|
Name |
Accession |
Description |
Interval |
E-value |
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
11-360 |
1.23e-161 |
|
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: 456.21 E-value: 1.23e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 11 PQFYRYHEGALASVPSLFKEYHAQRILVVHGTVSFEKAQPFLPFLADSEYQFFyhTYTGECSYFGAEQISQQIKEHQIDF 90
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFGIKRPLIIHGEKSWQAAKPYLPKLFEIEYPVL--RYDGECSYEEIDRLAEEAKEHQADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 91 LLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGKTeHFFRQAAFLITDPKLLLDAPRDYFV 170
Cdd:cd08172 79 IIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYD-YFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 171 AGLADTLAKWYESETILRQAhLQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLSEIVFAVSGLVGGFG 250
Cdd:cd08172 158 AGIGDTLAKWYEADAILRQL-EELPAFLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMVGGFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 251 DKYARNAAAHAMHDAMSKFlPKSHDYLHGEKVAYGIFYQLALEKRWAIIDALIPFYQELNLPMSLRQMGLYPEEEAVLDA 330
Cdd:cd08172 237 DEYGRSAGAHAIHNGLTKL-PETHHFLHGEKVAYGILVQLALEGKWDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQK 315
|
330 340 350
....*....|....*....|....*....|.
gi 1517577253 331 MVQFIDSKEKV-HLIPIEISQERLRQGIEEL 360
Cdd:cd08172 316 IAAFAASPEESiHLLPPDVTAEEVLQAIEKL 346
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
6-360 |
3.27e-105 |
|
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: 313.26 E-value: 3.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 6 KVKVGPQFYRYHEGALASVPSLFKEYHaQRILVVHGTVSFEKAQPFL-PFLADSEYQFFYHTYTGECSYFGAEQISQQIK 84
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLG-KRALIITGPTALKAAGDRLeESLEDAGIEVEVEVFGGECSEEEIERLAEEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 85 EHQIDFLLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGkTEHFFRQAAFLITDPKLLLDA 164
Cdd:COG0371 80 EQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDG-YSFLAKNPDLVLVDTDIIAKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 165 PRDYFVAGLADTLAKWYESETILRQ-AHLQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLSEIVFAVS 243
Cdd:COG0371 159 PVRLLAAGIGDALAKWYEARDWSLAhRDLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 244 GLVGGFGDKYAR--------NAAAHamhdamskfLPKSHDYLHGEKVAYGIFYQLALEKRWAIIDALIPFYQELNLPMSL 315
Cdd:COG0371 239 GLAMGIGSSRPGsgaahaihNGLTA---------LPETHHALHGEKVAFGTLVQLVLEGRPEEIEELLDFLRSVGLPTTL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1517577253 316 RQMGLYPEEEAVLDAMVQFI-DSKEKVHLIPIEISQERLRQGIEEL 360
Cdd:COG0371 310 ADLGLDDETEEELLTVAEAArPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
3-361 |
8.46e-57 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 189.17 E-value: 8.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 3 TDLKVKVGPQFYRYHEGALASVPSLFKEYHAQRILVVHGTVSFEKAQPFLP--FLADSEYQFfyhTYTGECSYFGAEQIS 80
Cdd:PRK10586 4 NPIRVVVGPANYFSHPGSIDHLHDFFTDEQLSRAVWIYGERAIAAAQPYLPpaFELPGAKHI---LFRGHCSESDVAQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 81 QQIKEHQiDFLLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEgkteHF--FRQAAFLI-TD 157
Cdd:PRK10586 81 AASGDDR-QVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQAL----HFeiFDDANFLVlVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 158 PKLLLDAPRDYFVAGLADTLAKWYESETILRQAHLQgePF-LQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLS 236
Cdd:PRK10586 156 PRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETL--PLtVRLGINNALAIRDVLLNSSEQALADQQNGQLTQDFCDVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 237 EIVFAVSGLVGGFGDKYARNAAAHAMHDAMSkFLPKSHDYLHGEKVAYGIFYQLALEKRWAIIDALIPFYQELNLPMSLR 316
Cdd:PRK10586 234 DAIIAGGGMVGGLGERYTRVAAAHAVHNGLT-VLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLIGAYQRFHLPTTLA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1517577253 317 QMGLYPEEEAVLDAMV-QFIDSKEKVHLIPIEISQERLRQGIEELE 361
Cdd:PRK10586 313 ELDVDINNQAEIDRVIaHTLRPVESIHYLPVTLTPDTLRAAFEKVE 358
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
11-353 |
2.48e-39 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 143.13 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 11 PQFYRYHEGALASVPSLFKEYHAqRILVVHGTVS-----FEKAQPFLPfLADSEYQFFyHTYTGECSYFGAEQISQQIKE 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGA-RALIVTDPGSlksglLDKVLASLE-EAGIEVVVF-DGVEPEPTLEEVDEAAALARE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 86 HQIDFLLGVGGGKLADLVGYSAHLNN------------------LNFGLVPTLASNCAPWTPLAVMYQENGAAEGKTEHF 147
Cdd:pfam00465 78 AGADVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 148 FRQAAFLITDPKLLLDAPRDYFVAGLADTLAKWYESETILRQAHLQGepflQLAGATAKLSQEAIMR-----DSKAALAA 222
Cdd:pfam00465 158 KLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTD----ALALEAIRLIAENLPRavadgEDLEAREN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 223 MDEGkltpefVHLSEIVFAVSGLVGGFGDKYArnaaahamhdaMSKFLPKSHDYLHGEKVAYGI----------FYQLAL 292
Cdd:pfam00465 234 MLLA------STLAGLAFSNAGLGAAHALAHA-----------LGGRYGIPHGLANAILLPYVLrfnapaapekLAQLAR 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1517577253 293 --------EKRWAIIDALIPFYQELNLPMSLRQMGLyPEEEavLDAMVQFIDSKEKVHLIPIEISQERL 353
Cdd:pfam00465 297 algedsdeEAAEEAIEALRELLRELGLPTTLSELGV-TEED--LDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
11-360 |
1.23e-161 |
|
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: 456.21 E-value: 1.23e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 11 PQFYRYHEGALASVPSLFKEYHAQRILVVHGTVSFEKAQPFLPFLADSEYQFFyhTYTGECSYFGAEQISQQIKEHQIDF 90
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFGIKRPLIIHGEKSWQAAKPYLPKLFEIEYPVL--RYDGECSYEEIDRLAEEAKEHQADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 91 LLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGKTeHFFRQAAFLITDPKLLLDAPRDYFV 170
Cdd:cd08172 79 IIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYD-YFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 171 AGLADTLAKWYESETILRQAhLQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLSEIVFAVSGLVGGFG 250
Cdd:cd08172 158 AGIGDTLAKWYEADAILRQL-EELPAFLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMVGGFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 251 DKYARNAAAHAMHDAMSKFlPKSHDYLHGEKVAYGIFYQLALEKRWAIIDALIPFYQELNLPMSLRQMGLYPEEEAVLDA 330
Cdd:cd08172 237 DEYGRSAGAHAIHNGLTKL-PETHHFLHGEKVAYGILVQLALEGKWDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQK 315
|
330 340 350
....*....|....*....|....*....|.
gi 1517577253 331 MVQFIDSKEKV-HLIPIEISQERLRQGIEEL 360
Cdd:cd08172 316 IAAFAASPEESiHLLPPDVTAEEVLQAIEKL 346
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
6-360 |
3.27e-105 |
|
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: 313.26 E-value: 3.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 6 KVKVGPQFYRYHEGALASVPSLFKEYHaQRILVVHGTVSFEKAQPFL-PFLADSEYQFFYHTYTGECSYFGAEQISQQIK 84
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLG-KRALIITGPTALKAAGDRLeESLEDAGIEVEVEVFGGECSEEEIERLAEEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 85 EHQIDFLLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGkTEHFFRQAAFLITDPKLLLDA 164
Cdd:COG0371 80 EQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDG-YSFLAKNPDLVLVDTDIIAKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 165 PRDYFVAGLADTLAKWYESETILRQ-AHLQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLSEIVFAVS 243
Cdd:COG0371 159 PVRLLAAGIGDALAKWYEARDWSLAhRDLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 244 GLVGGFGDKYAR--------NAAAHamhdamskfLPKSHDYLHGEKVAYGIFYQLALEKRWAIIDALIPFYQELNLPMSL 315
Cdd:COG0371 239 GLAMGIGSSRPGsgaahaihNGLTA---------LPETHHALHGEKVAFGTLVQLVLEGRPEEIEELLDFLRSVGLPTTL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1517577253 316 RQMGLYPEEEAVLDAMVQFI-DSKEKVHLIPIEISQERLRQGIEEL 360
Cdd:COG0371 310 ADLGLDDETEEELLTVAEAArPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
11-360 |
2.73e-83 |
|
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: 257.08 E-value: 2.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 11 PQFYRYHEGALASVPSLFKEYhAQRILVVHGTVSFEKA-QPFLPFLADSEYQFFYHTYTGECSYFGAEQISQQIKEHQID 89
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPL-GKKALIIGGKTALEAVgEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 90 FLLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGktEHFFRQAAFL-ITDPKLLLDAPRDY 168
Cdd:cd08550 80 VIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLG--YSLLKRSPDLvLVDTDIIAAAPVRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 169 FVAGLADTLAKWYESETILRqaHLQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLSEIVFAVSGLVGG 248
Cdd:cd08550 158 LAAGIGDTLAKWYEARPSSR--GGPDDLALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 249 FGDKYARNAAAHAMHDAMSKfLPKSHDYLHGEKVAYGIFYQLALEKR-WAIIDALIPFYQELNLPMSLRQMGLYPEEEAV 327
Cdd:cd08550 236 LGGGGCRTAAAHAIHNGLTK-LPETHGTLHGEKVAFGLLVQLALEGRsEEEIEELIEFLRRLGLPVTLEDLGLELTEEEL 314
|
330 340 350
....*....|....*....|....*....|...
gi 1517577253 328 LDAMVQFIDSKEKVHLIPIEISQERLRQGIEEL 360
Cdd:cd08550 315 RKIAEYACDPPDMAHMLPFPVTPEMLAEAILAA 347
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
3-361 |
8.46e-57 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 189.17 E-value: 8.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 3 TDLKVKVGPQFYRYHEGALASVPSLFKEYHAQRILVVHGTVSFEKAQPFLP--FLADSEYQFfyhTYTGECSYFGAEQIS 80
Cdd:PRK10586 4 NPIRVVVGPANYFSHPGSIDHLHDFFTDEQLSRAVWIYGERAIAAAQPYLPpaFELPGAKHI---LFRGHCSESDVAQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 81 QQIKEHQiDFLLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEgkteHF--FRQAAFLI-TD 157
Cdd:PRK10586 81 AASGDDR-QVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQAL----HFeiFDDANFLVlVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 158 PKLLLDAPRDYFVAGLADTLAKWYESETILRQAHLQgePF-LQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLS 236
Cdd:PRK10586 156 PRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETL--PLtVRLGINNALAIRDVLLNSSEQALADQQNGQLTQDFCDVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 237 EIVFAVSGLVGGFGDKYARNAAAHAMHDAMSkFLPKSHDYLHGEKVAYGIFYQLALEKRWAIIDALIPFYQELNLPMSLR 316
Cdd:PRK10586 234 DAIIAGGGMVGGLGERYTRVAAAHAVHNGLT-VLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLIGAYQRFHLPTTLA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1517577253 317 QMGLYPEEEAVLDAMV-QFIDSKEKVHLIPIEISQERLRQGIEELE 361
Cdd:PRK10586 313 ELDVDINNQAEIDRVIaHTLRPVESIHYLPVTLTPDTLRAAFEKVE 358
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
18-360 |
1.30e-55 |
|
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: 185.42 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 18 EGALASVPSLFKEYHaQRILVVHGTVSFEKAQP-FLPFLADSEYQFF-YHTYTGECSYFGAEQISQQIKEHQIDFLLGVG 95
Cdd:cd08171 8 EDAYDAIPKICSPYG-KKVVVIGGKKALAAAKPkLRAALEGSGLEITdFIWYGGEATYENVEKLKANPEVQEADMIFAVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 96 GGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGkTEHFFRQAAFLITDPKLLLDAPRDYFVAGLAD 175
Cdd:cd08171 87 GGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKE-YYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 176 TLAKWYESETILRQAHLqgEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFvhlSEIVFAV---SGLVGGF-GD 251
Cdd:cd08171 166 TLAKYYEVEFSARGDEL--DHTNALGVAISKMCSEPLLKYGVQALEDCRANKVSDAL---EQVVLDIivtTGLVSNLvEP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 252 KYarNAAAHAMHDAMSKFLPK-SHDYLHGEKVAYGIFYQLALEKRWAIIDALIPFYQELNLPMSLRQMGLYPEE-EAVLD 329
Cdd:cd08171 241 DY--NSSLAHALYYGLTTLPQiEEEHLHGEVVSYGVLVLLTVDGQFEELEKVYAFNKSIGLPTCLADLGLTVEDlEKVLD 318
|
330 340 350
....*....|....*....|....*....|.
gi 1517577253 330 AMVQFIDskekVHLIPIEISQERLRQGIEEL 360
Cdd:cd08171 319 KALKTKD----LRHSPYPITKEMFEEAIKDL 345
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
18-363 |
2.41e-48 |
|
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: 166.82 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 18 EGALASVPSLFKEYHAQRILVVHGTVSFEKAQPFLPFLADSEYQFFYHTYTGECSYFGAEQISQQIKEHQIDFLLGVGGG 97
Cdd:cd08170 8 PGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADVVIGIGGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 98 KLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGktEHFFRQA-AFLITDPKLLLDAPRDYFVAGLADT 176
Cdd:cd08170 88 KTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDE--YLFLPRNpDLVLVDTEIIAKAPVRFLVAGMGDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 177 LAKWYESETILRQAH--LQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTPEFVHLSEIVFAVSGLvgGF----- 249
Cdd:cd08170 166 LATYFEARACARSGApnMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGL--GFesggl 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 250 --------GdkyarnaaahamhdamskF--LPKSHDYLHGEKVAYGIFYQLALEKR-WAIIDALIPFYQELNLPMSLRQM 318
Cdd:cd08170 244 aaahaihnG------------------LtaLPETHHLLHGEKVAFGTLVQLVLEGRpDEEIEEVIRFCRSVGLPVTLADL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1517577253 319 GLYPEEEAVLDAMVQF-IDSKEKVHLIPIEISQERLRQGIEELEKY 363
Cdd:cd08170 306 GLEDVTDEELRKVAEAaCAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
18-357 |
1.04e-42 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 152.28 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 18 EGALASVPSLFKEYhAQRILVVHGTVSFEKAQP-FLPFLADSEYQFFYHTYTGECSYFGAEQISQQIKEHQIDFLLGVGG 96
Cdd:PRK09423 15 KGALARLGEYLKPL-GKRALVIADEFVLGIVGDrVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIAEENGCDVVIGIGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 97 GKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAaegktehfFRQAAFLITDPKLLL-------DAPRDYF 169
Cdd:PRK09423 94 GKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGE--------FERYLFLPKNPDLVLvdtaiiaKAPARFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 170 VAGLADTLAKWYESETILRqAH---LQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEGKLTP--EFV-----HLSEIV 239
Cdd:PRK09423 166 AAGIGDALATWFEARACSR-SGgttMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPalENVieantLLSGLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 240 FAVSGLVG------GFgdkyarnaaahamhdamsKFLPKSHDYLHGEKVAYGIFYQLALEKR-WAIIDALIPFYQELNLP 312
Cdd:PRK09423 245 FESGGLAAahaihnGL------------------TALEDTHHLTHGEKVAFGTLTQLVLENRpKEEIEEVIDFCHAVGLP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1517577253 313 MSLRQMGLYPEEEAVLDAMVQF-IDSKEKVHLIPIEISQERLRQGI 357
Cdd:PRK09423 307 TTLADLGLKEDSDEELRKVAEAaCAEGETIHNMPFKVTPEDVAAAI 352
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
11-353 |
2.48e-39 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 143.13 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 11 PQFYRYHEGALASVPSLFKEYHAqRILVVHGTVS-----FEKAQPFLPfLADSEYQFFyHTYTGECSYFGAEQISQQIKE 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGA-RALIVTDPGSlksglLDKVLASLE-EAGIEVVVF-DGVEPEPTLEEVDEAAALARE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 86 HQIDFLLGVGGGKLADLVGYSAHLNN------------------LNFGLVPTLASNCAPWTPLAVMYQENGAAEGKTEHF 147
Cdd:pfam00465 78 AGADVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 148 FRQAAFLITDPKLLLDAPRDYFVAGLADTLAKWYESETILRQAHLQGepflQLAGATAKLSQEAIMR-----DSKAALAA 222
Cdd:pfam00465 158 KLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTD----ALALEAIRLIAENLPRavadgEDLEAREN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 223 MDEGkltpefVHLSEIVFAVSGLVGGFGDKYArnaaahamhdaMSKFLPKSHDYLHGEKVAYGI----------FYQLAL 292
Cdd:pfam00465 234 MLLA------STLAGLAFSNAGLGAAHALAHA-----------LGGRYGIPHGLANAILLPYVLrfnapaapekLAQLAR 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1517577253 293 --------EKRWAIIDALIPFYQELNLPMSLRQMGLyPEEEavLDAMVQFIDSKEKVHLIPIEISQERL 353
Cdd:pfam00465 297 algedsdeEAAEEAIEALRELLRELGLPTTLSELGV-TEED--LDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
18-226 |
1.06e-16 |
|
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: 80.29 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 18 EGALASVPSLFKEYH-AQRILVVHGTVSFEKAqpfLPFLADSEYQFFYHTYTGECSYF----GAEQISQQIKEHQIDFLL 92
Cdd:cd08173 9 HGAINKIGEVLKKLLlGKRALIITGPNTYKIA---GKRVEDLLESSGVEVVIVDIATIeeaaEVEKVKKLIKESKADFII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 93 GVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQENGAAEGKTehffRQAAFLITDPKLLLDAPRDYFVAG 172
Cdd:cd08173 86 GVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKA----KAPIAIIADTEIISKAPKRLLAAG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1517577253 173 LADTLAK------WyesetilRQAH-LQGEPFLQLAGATAKLSQEAIMRDSKAALAAMDEG 226
Cdd:cd08173 162 CGDLISNitavkdW-------RLAHrLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEG 215
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
15-180 |
2.08e-14 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 72.34 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 15 RYHEGALASVPSLFKEYHAQRILVVHGTVSFEKAQPFLP-FLADSEYQ-FFYHTYTGECSYFGAEQISQQIKEHQIDFLL 92
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVAeSLKRAGIEvETRLEVAGNADMETAEKLVGALRERDADAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 93 GVGGGKLADLVGYSAHLNNLNFGLVPTLASN---CAPWTPLAVmyqengaaEGKTEHFFRQAAF-LITDPKLLLDAPRDY 168
Cdd:pfam13685 81 GVGGGTVIDLAKYAAFKLGKPFISVPTAASNdgfASPGASLTV--------DGKKRSIPAAAPFgVIADTDVIAAAPRRL 152
|
170
....*....|..
gi 1517577253 169 FVAGLADTLAKW 180
Cdd:pfam13685 153 LASGVGDLLAKI 164
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
69-331 |
3.11e-13 |
|
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: 68.93 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 69 GECSYFGAEQISQQIKEHQIDFLLGVGGGKLADLVGYSAHLNN--LNFGLVPTLASNCAPWTPLAVMYQENGAAEGKTEH 146
Cdd:cd07766 59 ENPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKAVAALLNrgIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGPH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 147 FFRQAAFLitDPKLLLDAPRDYFVAGLADTLAKWYESETILRQAHLQGEPFLQLAGataklsqeaimrdskaalaamdeg 226
Cdd:cd07766 139 YNPDVVFV--DTDITKGLPPRQVASGGVDALAHAVELEKVVEAATLAGMGLFESPG------------------------ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 227 kltpefvhlseivfavSGLVGGFGDKyarnaaahamhdamskfLPKSHDYLHGEKVAYGIFYQLALEKR-----WAIIDA 301
Cdd:cd07766 193 ----------------LGLAHAIGHA-----------------LTAFEGIPHGEAVAVGLPYVLKVANDmnpepEAAIEA 239
|
250 260 270
....*....|....*....|....*....|.
gi 1517577253 302 LIPFYQELNLPMSLRQMGLYPEE-EAVLDAM 331
Cdd:cd07766 240 VFKFLEDLGLPTHLADLGVSKEDiPKLAEKA 270
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
6-217 |
4.96e-13 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 69.15 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 6 KVKVGPqfyryheGALASVPSLFKEYH-AQRILVVHGTVSFEKA-QPFLPFLADS-EYQFFYhtyTGECSYFGAEQISQQ 82
Cdd:PRK00843 13 DVVVGH-------GVLDDIGDVCSDLKlTGRALIVTGPTTKKIAgDRVEENLEDAgDVEVVI---VDEATMEEVEKVEEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 83 IKEHQIDFLLGVGGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYqengaaEGKTEHFFRQAAFL--ITDPKL 160
Cdd:PRK00843 83 AKDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIK------GGGKPVSVKAKPPLavIADTEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1517577253 161 LLDAPRDYFVAGLADTLAK------WyesetilRQAH-LQGEPFLQLAGATAKLSQEAIMRDSK 217
Cdd:PRK00843 157 IAKAPYRLLAAGCGDIISNytavkdW-------RLAHrLRGEYYSEYAAALSLMTAKMLIENAD 213
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
11-179 |
1.18e-09 |
|
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: 59.07 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 11 PQFYRYHEGALASVPSLFKEYHA--QRILVVHGTVSFEK-AQPFLPFLADSEYQFFYHtytgECSYFGAEQISQQI-KEH 86
Cdd:cd08174 1 PLILKIEEGALEHLGKYLADRNQgfGKVAIVTGEGIDELlGEDILESLEEAGEIVTVE----ENTDNSAEELAEKAfSLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 87 QIDFLLGVGGGKLADLVGYSAHLNNLNFGLVPTLASN---CapwTPLAVMYqengaAEGKTEHFFRQAAF-LITDPKLLL 162
Cdd:cd08174 77 KVDAIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNdgiA---SPVAVLK-----VDGKRKSLGAKMPYgVIVDLDVIK 148
|
170
....*....|....*..
gi 1517577253 163 DAPRDYFVAGLADTLAK 179
Cdd:cd08174 149 SAPRRLILAGIGDLISN 165
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
19-330 |
2.07e-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: 58.35 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 19 GALASVPSLFKEYHAQRILVVHGTVSFEKAQpflpfladseyQFFYHTYTGECSYFGAEQISQQIKEHQI----DFLLGV 94
Cdd:cd08549 9 GAINKIEEILKKLNLKRVLIITGKNTKAKYC-----------RFFYDQLKTVCDIVYYDNIDNLEDELKKytfyDCVIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 95 GGGKLADLVGYSAHLNNLNFGLVPTLASNCAPWTPLAVMYQengaaEGKTEHFFRQAAF-LITDPKLLLDAPRDYFVAGL 173
Cdd:cd08549 78 GGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRI-----PGVKKTFMADAPIaIIADTEIIKKSPRRLLSAGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 174 ADTLAKWyeseTILRQ---AH-LQGEPFLQLAGATAKLS-QEAIMRDSKAALAAMDEGKLTPEFVHlSEIVFAVSglvgg 248
Cdd:cd08549 153 GDLVSNI----TAVLDwklAHkEKGEKYSEFAAILSKTSaKELVSYVLKASDLEEYHRVLVKALVG-SGIAMAIA----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 249 fGDKYARNAAAHAMHDAMSKFLPKSHD--YLHGEKVAYGIFYQLALEKRWAIIDALIP-----FYQELNLPMSLRQMGLY 321
Cdd:cd08549 223 -GSSRPASGSEHLFSHALDKLKEEYLNinVLHGEQVGVGTIIMSYLHEKENKKLSGLHerikmILKKVGAPTTAKQLGID 301
|
330
....*....|.
gi 1517577253 322 PE--EEAVLDA 330
Cdd:cd08549 302 EDliIEALTEA 312
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
18-225 |
1.73e-07 |
|
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: 52.51 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 18 EGALASVPSLFKEYHA-QRILVVHGTVSFEKA-QPFLPFLADSEYQFFYHTYTGECSYFGAEQISQQIKEH---QIDFLL 92
Cdd:cd08175 8 EGALKKLPEYLKELFGgKKVLVVADENTYAAAgEEVEAALEEAGVTVCLLIFPGEGDLIADEAAVGKVLLElekDTDLII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 93 GVGGGKLADLVGYSAHLNNLNFGLVPTLASncapwtplavM--YQENGAA---EGKTEHFFRQAA-FLITDPKLLLDAPR 166
Cdd:cd08175 88 AVGSGTINDLTKYAAYKLGIPYISVPTAPS----------MdgYTSSGAPiivDGVKKTFPAHAPkAIFADLDVLANAPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1517577253 167 DYFVAGLADTLAK------WYESEtilrqaHLQGEPFLQLAgatAKLSQEAI--MRDSKAALAAMDE 225
Cdd:cd08175 158 RMIAAGFGDLLGKytaladWKLSH------LLGGEYYCPEV---ADLVQEALekCLDNAEGIAARDP 215
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
5-174 |
5.95e-04 |
|
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: 41.23 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 5 LKVKVGPQFYRYH--EGALASVPSLFKE-YHAQRILVVH-GTVSFEKAQPFLPFLADSEYQFFYHTYT-GEC--SYFGAE 77
Cdd:COG0337 4 LTVNLGERSYDIRigRGLLDELGELLAElLKGRRVLVVTdENVAPLYGERLRAALEAAGFEVHLLVLPdGEAskTLETLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517577253 78 QISQQIKEHQI---DFLLGVGGGKLADLVGYSAH--LNNLNFGLVPT--LA---SncapwtplAVmyqenGaaeGKT--E 145
Cdd:COG0337 84 RILDALLEAGLdrdDLVVALGGGVVGDLAGFAAAtyLRGVPFIQVPTtlLAqvdS--------SV-----G---GKTgvN 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1517577253 146 HF--------FRQAAFLITDPKLLLDAPRDYFVAGLA 174
Cdd:COG0337 148 HPggknligaFHQPRAVLIDLDFLKTLPERELRAGLA 184
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
18-97 |
8.66e-04 |
|
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: 40.89 E-value: 8.66e-04
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gi 1517577253 18 EGALASVPSLFKEYHAQRILVV--HGTVSFEKAQPFLPFLADSEYQffYHTYTG---ECSYFGAEQISQQIKEHQIDFLL 92
Cdd:cd08551 8 AGALARLGEELKALGGKKVLLVtdPGLVKAGLLDKVLESLKAAGIE--VEVFDDvepNPTVETVEAAAELAREEGADLVI 85
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....*
gi 1517577253 93 GVGGG 97
Cdd:cd08551 86 AVGGG 90
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