|
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: 555.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 6 ASMTVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAFLPDVPFPDTLHLESDLATALAASRNILVVVPS 85
Cdd:PRK00094 2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALADADLILVAVPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 86 HVFGEVLRQIKPLMRPDARLVWATKGLEAETGRLLQDVAREALGDQIPLAVISGPTFAKELAAGLPTAISLASTDQTFAD 165
Cdd:PRK00094 82 QALREVLKQLKPLLPPDAPIVWATKGIEPGTGKLLSEVLEEELPDLAPIAVLSGPSFAKEVARGLPTAVVIASTDEELAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 166 DLQQLLHCGkSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATFMGMAG 245
Cdd:PRK00094 162 RVQELFHSP-YFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEITRLGVALGANPETFLGLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 246 LGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAAL 325
Cdd:PRK00094 241 LGDLVLTCTSPLSRNRRFGLALGQGKSLEEALAEIGMVAEGVRTAKAVYELAKKLGVEMPITEAVYAVLYEGKDPREAVE 320
|
....*
gi 16131479 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: 531.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 6 ASMTVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAFLPDVPFPDTLHLESDLATALAASRNILVVVPS 85
Cdd:COG0240 1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAGADLVLLAVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 86 HVFGEVLRQIKPLMRPDARLVWATKGLEAETGRLLQDVAREALGDQIPLAVISGPTFAKELAAGLPTAISLASTDQTFAD 165
Cdd:COG0240 81 QALREVLEQLAPLLPPGAPVVSATKGIEPGTGLLMSEVIAEELPGALRIAVLSGPSFAEEVARGLPTAVVVASEDEEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 166 DLQQLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATFMGMAG 245
Cdd:COG0240 161 RLQELLST-PYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEMTRLGVALGARPETFMGLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 246 LGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAAL 325
Cdd:COG0240 240 LGDLVLTCTSDLSRNRRFGLALGKGKSLEEALAEMGMVAEGVYTAKAVYELAEKLGVEMPITEAVYAVLYEGKSPREAVE 319
|
....*...
gi 16131479 326 TLLGRARK 333
Cdd:COG0240 320 ALMARPLK 327
|
|
| PRK12439 |
PRK12439 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
2-335 |
3.16e-85 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 171500 [Multi-domain] Cd Length: 341 Bit Score: 260.87 E-value: 3.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 2 NQRNASMTVIGAGSYGTALAITLARNGhEVVLWGHDPEHIATLERDRCNAAFLP-DVPFPDTLHLESDLATALAASRNIL 80
Cdd:PRK12439 4 AKREPKVVVLGGGSWGTTVASICARRG-PTLQWVRSAETADDINDNHRNSRYLGnDVVLSDTLRATTDFAEAANCADVVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 81 VVVPSHVFGEVLRQIKPLMRPDARLVWATKGLEAETGRLLQDVAREALGDQiPLAVISGPTFAKELAAGLPTAISLASTD 160
Cdd:PRK12439 83 MGVPSHGFRGVLTELAKELRPWVPVVSLVKGLEQGTNMRMSQIIEEVLPGH-PAGILAGPNIAREVAEGYAAAAVLAMPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 161 QTFADDLQQLLHCGKsFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATF 240
Cdd:PRK12439 162 QHLATRLSPLFRTRR-FRVYTTDDVVGVEMAGALKNVFAIAVGMGYSLGIGENTRAMVIARALREMTKLGVAMGGNPETF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 241 MGMAGLGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNA 320
Cdd:PRK12439 241 AGLAGMGDLIVTCTSQRSRNRHVGEQLGAGKPIDEIIASMNQVAEGVKAASVVMEFADEYGLNMPIAREVDAVINHGSTV 320
|
330
....*....|....*
gi 16131479 321 REAALTLLGRARKDE 335
Cdd:PRK12439 321 EQAYRGLIAEVPGHE 335
|
|
| PRK14618 |
PRK14618 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
10-335 |
1.07e-84 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237770 [Multi-domain] Cd Length: 328 Bit Score: 259.03 E-value: 1.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 10 VIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAFLPDVPFPDTLHLESDLATALAASRNILVVVPSHVFG 89
Cdd:PRK14618 9 VLGAGAWGTALAVLAASKGVPVRLWARRPEFAAALAAERENREYLPGVALPAELYPTADPEEALAGADFAVVAVPSKALR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 90 EVLRQIKPlmrpDARLVWATKGLEAETGRLLQDVAREALGDQIPLAVISGPTFAKELAAGLPTAISLASTDQTFADDLQQ 169
Cdd:PRK14618 89 ETLAGLPR----ALGYVSCAKGLAPDGGRLSELARVLEFLTQARVAVLSGPNHAEEIARFLPAATVVASPEPGLARRVQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 170 LLhCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATFMGMAGLGDL 249
Cdd:PRK14618 165 AF-SGPSFRVYTSRDRVGVELGGALKNVIALAAGMVDGLKLGDNAKAALITRGLREMVRFGVALGAEEATFYGLSGLGDL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 250 VLTCTDNQSRNRRFGMMLGQGMDVQSAQEKiGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAALTLLG 329
Cdd:PRK14618 244 IATATSPHSRNRAAGEAIVRGVDREHLEAG-GKVVEGLYTVKALDAWAKAHGHDLPIVEAVARVARGGWDPLAGLRSLMG 322
|
....*.
gi 16131479 330 RARKDE 335
Cdd:PRK14618 323 REAKEE 328
|
|
| PRK14619 |
PRK14619 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
7-335 |
8.51e-84 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237771 [Multi-domain] Cd Length: 308 Bit Score: 256.07 E-value: 8.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 7 SMTVIGAGSYGTALAITLARNGHEVVLWGHdpehiatlerdrcnaaflpdvpfpdtlHLESDLATALAASRNILVVVPSH 86
Cdd:PRK14619 6 TIAILGAGAWGSTLAGLASANGHRVRVWSR---------------------------RSGLSLAAVLADADVIVSAVSMK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 87 VFGEVLRQIKPL-MRPDARLVWATKGLEAETGRLLQDVAREALGDQiPLAVISGPTFAKELAAGLPTAISLASTDQTFAD 165
Cdd:PRK14619 59 GVRPVAEQVQALnLPPETIIVTATKGLDPETTRTPSQIWQAAFPNH-PVVVLSGPNLSKEIQQGLPAATVVASRDLAAAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 166 DLQQLLhCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATFMGMAG 245
Cdd:PRK14619 138 TVQQIF-SSERFRVYTNSDPLGTELGGTLKNVIAIAAGVCDGLQLGTNAKAALVTRALPEMIRVGTHLGAQTETFYGLSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 246 LGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLyCGKNAREAAL 325
Cdd:PRK14619 217 LGDLLATCTSPLSRNYQVGYGLAQGKSLEQILAELEGTAEGVNTANVLVQLAQQQNIAVPITEQVYRLL-QGEITPQQAL 295
|
330
....*....|.
gi 16131479 326 T-LLGRARKDE 335
Cdd:PRK14619 296 EeLMERDLKPE 306
|
|
| NAD_Gly3P_dh_C |
pfam07479 |
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent ... |
184-323 |
7.85e-79 |
|
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: 237.29 E-value: 7.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 184 DFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATFMGMAGLGDLVLTCTDNQSRNRRF 263
Cdd:pfam07479 1 DVIGVELGGALKNVIAIAAGIADGLGLGDNAKAALITRGLAEMIRLGKALGAKPETFFGLAGLGDLIVTCTSGLSRNRRF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 264 GMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREA 323
Cdd:pfam07479 81 GEALGKGKSLEEAEKELGQVAEGVYTAKAVYELAKKLGVEMPIFEAVYRILYEGKSPEEA 140
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
7-164 |
1.03e-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: 224.76 E-value: 1.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 7 SMTVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAFLPDVPFPDTLHLESDLATALAASRNILVVVPSH 86
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKGADIIVIVVPSQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131479 87 VFGEVLRQIKPLMRPDARLVWATKGLEAETGRLLQDVAREALGDQIPLAVISGPTFAKELAAGLPTAISLASTDQTFA 164
Cdd:pfam01210 81 ALREVLKQLKGLLKPDAILVSLSKGIEPGTLKLLSEVIEEELGIQPPIAVLSGPSHAEEVAQGLPTATVIASKDEEAA 158
|
|
| PRK14620 |
PRK14620 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
8-315 |
4.26e-68 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173083 [Multi-domain] Cd Length: 326 Bit Score: 216.24 E-value: 4.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 8 MTVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAFLPDVPFPDTLHLESDLATALAASRN-ILVVVPSH 86
Cdd:PRK14620 3 ISILGAGSFGTAIAIALSSKKISVNLWGRNHTTFESINTKRKNLKYLPTCHLPDNISVKSAIDEVLSDNATcIILAVPTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 87 VFGEVLRQIKPL-MRPDARLVWATKGLEAETGRLLQDVAREALGDQiPLAVISGPTFAKELAAGLPTAISLASTDQTFAD 165
Cdd:PRK14620 83 QLRTICQQLQDChLKKNTPILICSKGIEKSSLKFPSEIVNEILPNN-PIAILSGPSFAKEIAEKLPCSIVLAGQNETLGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 166 DLQQLLHcGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAA--LGADPATFMGM 243
Cdd:PRK14620 162 SLISKLS-NENLKIIYSQDIIGVQIGAALKNIIAIACGIVLGKNLGNNAHAAVITKGMNEIKTLYSAknGSIDLNTLIGP 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131479 244 AGLGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLY 315
Cdd:PRK14620 241 SCLGDLILTCTTLHSRNMSFGFKIGNGFNINQILSEGKSVIEGFSTVKPLISLAKKLNIELPICESIYNLLY 312
|
|
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
7-317 |
1.82e-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: 184.08 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 7 SMTVIGAGSYGTALAITLARNG--------HEVVLWGHDPEHIATLERDRCNAA-----FLPDVPFPDTLHLESDLATAl 73
Cdd:TIGR03376 1 RVAVVGSGNWGTAIAKIVAENAralpelfeESVRMWVFEEEIEGRNLTEIINTThenvkYLPGIKLPANLVAVPDLVEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 74 AASRNILV-VVPSHVFGEVLRQIKPLMRPDARLVWATKGLE--AETGRLLQDVAREALGdqIPLAVISGPTFAKELAAGL 150
Cdd:TIGR03376 80 AKGADILVfVIPHQFLEGICKQLKGHVKPNARAISCIKGLEvsKDGVKLLSDIIEEELG--IPCGVLSGANLANEVAKEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 151 PTAISLASTDQTFADD----LQQLLHcGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEM 226
Cdd:TIGR03376 158 FSETTVGYRDPADFDVdarvLKALFH-RPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 227 SRLGAALG--ADPATFMGMAGLGDLVLTCTDnqSRNRRFGMMLGQ-GMDVQSAQEKI--GQVVEGYRNTKEVRELAHRFG 301
Cdd:TIGR03376 237 IKFARMFFptGEVTFTFESCGVADLITTCLG--GRNFKVGRAFAKtGKSLEELEKELlnGQSLQGVATAKEVHELLKNKN 314
|
330
....*....|....*...
gi 16131479 302 V--EMPITEEIYQVLYCG 317
Cdd:TIGR03376 315 KddEFPLFEAVYQILYEG 332
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
9-322 |
8.73e-39 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 140.93 E-value: 8.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 9 TVIGAGSYGTALAITLARNGH-------EVVLWGHDP----EHIATL-ERDRCNAAFLPDVPFPDTLHLESDLATALAAS 76
Cdd:PTZ00345 15 SVIGSGNWGSAISKVVGENTQrnyifhnEVRMWVLEEivegEKLSDIiNTKHENVKYLPGIKLPDNIVAVSDLKEAVEDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 77 RNILVVVPSHVFGEVLRQIKPL--MRPDARLVWATKGLEAETGR--LLQDVAREALGdqIPLAVISGPTFAKELAAGLPT 152
Cdd:PTZ00345 95 DLLIFVIPHQFLESVLSQIKENnnLKKHARAISLTKGIIVENGKpvLCSDVIEEELG--IPCCALSGANVANDVAREEFS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 153 AISLASTDQTFADDLQQLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAA 232
Cdd:PTZ00345 173 EATIGCEDKDDALIWQRLFDR-PYFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMKLFGKI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 233 L--GADPATFMGMAGLGDLVLTCTDnqSRNRR----FGMMLGQGMDVQSAQEKI-GQVVEGYRNTKEVREL--AHRFGVE 303
Cdd:PTZ00345 252 FfpNVMDETFFESCGLADLITTCLG--GRNVRcaaeFAKRNGKKSWEEIEAELLnGQKLQGTVTLKEVYEVleSHDLKKE 329
|
330
....*....|....*....
gi 16131479 304 MPITEEIYQVLYCGKNARE 322
Cdd:PTZ00345 330 FPLFTVTYKIAFEGADPSS 348
|
|
| GPD_NAD_C_bact |
pfam20618 |
Bacterial GPD, NAD-dependent C-terminal; This is the C-terminal domain of NAD-dependent ... |
244-310 |
1.06e-27 |
|
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: 102.96 E-value: 1.06e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131479 244 AGLGDLVLTCTDNQSRNRRFGMMLGQGMDVqsAQEKIGQVVEGYRNTKEVRE-LAHRFGVEMPITEEI 310
Cdd:pfam20618 1 AGLGDLVLTCTSDLSRNRTFGLLLGKGMTL--AEAGNGQVAEGVRTAKAVAAiLARAHNVEMPILEAV 66
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
9-142 |
3.64e-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: 51.85 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPEHIA------TLERDRCNAAFLPDVPFPDTLHLESdlatalaaSRNILVV 82
Cdd:pfam02558 2 AILGAGAIGSLLGARLAKAGHDVTLILRGAELAAikknglRLTSPGGERIVPPPAVTSASESLGP--------IDLVIVT 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 83 VPSHVFGEVLRQIKPLMRPDARLVWATKGLEAEtgrllqDVAREALGDQiplAVISGPTF 142
Cdd:pfam02558 74 VKAYQTEEALEDIAPLLGPNTVVLLLQNGLGHE------EVLREAVPRE---RVLGGVTT 124
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
9-106 |
1.17e-05 |
|
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: 46.39 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 9 TVIGAGSYGTALAITLARNGHEVVLWGHdPEHIATLERDRCNAAFLPDVPFPDTLHLESDLAtALAASRNILVVVPSHVF 88
Cdd:COG1893 4 AILGAGAIGGLLGARLARAGHDVTLVAR-GAHAEALRENGLRLESPDGDRTTVPVPAVTDPE-ELGPADLVLVAVKAYDL 81
|
90
....*....|....*...
gi 16131479 89 GEVLRQIKPLMRPDARLV 106
Cdd:COG1893 82 EAAAEALAPLLGPDTVVL 99
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
10-106 |
2.08e-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: 45.57 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 10 VIGAGSYGTALAITLARNGHEVV-LWGHDPEHIATLerdrcnAAFLPDVPFPDTLHL--ESDLatalaasrnILVVVPSH 86
Cdd:COG5495 8 IIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERA------AALLGAVPALDLEELaaEADL---------VLLAVPDD 72
|
90 100
....*....|....*....|..
gi 16131479 87 VFGEVLRQIK--PLMRPDARLV 106
Cdd:COG5495 73 AIAEVAAGLAaaGALRPGQLVV 94
|
|
| PRK08229 |
PRK08229 |
2-dehydropantoate 2-reductase; Provisional |
4-135 |
2.47e-05 |
|
2-dehydropantoate 2-reductase; Provisional
Pssm-ID: 236193 [Multi-domain] Cd Length: 341 Bit Score: 45.38 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 4 RNASMTVIGAGSYGTALAITLARNGHEVVLWGHDP------EHIATLERDRCNAAFLPdvpfPDTLHLESDLAtALAASR 77
Cdd:PRK08229 1 MMARICVLGAGSIGCYLGGRLAAAGADVTLIGRARigdelrAHGLTLTDYRGRDVRVP----PSAIAFSTDPA-ALATAD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131479 78 NILVVVPSHVFGEVLRQIKPLMRPDARLVWATKGLEAEtgrllqDVAREALGDQIPLA 135
Cdd:PRK08229 76 LVLVTVKSAATADAAAALAGHARPGAVVVSFQNGVRNA------DVLRAALPGATVLA 127
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
9-106 |
3.25e-05 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 44.84 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERD--RCNAA--FLPDVPFPDTLHL-ESDLatalaasrnILVVV 83
Cdd:PRK06522 4 AILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENglRLEDGeiTVPVLAADDPAELgPQDL---------VILAV 74
|
90 100
....*....|....*....|...
gi 16131479 84 PSHVFGEVLRQIKPLMRPDARLV 106
Cdd:PRK06522 75 KAYQLPAALPSLAPLLGPDTPVL 97
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
6-114 |
3.84e-05 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 44.65 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 6 ASMTVIGAGSYGTALAITLARNGHEVVLWGHDPehiATLERDRCN-AAFLPDVPFPDTLHLES------------DLATA 72
Cdd:PRK06129 3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADP---AAAAAAPAYiAGRLEDLAAFDLLDGEApdavlarirvtdSLADA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16131479 73 LAASRNILVVVPSHVFG--EVLRQIKPLMRPDARLVWATKGLEA 114
Cdd:PRK06129 80 VADADYVQESAPENLELkrALFAELDALAPPHAILASSTSALLA 123
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
7-106 |
1.96e-04 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 43.05 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 7 SMTVIGA-GSYGTALAITLARNGHEVVLWGHDPEHIATLERdRCNAAFLPDvpfpdtlhlesdlATALAASRNILVV-VP 84
Cdd:PRK08655 2 KISIIGGtGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAK-ELGVEYAND-------------NIDAAKDADIVIIsVP 67
|
90 100
....*....|....*....|..
gi 16131479 85 SHVFGEVLRQIKPLMRPDARLV 106
Cdd:PRK08655 68 INVTEDVIKEVAPHVKEGSLLM 89
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
10-102 |
2.08e-04 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 42.43 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 10 VIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAflpdvpfpDTLhleSDLATALAASRNILVVVPS-HVF 88
Cdd:PRK09599 5 MIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGA--------DSL---EELVAKLPAPRVVWLMVPAgEIT 73
|
90
....*....|....
gi 16131479 89 GEVLRQIKPLMRPD 102
Cdd:PRK09599 74 DATIDELAPLLSPG 87
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
9-148 |
2.59e-04 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 42.70 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRcnaaflpdVPF--P------------DTLHLESDLATALA 74
Cdd:COG1004 4 AVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGE--------IPIyePgleelvarnvaaGRLRFTTDLAEAVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 75 ASRNILVVVP-----------SHVFgEVLRQIKPLMRPDARLVwaTK-----GleaeTGRLLQDVAREAL-GDQIPLAVI 137
Cdd:COG1004 76 EADVVFIAVGtpsdedgsadlSYVL-AAARSIGEALKGYKVVV--TKstvpvG----TADRVRAIIAEELrGAGVDFDVV 148
|
170
....*....|.
gi 16131479 138 SGPTFAKELAA 148
Cdd:COG1004 149 SNPEFLREGSA 159
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
10-44 |
1.66e-03 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 39.00 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|....*
gi 16131479 10 VIGAGSYGTALAITLARNGHEVVLWGHDPEHIATL 44
Cdd:COG2085 3 IIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAAL 37
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
10-106 |
1.88e-03 |
|
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: 39.28 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 10 VIGAGSYGTALAITLARNG---HEVVLWGHDPEHIATLERdRCNaaflpdvpfpdtLHLESDLATALAASRNILVVVPSH 86
Cdd:COG0345 7 FIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAE-RYG------------VRVTTDNAEAAAQADVVVLAVKPQ 73
|
90 100
....*....|....*....|
gi 16131479 87 VFGEVLRQIKPLMRPDARLV 106
Cdd:COG0345 74 DLAEVLEELAPLLDPDKLVI 93
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
9-106 |
3.64e-03 |
|
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: 38.75 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 9 TVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCnaaflpdvPFPD--------------TLHLESDLATALA 74
Cdd:TIGR03026 4 AVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKS--------PIYEpgldellakalkagRLRATTDYEEAIR 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 16131479 75 ASRNILVVVP-----------SHVFgEVLRQIKPLMRPDARLV 106
Cdd:TIGR03026 76 DADVIIICVPtplkedgspdlSYVE-SAAETIAKHLRKGATVV 117
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
9-103 |
6.51e-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: 37.80 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131479 9 TVIGAGSYGTALAITLARNG--HEVVLWGHDPEHIAT-LERDRCNAAflpdvpfpdtlhlESDLATALAASRNILVVVPS 85
Cdd:COG0287 5 AIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLERaLELGVIDRA-------------ATDLEEAVADADLVVLAVPV 71
|
90
....*....|....*...
gi 16131479 86 HVFGEVLRQIKPLMRPDA 103
Cdd:COG0287 72 GATIEVLAELAPHLKPGA 89
|
|
| |
