|
Name |
Accession |
Description |
Interval |
E-value |
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
6-330 |
0e+00 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 550.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 6 ASMTVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNVAFLPDVPFPDSLHLESDLATALAASRNILIVVPS 85
Cdd:PRK00094 2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALADADLILVAVPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 86 HVFGDVLRQIKPLMRPDARIVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLASTDQAFSD 165
Cdd:PRK00094 82 QALREVLKQLKPLLPPDAPIVWATKGIEPGTGKLLSEVLEEELPDLAPIAVLSGPSFAKEVARGLPTAVVIASTDEELAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 166 DLQQLLHCGkSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGEALGADPATFMGMAG 245
Cdd:PRK00094 162 RVQELFHSP-YFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEITRLGVALGANPETFLGLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 246 LGDLVLTCTDNQSRNRRFGMMLGQGSDVKGAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAAL 325
Cdd:PRK00094 241 LGDLVLTCTSPLSRNRRFGLALGQGKSLEEALAEIGMVAEGVRTAKAVYELAKKLGVEMPITEAVYAVLYEGKDPREAVE 320
|
....*
gi 2094593882 326 TLLGR 330
Cdd:PRK00094 321 DLMGR 325
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
6-333 |
0e+00 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 525.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 6 ASMTVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNVAFLPDVPFPDSLHLESDLATALAASRNILIVVPS 85
Cdd:COG0240 1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAGADLVLLAVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 86 HVFGDVLRQIKPLMRPDARIVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLASTDQAFSD 165
Cdd:COG0240 81 QALREVLEQLAPLLPPGAPVVSATKGIEPGTGLLMSEVIAEELPGALRIAVLSGPSFAEEVARGLPTAVVVASEDEEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 166 DLQQLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGEALGADPATFMGMAG 245
Cdd:COG0240 161 RLQELLST-PYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEMTRLGVALGARPETFMGLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 246 LGDLVLTCTDNQSRNRRFGMMLGQGSDVKGAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAAL 325
Cdd:COG0240 240 LGDLVLTCTSDLSRNRRFGLALGKGKSLEEALAEMGMVAEGVYTAKAVYELAEKLGVEMPITEAVYAVLYEGKSPREAVE 319
|
....*...
gi 2094593882 326 TLLGRARK 333
Cdd:COG0240 320 ALMARPLK 327
|
|
| PRK14618 |
PRK14618 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
10-335 |
7.47e-83 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237770 [Multi-domain] Cd Length: 328 Bit Score: 254.41 E-value: 7.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 10 VIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNVAFLPDVPFPDSLHLESDLATALAASRNILIVVPSHVFG 89
Cdd:PRK14618 9 VLGAGAWGTALAVLAASKGVPVRLWARRPEFAAALAAERENREYLPGVALPAELYPTADPEEALAGADFAVVAVPSKALR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 90 DVLRQIKPlmrpDARIVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLASTDQAFSDDLQQ 169
Cdd:PRK14618 89 ETLAGLPR----ALGYVSCAKGLAPDGGRLSELARVLEFLTQARVAVLSGPNHAEEIARFLPAATVVASPEPGLARRVQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 170 LLhCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGEALGADPATFMGMAGLGDL 249
Cdd:PRK14618 165 AF-SGPSFRVYTSRDRVGVELGGALKNVIALAAGMVDGLKLGDNAKAALITRGLREMVRFGVALGAEEATFYGLSGLGDL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 250 VLTCTDNQSRNRRFGMMLGQGSDVKGAQEKiGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAALTLLG 329
Cdd:PRK14618 244 IATATSPHSRNRAAGEAIVRGVDREHLEAG-GKVVEGLYTVKALDAWAKAHGHDLPIVEAVARVARGGWDPLAGLRSLMG 322
|
....*.
gi 2094593882 330 RARKDE 335
Cdd:PRK14618 323 REAKEE 328
|
|
| PRK14619 |
PRK14619 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
7-335 |
3.02e-82 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237771 [Multi-domain] Cd Length: 308 Bit Score: 251.83 E-value: 3.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 7 SMTVIGAGSYGTALAITLARNGHEVVLWghdpkhiatlqrdrcnvaflpdvpfpdSLHLESDLATALAASRNILIVVPSH 86
Cdd:PRK14619 6 TIAILGAGAWGSTLAGLASANGHRVRVW---------------------------SRRSGLSLAAVLADADVIVSAVSMK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 87 VFGDVLRQIKPL-MRPDARIVWATKGLEAETGRLLQDVAREALGDEiPLAVISGPTFAKELAAGLPTAISLASTDQAFSD 165
Cdd:PRK14619 59 GVRPVAEQVQALnLPPETIIVTATKGLDPETTRTPSQIWQAAFPNH-PVVVLSGPNLSKEIQQGLPAATVVASRDLAAAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 166 DLQQLLhCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGEALGADPATFMGMAG 245
Cdd:PRK14619 138 TVQQIF-SSERFRVYTNSDPLGTELGGTLKNVIAIAAGVCDGLQLGTNAKAALVTRALPEMIRVGTHLGAQTETFYGLSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 246 LGDLVLTCTDNQSRNRRFGMMLGQGSDVKGAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLyCGKNAREAAL 325
Cdd:PRK14619 217 LGDLLATCTSPLSRNYQVGYGLAQGKSLEQILAELEGTAEGVNTANVLVQLAQQQNIAVPITEQVYRLL-QGEITPQQAL 295
|
330
....*....|.
gi 2094593882 326 T-LLGRARKDE 335
Cdd:PRK14619 296 EeLMERDLKPE 306
|
|
| PRK12439 |
PRK12439 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
10-335 |
4.20e-82 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 171500 [Multi-domain] Cd Length: 341 Bit Score: 252.78 E-value: 4.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 10 VIGAGSYGTALAITLARNGhEVVLWGHDPKHIATLQRDRCNVAFLP-DVPFPDSLHLESDLATALAASRNILIVVPSHVF 88
Cdd:PRK12439 12 VLGGGSWGTTVASICARRG-PTLQWVRSAETADDINDNHRNSRYLGnDVVLSDTLRATTDFAEAANCADVVVMGVPSHGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 89 GDVLRQIKPLMRPDARIVWATKGLEAETGRLLQDVAREALGDEiPLAVISGPTFAKELAAGLPTAISLASTDQAFSDDLQ 168
Cdd:PRK12439 91 RGVLTELAKELRPWVPVVSLVKGLEQGTNMRMSQIIEEVLPGH-PAGILAGPNIAREVAEGYAAAAVLAMPDQHLATRLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 169 QLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGEALGADPATFMGMAGLGD 248
Cdd:PRK12439 170 PLFRT-RRFRVYTTDDVVGVEMAGALKNVFAIAVGMGYSLGIGENTRAMVIARALREMTKLGVAMGGNPETFAGLAGMGD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 249 LVLTCTDNQSRNRRFGMMLGQGSDVKGAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAALTLL 328
Cdd:PRK12439 249 LIVTCTSQRSRNRHVGEQLGAGKPIDEIIASMNQVAEGVKAASVVMEFADEYGLNMPIAREVDAVINHGSTVEQAYRGLI 328
|
....*..
gi 2094593882 329 GRARKDE 335
Cdd:PRK12439 329 AEVPGHE 335
|
|
| NAD_Gly3P_dh_C |
pfam07479 |
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent ... |
184-323 |
2.50e-77 |
|
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the C-terminal substrate-binding domain.
Pssm-ID: 462178 [Multi-domain] Cd Length: 142 Bit Score: 233.43 E-value: 2.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 184 DFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGEALGADPATFMGMAGLGDLVLTCTDNQSRNRRF 263
Cdd:pfam07479 1 DVIGVELGGALKNVIAIAAGIADGLGLGDNAKAALITRGLAEMIRLGKALGAKPETFFGLAGLGDLIVTCTSGLSRNRRF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 264 GMMLGQGSDVKGAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREA 323
Cdd:pfam07479 81 GEALGKGKSLEEAEKELGQVAEGVYTAKAVYELAKKLGVEMPIFEAVYRILYEGKSPEEA 140
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
7-163 |
5.60e-73 |
|
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.
Pssm-ID: 395967 [Multi-domain] Cd Length: 158 Bit Score: 222.84 E-value: 5.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 7 SMTVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNVAFLPDVPFPDSLHLESDLATALAASRNILIVVPSH 86
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKGADIIVIVVPSQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2094593882 87 VFGDVLRQIKPLMRPDARIVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLASTDQAF 163
Cdd:pfam01210 81 ALREVLKQLKGLLKPDAILVSLSKGIEPGTLKLLSEVIEEELGIQPPIAVLSGPSHAEEVAQGLPTATVIASKDEEA 157
|
|
| PRK14620 |
PRK14620 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
8-315 |
6.16e-67 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173083 [Multi-domain] Cd Length: 326 Bit Score: 213.16 E-value: 6.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 8 MTVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNVAFLPDVPFPDSLHLESDLATALAASRNILIV-VPSH 86
Cdd:PRK14620 3 ISILGAGSFGTAIAIALSSKKISVNLWGRNHTTFESINTKRKNLKYLPTCHLPDNISVKSAIDEVLSDNATCIILaVPTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 87 VFGDVLRQIKPL-MRPDARIVWATKGLEAETGRLLQDVAREALGDEiPLAVISGPTFAKELAAGLPTAISLASTDQAFSD 165
Cdd:PRK14620 83 QLRTICQQLQDChLKKNTPILICSKGIEKSSLKFPSEIVNEILPNN-PIAILSGPSFAKEIAEKLPCSIVLAGQNETLGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 166 DLQQLLHcGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGEA--LGADPATFMGM 243
Cdd:PRK14620 162 SLISKLS-NENLKIIYSQDIIGVQIGAALKNIIAIACGIVLGKNLGNNAHAAVITKGMNEIKTLYSAknGSIDLNTLIGP 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2094593882 244 AGLGDLVLTCTDNQSRNRRFGMMLGQGSDVKGAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLY 315
Cdd:PRK14620 241 SCLGDLILTCTTLHSRNMSFGFKIGNGFNINQILSEGKSVIEGFSTVKPLISLAKKLNIELPICESIYNLLY 312
|
|
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
7-317 |
1.38e-55 |
|
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic enzyme, glycerol-3-phosphate dehydrogenase (NAD(+)) (EC 1.1.1.8). Enzymatic activity for 1.1.1.8 is defined as sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH. Note the very similar reactions of enzymes defined as EC 1.1.1.94 and 1.1.99.5, assigned to families of proteins in the bacteria.
Pssm-ID: 274551 [Multi-domain] Cd Length: 342 Bit Score: 184.47 E-value: 1.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 7 SMTVIGAGSYGTALAITLARNG--------HEVVLWGHDPKHIAT-----LQRDRCNVAFLPDVPFPDSLHLESDLATAL 73
Cdd:TIGR03376 1 RVAVVGSGNWGTAIAKIVAENAralpelfeESVRMWVFEEEIEGRnlteiINTTHENVKYLPGIKLPANLVAVPDLVEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 74 AASRNILIVVPSHVFGDVLRQIKPLMRPDARIVWATKGLE--AETGRLLQDVAREALGdeIPLAVISGPTFAKELAAGLP 151
Cdd:TIGR03376 81 KGADILVFVIPHQFLEGICKQLKGHVKPNARAISCIKGLEvsKDGVKLLSDIIEEELG--IPCGVLSGANLANEVAKEKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 152 TAISLASTDQAFSDD----LQQLLHcGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMS 227
Cdd:TIGR03376 159 SETTVGYRDPADFDVdarvLKALFH-RPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEMI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 228 RLGEALG--ADPATFMGMAGLGDLVLTCTDnqSRNRRFGMMLGQ-GSDVKGAQEKI--GQVVEGYRNTKEVRELAHRFGV 302
Cdd:TIGR03376 238 KFARMFFptGEVTFTFESCGVADLITTCLG--GRNFKVGRAFAKtGKSLEELEKELlnGQSLQGVATAKEVHELLKNKNK 315
|
330
....*....|....*..
gi 2094593882 303 --EMPITEEIYQVLYCG 317
Cdd:TIGR03376 316 ddEFPLFEAVYQILYEG 332
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
9-322 |
1.50e-39 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 142.85 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNGH-------EVVLWGHDP-----KHIATLQRDRCNVAFLPDVPFPDSLHLESDLATALAAS 76
Cdd:PTZ00345 15 SVIGSGNWGSAISKVVGENTQrnyifhnEVRMWVLEEivegeKLSDIINTKHENVKYLPGIKLPDNIVAVSDLKEAVEDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 77 rNILI-VVPSHVFGDVLRQIKPL--MRPDARIVWATKGLEAETGR--LLQDVAREALGdeIPLAVISGPTFAKELAAGLP 151
Cdd:PTZ00345 95 -DLLIfVIPHQFLESVLSQIKENnnLKKHARAISLTKGIIVENGKpvLCSDVIEEELG--IPCCALSGANVANDVAREEF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 152 TAISLASTDQAFSDDLQQLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLTEMSRLGE 231
Cdd:PTZ00345 172 SEATIGCEDKDDALIWQRLFDR-PYFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMKLFGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 232 AL--GADPATFMGMAGLGDLVLTCTDnqSRNRR----FGMMLGQGSDVKGAQEKI-GQVVEGYRNTKEVREL--AHRFGV 302
Cdd:PTZ00345 251 IFfpNVMDETFFESCGLADLITTCLG--GRNVRcaaeFAKRNGKKSWEEIEAELLnGQKLQGTVTLKEVYEVleSHDLKK 328
|
330 340
....*....|....*....|
gi 2094593882 303 EMPITEEIYQVLYCGKNARE 322
Cdd:PTZ00345 329 EFPLFTVTYKIAFEGADPSS 348
|
|
| GPD_NAD_C_bact |
pfam20618 |
Bacterial GPD, NAD-dependent C-terminal; This is the C-terminal domain of NAD-dependent ... |
244-310 |
1.21e-26 |
|
Bacterial GPD, NAD-dependent C-terminal; This is the C-terminal domain of NAD-dependent glycerol-3-phosphate dehydrogenase (GPD) from bacteria and archaea. GPD catalyzes the reversible reduction of dihydroxyacetone phosphate to glycerol-3-phosphate.
Pssm-ID: 466767 [Multi-domain] Cd Length: 66 Bit Score: 100.26 E-value: 1.21e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2094593882 244 AGLGDLVLTCTDNQSRNRRFGMMLGQGsdVKGAQEKIGQVVEGYRNTKEVRE-LAHRFGVEMPITEEI 310
Cdd:pfam20618 1 AGLGDLVLTCTSDLSRNRTFGLLLGKG--MTLAEAGNGQVAEGVRTAKAVAAiLARAHNVEMPILEAV 66
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
9-142 |
1.15e-08 |
|
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.
Pssm-ID: 426831 [Multi-domain] Cd Length: 147 Bit Score: 53.39 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPKHIA------TLQRDRCNVAFLPDVPFPDSLHLESdlatalaaSRNILIV 82
Cdd:pfam02558 2 AILGAGAIGSLLGARLAKAGHDVTLILRGAELAAikknglRLTSPGGERIVPPPAVTSASESLGP--------IDLVIVT 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 83 VPSHVFGDVLRQIKPLMRPDARIVWATKGLEAEtgrllqDVAREALGDEiplAVISGPTF 142
Cdd:pfam02558 74 VKAYQTEEALEDIAPLLGPNTVVLLLQNGLGHE------EVLREAVPRE---RVLGGVTT 124
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
9-131 |
2.26e-07 |
|
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 51.78 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNGHEVVLWGHdPKHIATLQRDRCNVAFLPDVPFPDSLHLESDLAtALAASRNILIVVPSHVF 88
Cdd:COG1893 4 AILGAGAIGGLLGARLARAGHDVTLVAR-GAHAEALRENGLRLESPDGDRTTVPVPAVTDPE-ELGPADLVLVAVKAYDL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2094593882 89 GDVLRQIKPLMRPDARIVWATKGLEAEtgrllqDVAREALGDE 131
Cdd:COG1893 82 EAAAEALAPLLGPDTVVLSLQNGLGHE------ERLAEALGAE 118
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
9-106 |
4.90e-06 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 47.54 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNV----AFLPDVPFPDSLHL-ESDLatalaasrnILIVV 83
Cdd:PRK06522 4 AILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLedgeITVPVLAADDPAELgPQDL---------VILAV 74
|
90 100
....*....|....*....|...
gi 2094593882 84 PSHVFGDVLRQIKPLMRPDARIV 106
Cdd:PRK06522 75 KAYQLPAALPSLAPLLGPDTPVL 97
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
9-148 |
9.93e-06 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 46.94 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRcnvaflpdVPF--P------------DSLHLESDLATALA 74
Cdd:COG1004 4 AVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGE--------IPIyePgleelvarnvaaGRLRFTTDLAEAVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 75 ASRNILIVVP-----------SHVFGdVLRQIKPLMRPDARIVwaTK-----GleaeTGRLLQDVAREAL-GDEIPLAVI 137
Cdd:COG1004 76 EADVVFIAVGtpsdedgsadlSYVLA-AARSIGEALKGYKVVV--TKstvpvG----TADRVRAIIAEELrGAGVDFDVV 148
|
170
....*....|.
gi 2094593882 138 SGPTFAKELAA 148
Cdd:COG1004 149 SNPEFLREGSA 159
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
7-102 |
1.38e-05 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 46.52 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 7 SMTVIGA-GSYGTALAITLARNGHEVVLWGHDPKHIATLQRdRCNVAFLPDvpfpdslhlesdlATALAASRNILIV-VP 84
Cdd:PRK08655 2 KISIIGGtGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAK-ELGVEYAND-------------NIDAAKDADIVIIsVP 67
|
90
....*....|....*...
gi 2094593882 85 SHVFGDVLRQIKPLMRPD 102
Cdd:PRK08655 68 INVTEDVIKEVAPHVKEG 85
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
6-114 |
5.66e-05 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 44.26 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 6 ASMTVIGAGSYGTALAITLARNGHEVVLWGHDPkhiATLQRDRCNVA-FLPDVPFPDSLHLES------------DLATA 72
Cdd:PRK06129 3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADP---AAAAAAPAYIAgRLEDLAAFDLLDGEApdavlarirvtdSLADA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2094593882 73 LAASRNILIVVPSHVFG--DVLRQIKPLMRPDARIVWATKGLEA 114
Cdd:PRK06129 80 VADADYVQESAPENLELkrALFAELDALAPPHAILASSTSALLA 123
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
10-106 |
5.77e-05 |
|
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];
Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 44.03 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 10 VIGAGSYGTALAITLARNGHEVV-LWGHDPKHIATLqrdrcnVAFLPDVPF--PDSLHLESDLatalaasrnILIVVPSH 86
Cdd:COG5495 8 IIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERA------AALLGAVPAldLEELAAEADL---------VLLAVPDD 72
|
90 100
....*....|....*....|..
gi 2094593882 87 VFGDVLRQIK--PLMRPDARIV 106
Cdd:COG5495 73 AIAEVAAGLAaaGALRPGQLVV 94
|
|
| PRK08229 |
PRK08229 |
2-dehydropantoate 2-reductase; Provisional |
5-135 |
1.11e-04 |
|
2-dehydropantoate 2-reductase; Provisional
Pssm-ID: 236193 [Multi-domain] Cd Length: 341 Bit Score: 43.45 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 5 NASMTVIGAGSYGTALAITLARNGHEVVLWGHDP------KHIATLQRDRCNVAFLPdvpfPDSLHLESDLAtALAASRN 78
Cdd:PRK08229 2 MARICVLGAGSIGCYLGGRLAAAGADVTLIGRARigdelrAHGLTLTDYRGRDVRVP----PSAIAFSTDPA-ALATADL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2094593882 79 ILIVVPSHVFGDVLRQIKPLMRPDARIVWATKGLEAEtgrllqDVAREALGDEIPLA 135
Cdd:PRK08229 77 VLVTVKSAATADAAAALAGHARPGAVVVSFQNGVRNA------DVLRAALPGATVLA 127
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
9-106 |
1.48e-04 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 43.37 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNV------AFLPDVPFPDSLHLESDLATALAASRNILIV 82
Cdd:TIGR03026 4 AVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIyepgldELLAKALKAGRLRATTDYEEAIRDADVIIIC 83
|
90 100 110
....*....|....*....|....*....|....*
gi 2094593882 83 VP-----------SHVFgDVLRQIKPLMRPDARIV 106
Cdd:TIGR03026 84 VPtplkedgspdlSYVE-SAAETIAKHLRKGATVV 117
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
10-106 |
4.09e-04 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 41.59 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 10 VIGAGSYGTALAITLARNG---HEVVLWGHDPKHIATLQRdRCNVaflpdvpfpdslHLESDLATALAASRNILIVVPSH 86
Cdd:COG0345 7 FIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAE-RYGV------------RVTTDNAEAAAQADVVVLAVKPQ 73
|
90 100
....*....|....*....|
gi 2094593882 87 VFGDVLRQIKPLMRPDARIV 106
Cdd:COG0345 74 DLAEVLEELAPLLDPDKLVI 93
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
10-102 |
1.54e-03 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 39.73 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 10 VIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCNVAflpdvpfpDSLhleSDLATALAASRNILIVVPS-HVF 88
Cdd:PRK09599 5 MIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGA--------DSL---EELVAKLPAPRVVWLMVPAgEIT 73
|
90
....*....|....
gi 2094593882 89 GDVLRQIKPLMRPD 102
Cdd:PRK09599 74 DATIDELAPLLSPG 87
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
9-105 |
8.44e-03 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 37.41 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNG--HEVVLWGHDPKHIATLQRDRcnvafLPDvpfpdslHLESDLATALAASRNILIVVPSH 86
Cdd:COG0287 5 AIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLERALELG-----VID-------RAATDLEEAVADADLVVLAVPVG 72
|
90
....*....|....*....
gi 2094593882 87 VFGDVLRQIKPLMRPDARI 105
Cdd:COG0287 73 ATIEVLAELAPHLKPGAIV 91
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
9-106 |
9.84e-03 |
|
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 397677 [Multi-domain] Cd Length: 186 Bit Score: 36.46 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593882 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPKHIATLQRDRCnvaflpdvPF--PD-----------SLHLESDLATALAA 75
Cdd:pfam03721 4 SVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQI--------PIyePGldelvkanvsgRLSFTTDYSTAIEE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2094593882 76 SRNILIVVP------------SHVFgDVLRQIKPLMRPDARIV 106
Cdd:pfam03721 76 ADVIFIAVGtpskkgggaadlKYVE-SAARSIAPHLKKGKVVV 117
|
|
| |
