPTVENVDKCARLARENGADFVIAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 93 GGGKAIDTTKGIS-------------------KKLNIPIIICPTVASSDAPTSRLIIVYD-ENHKVQGVEKTKRNPDIVL 152
Cdd:cd08196 91 GGGSVLDTAKAAAclaktdgsiedylegkkkiPKKGLPLIAIPTTAGTGSEVTPVAVLTDkEKGKKAPLVSPGFYPDIAI 170
|
..
gi 262259464 153 VD 154
Cdd:cd08196 171 VD 172
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
14-257 |
7.71e-10 |
|
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: 59.87 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDPAIEGP-ILDKVTISLNQSNLDFIsykfpgecTYETIERLSHIMEQHDI------ 86
Cdd:cd08176 12 GWGAIEEIGEEAKKRGFKKALIVTDKGLVKFgIVDKVTDVLKEAGIAYT--------VFDEVKPNPTIENVMAGvaayke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 87 ---DSIIALGGGKAIDTTKGI-------------------SKKLNIPIIICPTVASSDAPTSrliIVY-----DENHKVQ 139
Cdd:cd08176 84 sgaDGIIAVGGGSSIDTAKAIgiivanpgadvrslegvapTKNPAVPIIAVPTTAGTGSEVT---INYvitdtEKKRKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 140 GVEkTKRNPDIVLVDLDTIVQAPaRFFAAGIG-DAIskmfevnqcknAHGLNSFSTP---PLETALLLA--NNTYSNLI- 212
Cdd:cd08176 161 CVD-PHDIPTVAIVDPDLMSSMP-KGLTAATGmDAL-----------THAIEGYITKgawELSDMLALKaiELIAKNLRk 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 262259464 213 -TWGKMAYEDVKQHHItpsvervvesTVLLSGLGFESGGL----SLAHAL 257
Cdd:cd08176 228 aVANPNNVEARENMAL----------AQYIAGMAFSNVGLgivhSMAHPL 267
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
7-257 |
1.60e-09 |
|
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: 58.68 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 7 FPGEYIQGEHALRNISDIATRHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISYKF----PgecTYETIERLSHIM 81
Cdd:cd08188 5 IPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKlGLVKKVTDVLEEAGIEYVIFDGvqpnP---TVTNVNEGLELF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 82 EQHDIDSIIALGGGKAIDTTKGI------------------SKKLNIPIIICPTVASSDAPTSRLIIVYDENHKVQGVEK 143
Cdd:cd08188 82 KENGCDFIISVGGGSAHDCAKAIgilatnggeiedyegvdkSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 144 TKRN-PDIVLVDLDTIVQAPARFFAA-GIgDAISKMFEVNQCKNAHGL-NSFStppLETALLLANNTY------SNLITW 214
Cdd:cd08188 162 DWNVtPTIAVNDPELMLGMPPSLTAAtGM-DALTHAIEAYVSTGATPLtDALA---LEAIRLIAENLPkavangKDLEAR 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 262259464 215 GKMAYEDvkqhhitpsvervvestvLLSGLGFESGGLSLAHAL 257
Cdd:cd08188 238 ENMAYAQ------------------FLAGMAFNNAGLGYVHAM 262
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
14-347 |
3.54e-09 |
|
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: 57.83 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIAtRHQFKKIGIIY--DPAIEGPILDKVTISLNQSNLDFISykFPGectyetIE---RLSHIME------ 82
Cdd:cd08187 13 GKGAIEELGEEI-KKYGKKVLLVYggGSIKKNGLYDRVVASLKEAGIEVVE--FGG------VEpnpRLETVREgielar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 83 QHDIDSIIALGGGKAIDTTKGIS----------------KKLN--IPIIICPTVASSDAPTSRL-IIVYDENHKVQGVEK 143
Cdd:cd08187 84 EENVDFILAVGGGSVIDAAKAIAagakydgdvwdfftgkAPPEkaLPVGTVLTLAATGSEMNGGaVITNEETKEKLGFGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 144 TKRNPDIVLVDLDTIVQAPARFFAAGIGDAISKMFEvnqcknahglNSFSTPP--------LETALLlanntysNLITWG 215
Cdd:cd08187 164 PLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLE----------QYFTGTEdaplqdrlAEGLLR-------TVIENG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 216 KMAYEDvkqhhitPS-VE-R---VVESTVLLSGLgFESGG------------LS----LAHAliRGLTAI---------- 264
Cdd:cd08187 227 PKALKD-------PDdYEaRanlMWAATLALNGL-LGAGRggdwathaieheLSalydITHG--AGLAIVfpawmryvlk 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 265 --PE----LATNLHGeLVAYGTVVQAVLEnrkhiFIIELINFLKSVDLPTTIAELGyhqeISDSMLETIIMHTLQNDYSK 338
Cdd:cd08187 297 kkPErfaqFARRVFG-IDPGGDDEETALE-----GIEALEEFFKSIGLPTTLSELG----IDEEDIEEMAEKAVRGGGLG 366
|
....*....
gi 262259464 339 NFEPPLNKE 347
Cdd:cd08187 367 GGFKPLTRE 375
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-138 |
4.89e-09 |
|
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: 57.17 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISYK-FPGECTYETIERLSHIMEQHD 85
Cdd:cd14865 6 PTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAaGLLKKVEDALGDAIEIVGVFDdVPPDSSVAVVNEAAARAREAG 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262259464 86 IDSIIALGGGKAIDTTKG--------------------ISKKLnIPIIICPTVASSDAPTSRLIIVYDENHKV 138
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGvnillseggddlddygganrLTRPL-KPLIAIPTTAGTGSEVTLVAVIKDEEKKV 157
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-318 |
1.26e-08 |
|
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: 56.01 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 10 EYIQGEHALRNISDIATRHQFKKIGIIYDPAI-EGPILDKVTISLNQSNLDFISYK--FPGECTYEtIERLSHIMEQHDI 86
Cdd:cd17814 6 EFIFGVGARKLAGRYAKNLGARKVLVVTDPGViKAGWVDEVLDSLEAEGLEYVVFSdvTPNPRDFE-VMEGAELYREEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 87 DSIIALGGGKAIDTTKGIS---------------KKLNIPI--IIC-PTVASSDAPTSRLIIVYD--ENHKVQGVEKTKR 146
Cdd:cd17814 85 DGIVAVGGGSPIDCAKGIGivvsngghildyegvDKVRRPLppLICiPTTAGSSADVSQFAIITDteRRVKMAIISKTLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 147 nPDIVLVDLDTIVQAPARFFAAGIGDAISKMFEVnQCKNA-------HGLNSFSTppLETALLLANNTYSNLITWGKMAY 219
Cdd:cd17814 165 -PDVSLIDPETLTTMDPELTACTGMDALTHAIEA-YVSNAsspltdlHALEAIRL--ISENLPKAVADPDDLEAREKMML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 220 EDvkqhhitpsvervvestvLLSGLGFESGGLSLAHAL---IRGLTAIPelatnlHGELVA-----------------YG 279
Cdd:cd17814 241 AS------------------LQAGLAFSNASLGAVHAMahsLGGLLDLP------HGECNAlllphvirfnfpaaperYR 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 262259464 280 TVVQAV--------LENRKHIFIIELINFLKSVDLPTTIAELGYHQE 318
Cdd:cd17814 297 KIAEAMgldvdgldDEEVAERLIEAIRDLREDLGIPETLSELGVDEE 343
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
14-333 |
1.60e-08 |
|
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: 55.58 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIatrhQFKKIGIIYDPAIEG-PILDKVTISLNQSNldfiSYK-F------PgecTYETIERLSHIMEQHD 85
Cdd:cd08180 10 GEDSLERLKEL----KGKRVFIVTDPFMVKsGMVDKVTDELDKSN----EVEiFsdvvpdP---SIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 86 IDSIIALGGGKAIDTTKGI-------SKKLNIPIIIC-PTVAS--SDAPTSRLIIVYDENHKVQGVEKTKRnPDIVLVDL 155
Cdd:cd08180 79 PDTIIALGGGSAIDAAKAIiyfalkqKGNIKKPLFIAiPTTSGtgSEVTSFAVITDPEKGIKYPLVDDSML-PDIAILDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 156 DTIVQAPARFFA-AGIgDAISKMFEVNQCKNAhglNSFSTPPLETALLLAnntYSNLITwgkmAYEDV-------KQHHI 227
Cdd:cd08180 158 ELVKSVPPKVTAdTGM-DVLTHALEAYVSTNA---NDFTDALAEKAIKLV---FENLPR----AYRDGddleareKMHNA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 228 tpsvervveSTvlLSGLGFESGGL----SLAHALiRGLTAIPelatnlHGELVA----YgtVVQavlenrkhiFIIELIN 299
Cdd:cd08180 227 ---------SC--MAGIAFNNAGLginhSLAHAL-GGRFHIP------HGRANAillpY--VIE---------FLIAAIR 277
|
330 340 350
....*....|....*....|....*....|....*
gi 262259464 300 FL-KSVDLPTTIAELGYHQEISDSMLETIIMHTLQ 333
Cdd:cd08180 278 RLnKKLGIPSTLKELGIDEEEFEKAIDEMAEAALA 312
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
14-315 |
2.28e-08 |
|
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: 55.24 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQHDIDSIIA 91
Cdd:cd08190 7 GPGATRELGMDLKRLGAKKVLVVTDPGLAKlGLVERVLESLEKAGIEVVVYdGVRVEPTDESFEEAIEFAKEGDFDAFVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 92 LGGGKAIDTTK--------------------GISKKLN---IPIIICPTVASSDAPTSRLIIVYDENHKVqgveKT---K 145
Cdd:cd08190 87 VGGGSVIDTAKaanlyathpgdfldyvnapiGKGKPVPgplKPLIAIPTTAGTGSETTGVAIFDLEELKV----KTgisS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 146 RN--PDIVLVDLDTIVQAPARFFAAGIGDAISkmfevnqcknaHGLNSFSTPPLeTALLLANN-----TY--SNLIT--W 214
Cdd:cd08190 163 RYlrPTLAIVDPLLTLTLPPRVTASSGFDVLC-----------HALESYTARPY-NARPRPANpderpAYqgSNPISdvW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 215 GKMAYEdvkqhHITPSVERVVE--------------STvlLSGLGFESGGLSLAHAL---IRGLTA-------------I 264
Cdd:cd08190 231 AEKAIE-----LIGKYLRRAVNdgddlearsnmllaST--LAGIGFGNAGVHLPHAMaypIAGLVKdyrppgypvdhphV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262259464 265 PelatnlHGELVAYGTVvqAVLE------NRKHIFIIEL---------------------INFLKSVDLPTTIAELGY 315
Cdd:cd08190 304 P------HGLSVALTAP--AVFRftapacPERHLEAAELlgadtsgasdrdagevladalIKLMRDIGIPNGLSALGY 373
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-104 |
2.47e-08 |
|
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: 55.17 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 12 IQGEHALRNISDIATRHQFKKIGIIYDPAI-EGPILDKVTISLNQSNLDFISYKF----PgecTYETIERLSHIMEQHDI 86
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGIKRVLIVTDKGLvKLGLLDPLLDALKKAGIEYVVFDGvvpdP---TIDNVEEGLALYKENGC 85
|
90
....*....|....*...
gi 262259464 87 DSIIALGGGKAIDTTKGI 104
Cdd:cd08189 86 DAIIAIGGGSVIDCAKVI 103
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
40-292 |
2.68e-08 |
|
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: 54.82 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 40 AIEGPILDKVTISLNQSNLDFISYKFPGECTYETIERLSHIMEQHDIDSIIALGGGKAIDTTKGIS-------------- 105
Cdd:cd08183 33 SLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCDVVIAIGGGSVIDAAKAIAalltnegsvldyle 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 106 -----KKLN---IPIIICPTVASSDAPTSR--LIIVYDenhkvQGVEKTKRN----PDIVLVDLDTIVQAPARFFAA-GI 170
Cdd:cd08183 113 vvgkgRPLTeppLPFIAIPTTAGTGSEVTKnaVLSSPE-----HGVKVSLRSpsmlPDVALVDPELTLSLPPEVTAAsGL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 171 gDAISKMFEVNQCKNAhglNSFSTP-PLE------TALLLANNTYSNLITWGKMAYedvkqhhitpsvervvesTVLLSG 243
Cdd:cd08183 188 -DALTQLIEPYVSRKA---NPLTDAlAREglrlaaRSLRRAYEDGEDLEAREDMAL------------------ASLLGG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 262259464 244 LGFESGGLSLAHAL---IRGLTAIPelatnlHGelVAYGTVVQAVLE-NRKHI 292
Cdd:cd08183 246 LALANAGLGAVHGLagpLGGMFGAP------HG--AICAALLPPVLEaNLRAL 290
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
14-313 |
2.92e-08 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 54.71 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISD-IATRHQFKKIGIIYDPAIEGPILDKVTISLNQSNLDFISYKFP-GEC--TYETIERLSHIMEQHDIDS- 88
Cdd:COG0337 18 GRGLLDELGElLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPdGEAskTLETLERILDALLEAGLDRd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 89 --IIALGGGKAIDTT--------KGiskklnIPIIICPT-----VASSdaptsrliivydenhkVQGveKT------KRN 147
Cdd:COG0337 98 dlVVALGGGVVGDLAgfaaatylRG------VPFIQVPTtllaqVDSS----------------VGG--KTgvnhpgGKN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 148 -------PDIVLVDLDTIVQAPARFFAAGIGDAIsKmfevnqcknaHGL----NSFSTppLETAL--LLANNtysnlitw 214
Cdd:COG0337 154 ligafhqPRAVLIDLDFLKTLPERELRAGLAEVI-K----------YGLiadaEFFEW--LEENAdaLLARD-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 215 gkmayEDVKQHHITPSVE---RVVESTVllsglgFESG-------GLSLAHALirgltaipELATN---LHGELVAYGTV 281
Cdd:COG0337 213 -----PEALEEAIARSCEikaEVVAADE------RESGlrallnfGHTFGHAI--------EAATGyrlLHGEAVAIGMV 273
|
330 340 350
....*....|....*....|....*....|....*.
gi 262259464 282 VQAVLENRKHIF----IIELINFLKSVDLPTTIAEL 313
Cdd:COG0337 274 FAARLSARLGLLseedVERIRALLEALGLPTRLPAL 309
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
27-351 |
7.24e-08 |
|
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: 53.77 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 27 RHQFKKIGIIYDPAIEG-PILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQHDIDSIIALGGGKAIDTTKGI 104
Cdd:cd14862 21 QLSGKRALIVTDKVLVKlGLLKKVLKRLLQAGFEVEVFdEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 105 ----------------------SKKlniPIIIC-PTVA--SSDApTSRLIIVYDENHKVQGVEKTKRNPDIVLVDLDTIV 159
Cdd:cd14862 101 wvlyerpdldpedispldllglRKK---AKLIAiPTTSgtGSEA-TWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 160 QAPARfFAAGIG-DAIskmfevnqcknAHGLNSFSTppletalllannTYSNLITWGkMAYEDVKQhhITPSVERVV--- 235
Cdd:cd14862 177 GMPPK-LTAGTGlDAL-----------AHAVEAYLS------------TWSNDFSDA-LALKAIEL--IFKYLPRAYkdg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 236 ------ESTVL---LSGLGFESGGLSLAHALIRGLTAIPELAtnlHGELVayGTVVQAVLE----------NRKHIFIIE 296
Cdd:cd14862 230 ddlearEKMHNaatIAGLAFGNSQAGLAHALGHSLGAVFHVP---HGIAV--GLFLPYVIEfyakvtderyDLLKLLGIE 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 297 --------------LINFLKSVDLPTTIAELGYHQEISDSMLETIIMHTLqNDYSKNFEP-PLNKENLKQ 351
Cdd:cd14862 305 ardeeealkklveaIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAM-EDSCTITSPrPPSEEDLKK 373
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
14-179 |
1.44e-07 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 52.69 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDPA-IEGPILDKVTISLNQSNLDFISYKfpGECTYETIERLSHIME---QHDIDSI 89
Cdd:PRK10624 14 GRGAIGALTDEVKRRGFKKALIVTDKTlVKCGVVAKVTDVLDAAGLAYEIYD--GVKPNPTIEVVKEGVEvfkASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 90 IALGGGKAIDTTKGI--------------------SKKLNIPIIICPTVASSDAPTSRLIIVYDE--NHKVQGVEkTKRN 147
Cdd:PRK10624 92 IAIGGGSPQDTCKAIgiisnnpefadvrslegvapTKKPSVPIIAIPTTAGTAAEVTINYVITDEekRRKFVCVD-PHDI 170
|
170 180 190
....*....|....*....|....*....|..
gi 262259464 148 PDIVLVDLDTIVQAPARFFAAGIGDAISKMFE 179
Cdd:PRK10624 171 PQVAFVDADMMDSMPPGLKAATGVDALTHAIE 202
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
7-315 |
6.44e-07 |
|
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: 50.59 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 7 FPGEYIQGEHALRNISDIATRHQFKKIGIIYDPAI-EGPILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQH 84
Cdd:cd14861 2 YPTRIRFGAGAIAELPEELKALGIRRPLLVTDPGLaALGIVDRVLEALGAAGLSPAVFsDVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 85 DIDSIIALGGGKAIDTTKGISKKLN----------------------IPIIICPTVASSDAPTSR-LIIVYDENHKVQGV 141
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMAThpgplwdyedgeggpaaitpavPPLIAIPTTAGTGSEVGRaAVITDDDTGRKKII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 142 EKTKRNPDIVLVDLDTIVQAPARFFAA-GIgDAISkmfevnqcknaHGLNSFSTP---PLETAlllanntysnlitwgkM 217
Cdd:cd14861 162 FSPKLLPKVAICDPELTLGLPPRLTAAtGM-DALT-----------HCIEAYLSPgfhPMADG----------------I 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 218 AYEDVkqHHITPSVERVVE------------STVLLSGLGFESgGLSLAHALIRGLTAIPELAtnlHGELVAygTVVQAV 285
Cdd:cd14861 214 ALEGL--RLISEWLPRAVAdgsdleargemmMAALMGAVAFQK-GLGAVHALAHALGALYGLH---HGLLNA--ILLPYV 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 262259464 286 LE-NRKHI--------------------FIIELINFLKSVDLPTTIAELGY 315
Cdd:cd14861 286 LRfNRPAVedklarlaralglglggfddFIAWVEDLNERLGLPATLSELGV 336
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-353 |
6.11e-06 |
|
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: 47.61 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIATRHQFKKIGIIYDPAIE------------GPILDKVTISLNQSNldfisykfPgecTYETIE 75
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVresgaadildalGGRIPVVVFSDFSPN--------P---DLEDLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 76 RLSHIMEQHDIDSIIALGGGKAIDTTKGIS-------KKLN-------------IPIIICPTVASSDAPTSRLIIVYDEN 135
Cdd:cd08182 70 RGIELFRESGPDVIIAVGGGSVIDTAKAIAallgspgENLLllrtgekapeenaLPLIAIPTTAGTGSEVTPFATIWDEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 136 HKVqgvektKRN-------PDIVLVDLDTIVQAPARFFAAGIGDAISkmfevnqcknaHGLNSF----STPpletalllA 204
Cdd:cd08182 150 EGK------KYSlahpslyPDAAILDPELTLSLPLYLTASTGLDALS-----------HAIESIwsvnANP--------E 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 205 NNTYS----NLITwgkMAYEDVKQHHITPSV-ERVVESTvLLSGLGFESGGLSLAHALIRGLTA---------------- 263
Cdd:cd08182 205 SRAYAlraiRLIL---ENLPLLLENLPNLEArEAMAEAS-LLAGLAISITKTTAAHAISYPLTSrygvphghacaltlpa 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 264 -IPELATNLHG--ELVAYGTVVQAVLENRKHIFIIELINFLKSVDLPTTIAELGyhqeISDSMLETIIMHTLQNDYSKNF 340
Cdd:cd08182 281 vLRYNAGADDEcdDDPRGREILLALGASDPAEAAERLRALLESLGLPTRLSEYG----VTAEDLEALAASVNTPERLKNN 356
|
410
....*....|...
gi 262259464 341 EPPLNKENLKQAI 353
Cdd:cd08182 357 PVRLSEEDLLRLL 369
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
14-95 |
1.63e-05 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; 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, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 46.28 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDPAIEGPILDKVTISLNQSNLDFISYKFP-GEC--TYETIERLSHIMEQHDID--- 87
Cdd:cd08195 7 GSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPaGEKskSLETVERIYDFLLEAGLDrds 86
|
....*...
gi 262259464 88 SIIALGGG 95
Cdd:cd08195 87 LLIALGGG 94
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
71-257 |
2.67e-05 |
|
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: 45.68 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 71 YETIERLSHIMEQHDIDSIIALGGGKAIDTTKGI------------------------SKKLN---IPIIICPTVAS--- 120
Cdd:cd14866 69 LETVEAAAEALREADADAVVAVGGGSAIVTARAAsillaedrdvrelctrraedglmvSPRLDapkLPIFVVPTTPTtad 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 121 -------SDAPTSRLIIVYDenhkvqgvEKTKrnPDIVLVDLDTIVQAPARFFAAGIGDAISKMFEvnqcknahGLNSFS 193
Cdd:cd14866 149 vkagsavTDPPAGQRLALFD--------PKTR--PAAVFYDPELLATAPASLVAGAAMNGFDMAVE--------GLYSRH 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262259464 194 TPPLETALLL--ANNTYSNLITWGKMAYEDVKqhhitpsvERVVEStVLLSGLGFESGGLSLAHAL 257
Cdd:cd14866 211 ADPLADATLMhaLRLLADGLPRLADDDDPAAR--------ADLVLA-AVLAGYGTDHTGGGVIHAL 267
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
44-332 |
8.17e-05 |
|
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: 44.03 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 44 PILDKVTISLNQSNLDFIsykfpgecTYETIER---LSHIME------QHDIDSIIALGGGKAIDTTKGIS--------- 105
Cdd:cd08185 41 GLLDRVKKLLEKAGVEVV--------VFDKVEPnplTTTVMEgaalakEEGCDFVIGLGGGSSMDAAKAIAfmatnpgdi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 106 -------------KKLNIPIIICPTVASSDAPTSRLIIVYDENHKvqgvEKTK-RNPDIV----LVDLDTIVQAPARFFA 167
Cdd:cd08185 113 wdyifggtgkgppPEKALPIIAIPTTAGTGSEVDPWAVITNPETK----EKKGiGHPALFpkvsIVDPELMLTVPPRVTA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 168 A-GIgDAISKMFE--VNqcKNAhglNSFSTPPLETALLL-------ANNTYSNLITWGKMAYEDvkqhhitpsvervves 237
Cdd:cd08185 189 YtGF-DALFHAFEsyIS--KNA---NPFSDMLALEAIRLvakylprAVKDGSDLEAREKMAWAS---------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 238 tvLLSGLGFESGGLSLAHAL---IRGLTaiPELAtnlHGE-LVA----------------YGTVVQAVL-----ENRKHI 292
Cdd:cd08185 247 --TLAGIVIANSGTTLPHGLehpLSGYH--PNIP---HGAgLAAlypayfeftiekapekFAFVARAEAsglsdAKAAED 319
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 262259464 293 FIIELINFLKSVDLPTTIAELGyhqeISDSMLETIIMHTL 332
Cdd:cd08185 320 FIEALRKLLKDIGLDDLLSDLG----VTEEDIPWLAENAM 355
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
8-104 |
1.62e-04 |
|
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: 43.33 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 8 PGEYIQGEHALRNISDIatrhQFKKIGIIYDPAI--EGPILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQH 84
Cdd:cd08179 5 PRDIYFGEGALEYLKTL----KGKRAFIVTGGGSmkRNGFLDKVEDYLKEAGMEVKVFeGVEPDPSVETVEKGAEAMREF 80
|
90 100
....*....|....*....|
gi 262259464 85 DIDSIIALGGGKAIDTTKGI 104
Cdd:cd08179 81 EPDWIIAIGGGSVIDAAKAM 100
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
14-105 |
1.99e-04 |
|
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: 43.02 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 14 GEHALRNISDIATRHQFKKIGIIYDP--AIEGPILDKVTISLNQSNLDFISY-KFPGECTYETIERLSHIMEQHDIDSII 90
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGRssYKKSGAWDDVEKALEENGIEYVVYdKVTPNPTVDQADEAAKLARDFGADAVI 86
|
90
....*....|....*
gi 262259464 91 ALGGGKAIDTTKGIS 105
Cdd:cd08186 87 AIGGGSPIDTAKSVA 101
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
30-104 |
4.92e-04 |
|
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: 41.79 E-value: 4.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262259464 30 FKKIGIIYDPAIE--GpILDKVTISLNQSNLDF-ISYKFPGECTYETIERLSHIMEQHDIDSIIALGGGKAIDTTKGI 104
Cdd:cd08178 23 VKRAFIVTDRVLYklG-YVDKVLDVLEARGVETeVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIM 99
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
70-179 |
7.33e-04 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 41.09 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 70 TYETIERLSHIMEQHDIDSIIALGGGKAIDTTKGI------------------SKKLNIPIIICPTVASSDAPTSRLIIV 131
Cdd:PRK09860 73 TTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIalvaanggdirdyegvdrSAKPQLPMIAINTTAGTASEMTRFCII 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 262259464 132 YDENHKVQGVEKTKR-NPDIVLVDLDTIVQAPARFFAAGIGDAISKMFE 179
Cdd:PRK09860 153 TDEARHIKMAIVDKHvTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIE 201
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
72-164 |
1.81e-03 |
|
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: 39.80 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262259464 72 ETIERLSHIMEQHDIDSIIALGGGKAIDTTKGISKKLNIPIIICPTV-ASSDApTSRLIIvydenhKVQGVEKTKRNPDI 150
Cdd:cd08177 63 EVAERALAAAREAGADGLVAIGGGSAIGLAKAIALRTGLPIVAVPTTyAGSEM-TPIWGE------TEDGVKTTGRDPRV 135
|
90
....*....|....*...
gi 262259464 151 ----VLVDLDTIVQAPAR 164
Cdd:cd08177 136 lprtVIYDPDLTLGLPAA 153
|
|
| |
