|
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: 547.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 6 ASMTVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNVAFLPDVPFPDTLHLESDLATALAASRNILVVVPS 85
Cdd:PRK00094 2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALADADLILVAVPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 86 HVFGQVLRQIKPLMRPDARVVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLAATDETFAD 165
Cdd:PRK00094 82 QALREVLKQLKPLLPPDAPIVWATKGIEPGTGKLLSEVLEEELPDLAPIAVLSGPSFAKEVARGLPTAVVIASTDEELAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 166 DLQQLLHCGkSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPTTFMGMAG 245
Cdd:PRK00094 162 RVQELFHSP-YFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEITRLGVALGANPETFLGLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 246 LGDLVLTCTDNQSRNRRFGMMLGQGADVQSAQEKIGQVVEGYRNTKEVRELAARVGVEMPITEEIYQVLYCGKNAREAAL 325
Cdd:PRK00094 241 LGDLVLTCTSPLSRNRRFGLALGQGKSLEEALAEIGMVAEGVRTAKAVYELAKKLGVEMPITEAVYAVLYEGKDPREAVE 320
|
....*
gi 495054616 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: 522.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 6 ASMTVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNVAFLPDVPFPDTLHLESDLATALAASRNILVVVPS 85
Cdd:COG0240 1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAGADLVLLAVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 86 HVFGQVLRQIKPLMRPDARVVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLAATDETFAD 165
Cdd:COG0240 81 QALREVLEQLAPLLPPGAPVVSATKGIEPGTGLLMSEVIAEELPGALRIAVLSGPSFAEEVARGLPTAVVVASEDEEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 166 DLQQLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPTTFMGMAG 245
Cdd:COG0240 161 RLQELLST-PYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEMTRLGVALGARPETFMGLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 246 LGDLVLTCTDNQSRNRRFGMMLGQGADVQSAQEKIGQVVEGYRNTKEVRELAARVGVEMPITEEIYQVLYCGKNAREAAL 325
Cdd:COG0240 240 LGDLVLTCTSDLSRNRRFGLALGKGKSLEEALAEMGMVAEGVYTAKAVYELAEKLGVEMPITEAVYAVLYEGKSPREAVE 319
|
....*...
gi 495054616 326 TLLGRTRK 333
Cdd:COG0240 320 ALMARPLK 327
|
|
| PRK14618 |
PRK14618 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
2-335 |
1.23e-82 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237770 [Multi-domain] Cd Length: 328 Bit Score: 253.64 E-value: 1.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 2 NTINASMTVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNVAFLPDVPFPDTLHLESDLATALAASRNILV 81
Cdd:PRK14618 1 MHHGMRVAVLGAGAWGTALAVLAASKGVPVRLWARRPEFAAALAAERENREYLPGVALPAELYPTADPEEALAGADFAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 82 VVPShvfgQVLRQIKPLMRPDARVVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLAATDE 161
Cdd:PRK14618 81 AVPS----KALRETLAGLPRALGYVSCAKGLAPDGGRLSELARVLEFLTQARVAVLSGPNHAEEIARFLPAATVVASPEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 162 TFADDLQQLLhCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPTTFM 241
Cdd:PRK14618 157 GLARRVQAAF-SGPSFRVYTSRDRVGVELGGALKNVIALAAGMVDGLKLGDNAKAALITRGLREMVRFGVALGAEEATFY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 242 GMAGLGDLVLTCTDNQSRNRRFGMMLGQGADVQSAQEKiGQVVEGYRNTKEVRELAARVGVEMPITEEIYQVLYCGKNAR 321
Cdd:PRK14618 236 GLSGLGDLIATATSPHSRNRAAGEAIVRGVDREHLEAG-GKVVEGLYTVKALDAWAKAHGHDLPIVEAVARVARGGWDPL 314
|
330
....*....|....
gi 495054616 322 EAALTLLGRTRKDE 335
Cdd:PRK14618 315 AGLRSLMGREAKEE 328
|
|
| PRK12439 |
PRK12439 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
10-335 |
1.31e-80 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 171500 [Multi-domain] Cd Length: 341 Bit Score: 248.93 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 10 VIGAGSYGTALAITLARNGHhVVLWGHDPAHIATLQADRCNVAFLP-DVPFPDTLHLESDLATALAASRNILVVVPSHVF 88
Cdd:PRK12439 12 VLGGGSWGTTVASICARRGP-TLQWVRSAETADDINDNHRNSRYLGnDVVLSDTLRATTDFAEAANCADVVVMGVPSHGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 89 GQVLRQIKPLMRPDARVVWATKGLEAETGRLLQDVAREALGDEiPLAVISGPTFAKELAAGLPTAISLAATDETFADDLQ 168
Cdd:PRK12439 91 RGVLTELAKELRPWVPVVSLVKGLEQGTNMRMSQIIEEVLPGH-PAGILAGPNIAREVAEGYAAAAVLAMPDQHLATRLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 169 QLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPTTFMGMAGLGD 248
Cdd:PRK12439 170 PLFRT-RRFRVYTTDDVVGVEMAGALKNVFAIAVGMGYSLGIGENTRAMVIARALREMTKLGVAMGGNPETFAGLAGMGD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 249 LVLTCTDNQSRNRRFGMMLGQGADVQSAQEKIGQVVEGYRNTKEVRELAARVGVEMPITEEIYQVLYCGKNAREAALTLL 328
Cdd:PRK12439 249 LIVTCTSQRSRNRHVGEQLGAGKPIDEIIASMNQVAEGVKAASVVMEFADEYGLNMPIAREVDAVINHGSTVEQAYRGLI 328
|
....*..
gi 495054616 329 GRTRKDE 335
Cdd:PRK12439 329 AEVPGHE 335
|
|
| PRK14619 |
PRK14619 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
7-335 |
6.24e-80 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237771 [Multi-domain] Cd Length: 308 Bit Score: 246.05 E-value: 6.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 7 SMTVIGAGSYGTALAITLARNGHHVVLWGHdpahiatlqadrcnvaflpdvpfpdtlHLESDLATALAASRNILVVVPSH 86
Cdd:PRK14619 6 TIAILGAGAWGSTLAGLASANGHRVRVWSR---------------------------RSGLSLAAVLADADVIVSAVSMK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 87 VFGQVLRQIKPL-MRPDARVVWATKGLEAETGRLLQDVAREALGDEiPLAVISGPTFAKELAAGLPTAISLAATDETFAD 165
Cdd:PRK14619 59 GVRPVAEQVQALnLPPETIIVTATKGLDPETTRTPSQIWQAAFPNH-PVVVLSGPNLSKEIQQGLPAATVVASRDLAAAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 166 DLQQLLhCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPTTFMGMAG 245
Cdd:PRK14619 138 TVQQIF-SSERFRVYTNSDPLGTELGGTLKNVIAIAAGVCDGLQLGTNAKAALVTRALPEMIRVGTHLGAQTETFYGLSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 246 LGDLVLTCTDNQSRNRRFGMMLGQGADVQSAQEKIGQVVEGYRNTKEVRELAARVGVEMPITEEIYQVLyCGKNAREAAL 325
Cdd:PRK14619 217 LGDLLATCTSPLSRNYQVGYGLAQGKSLEQILAELEGTAEGVNTANVLVQLAQQQNIAVPITEQVYRLL-QGEITPQQAL 295
|
330
....*....|.
gi 495054616 326 T-LLGRTRKDE 335
Cdd:PRK14619 296 EeLMERDLKPE 306
|
|
| NAD_Gly3P_dh_C |
pfam07479 |
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent ... |
184-323 |
2.42e-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: 2.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 184 DFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPTTFMGMAGLGDLVLTCTDNQSRNRRF 263
Cdd:pfam07479 1 DVIGVELGGALKNVIAIAAGIADGLGLGDNAKAALITRGLAEMIRLGKALGAKPETFFGLAGLGDLIVTCTSGLSRNRRF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 264 GMMLGQGADVQSAQEKIGQVVEGYRNTKEVRELAARVGVEMPITEEIYQVLYCGKNAREA 323
Cdd:pfam07479 81 GEALGKGKSLEEAEKELGQVAEGVYTAKAVYELAKKLGVEMPIFEAVYRILYEGKSPEEA 140
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
7-164 |
1.04e-70 |
|
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: 217.06 E-value: 1.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 7 SMTVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNVAFLPDVPFPDTLHLESDLATALAASRNILVVVPSH 86
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKGADIIVIVVPSQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495054616 87 VFGQVLRQIKPLMRPDARVVWATKGLEAETGRLLQDVAREALGDEIPLAVISGPTFAKELAAGLPTAISLAATDETFA 164
Cdd:pfam01210 81 ALREVLKQLKGLLKPDAILVSLSKGIEPGTLKLLSEVIEEELGIQPPIAVLSGPSHAEEVAQGLPTATVIASKDEEAA 158
|
|
| PRK14620 |
PRK14620 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
8-315 |
8.74e-69 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173083 [Multi-domain] Cd Length: 326 Bit Score: 218.16 E-value: 8.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 8 MTVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNVAFLPDVPFPDTLHLESDLATALAASRN-ILVVVPSH 86
Cdd:PRK14620 3 ISILGAGSFGTAIAIALSSKKISVNLWGRNHTTFESINTKRKNLKYLPTCHLPDNISVKSAIDEVLSDNATcIILAVPTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 87 VFGQVLRQIKPL-MRPDARVVWATKGLEAETGRLLQDVAREALGDEiPLAVISGPTFAKELAAGLPTAISLAATDETFAD 165
Cdd:PRK14620 83 QLRTICQQLQDChLKKNTPILICSKGIEKSSLKFPSEIVNEILPNN-PIAILSGPSFAKEIAEKLPCSIVLAGQNETLGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 166 DLQQLLHcGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAA--LGADPTTFMGM 243
Cdd:PRK14620 162 SLISKLS-NENLKIIYSQDIIGVQIGAALKNIIAIACGIVLGKNLGNNAHAAVITKGMNEIKTLYSAknGSIDLNTLIGP 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495054616 244 AGLGDLVLTCTDNQSRNRRFGMMLGQGADVQSAQEKIGQVVEGYRNTKEVRELAARVGVEMPITEEIYQVLY 315
Cdd:PRK14620 241 SCLGDLILTCTTLHSRNMSFGFKIGNGFNINQILSEGKSVIEGFSTVKPLISLAKKLNIELPICESIYNLLY 312
|
|
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
7-317 |
6.44e-58 |
|
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: 190.63 E-value: 6.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 7 SMTVIGAGSYGTALAITLARNG--------HHVVLW-------GHDPAHIatLQADRCNVAFLPDVPFPDTLHLESDLAT 71
Cdd:TIGR03376 1 RVAVVGSGNWGTAIAKIVAENAralpelfeESVRMWvfeeeieGRNLTEI--INTTHENVKYLPGIKLPANLVAVPDLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 72 AlAASRNILV-VVPSHVFGQVLRQIKPLMRPDARVVWATKGLE--AETGRLLQDVAREALGdeIPLAVISGPTFAKELAA 148
Cdd:TIGR03376 79 A-AKGADILVfVIPHQFLEGICKQLKGHVKPNARAISCIKGLEvsKDGVKLLSDIIEEELG--IPCGVLSGANLANEVAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 149 GLPTAISLAATDETFADD----LQQLLHcGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLA 224
Cdd:TIGR03376 156 EKFSETTVGYRDPADFDVdarvLKALFH-RPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 225 EMSRLGAALG--ADPTTFMGMAGLGDLVLTCTDnqSRNRRFGMMLGQ-GADVQSAQEKI--GQVVEGYRNTKEVRELAAR 299
Cdd:TIGR03376 235 EMIKFARMFFptGEVTFTFESCGVADLITTCLG--GRNFKVGRAFAKtGKSLEELEKELlnGQSLQGVATAKEVHELLKN 312
|
330 340
....*....|....*....|
gi 495054616 300 VGV--EMPITEEIYQVLYCG 317
Cdd:TIGR03376 313 KNKddEFPLFEAVYQILYEG 332
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
9-322 |
7.14e-38 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 138.61 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 9 TVIGAGSYGTALAITLARNGHH-------VVLW-------GHDPAHIatLQADRCNVAFLPDVPFPDTLHLESDLATALA 74
Cdd:PTZ00345 15 SVIGSGNWGSAISKVVGENTQRnyifhneVRMWvleeiveGEKLSDI--INTKHENVKYLPGIKLPDNIVAVSDLKEAVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 75 ASRNILVVVPSHVFGQVLRQIKPL--MRPDARVVWATKGLEAETGR--LLQDVAREALGdeIPLAVISGPTFAKELAAGL 150
Cdd:PTZ00345 93 DADLLIFVIPHQFLESVLSQIKENnnLKKHARAISLTKGIIVENGKpvLCSDVIEEELG--IPCCALSGANVANDVAREE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 151 PTAISLAATDETFADDLQQLLHCgKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLG 230
Cdd:PTZ00345 171 FSEATIGCEDKDDALIWQRLFDR-PYFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMKLFG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 231 AALGADPT--TFMGMAGLGDLVLTCTDnqSRNRR----FGMMLGQGADVQSAQEKI-GQVVEGYRNTKEVREL--AARVG 301
Cdd:PTZ00345 250 KIFFPNVMdeTFFESCGLADLITTCLG--GRNVRcaaeFAKRNGKKSWEEIEAELLnGQKLQGTVTLKEVYEVleSHDLK 327
|
330 340
....*....|....*....|.
gi 495054616 302 VEMPITEEIYQVLYCGKNARE 322
Cdd:PTZ00345 328 KEFPLFTVTYKIAFEGADPSS 348
|
|
| GPD_NAD_C_bact |
pfam20618 |
Bacterial GPD, NAD-dependent C-terminal; This is the C-terminal domain of NAD-dependent ... |
244-310 |
8.58e-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: 97.95 E-value: 8.58e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495054616 244 AGLGDLVLTCTDNQSRNRRFGMMLGQGadVQSAQEKIGQVVEGYRNTKEVRE-LAARVGVEMPITEEI 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 |
1.87e-07 |
|
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: 49.92 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 9 TVIGAGSYGTALAITLARNGHHVVLWGHDPAHIA------TLQADRCNVAFLPDVPFPDTLHLESdlatalaaSRNILVV 82
Cdd:pfam02558 2 AILGAGAIGSLLGARLAKAGHDVTLILRGAELAAikknglRLTSPGGERIVPPPAVTSASESLGP--------IDLVIVT 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 83 VPSHVFGQVLRQIKPLMRPDARVVWATKGLEAEtgrllqDVAREALGDEiplAVISGPTF 142
Cdd:pfam02558 74 VKAYQTEEALEDIAPLLGPNTVVLLLQNGLGHE------EVLREAVPRE---RVLGGVTT 124
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
9-314 |
9.98e-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: 49.47 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 9 TVIGAGSYGTALAITLARNGHHVVLWGHdPAHIATLQADRCNVAFLPDVPFPDTLHLESDLAtALAASRNILVVVPSHVF 88
Cdd:COG1893 4 AILGAGAIGGLLGARLARAGHDVTLVAR-GAHAEALRENGLRLESPDGDRTTVPVPAVTDPE-ELGPADLVLVAVKAYDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 89 GQVLRQIKPLMRPDARVVWATKGLEAEtgrllqDVAREALGDEiplAVISGPTF--AKELAAGL-----PTAISLAATDE 161
Cdd:COG1893 82 EAAAEALAPLLGPDTVVLSLQNGLGHE------ERLAEALGAE---RVLGGVVTigATREEPGVvrhtgGGRLVLGELDG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 162 TFADDLQQLL----HCGksFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANART----ALITRGLAEMSRLGAAL 233
Cdd:COG1893 153 GPSERLEALAelleAAG--IPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADpearALARALMREVLAVARAE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 234 GADPTTfmgmAGLGDLVLTCTDNQSRNRrfGMMLgqgADVQSaqekiGQVVE-GYRNtKEVRELAARVGVEMPITEEIYQ 312
Cdd:COG1893 231 GVPLPE----DDLEERVAAVAEATADNR--SSML---QDLEA-----GRPTEiDAIN-GAVVRLARRLGVPTPVNEALYA 295
|
..
gi 495054616 313 VL 314
Cdd:COG1893 296 LL 297
|
|
| PRK08229 |
PRK08229 |
2-dehydropantoate 2-reductase; Provisional |
5-135 |
2.38e-05 |
|
2-dehydropantoate 2-reductase; Provisional
Pssm-ID: 236193 [Multi-domain] Cd Length: 341 Bit Score: 45.38 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 5 NASMTVIGAGSYGTALAITLARNGHHVVLWGHDP------AHIATLQADRCNVAFLPdvpfPDTLHLESDLAtALAASRN 78
Cdd:PRK08229 2 MARICVLGAGSIGCYLGGRLAAAGADVTLIGRARigdelrAHGLTLTDYRGRDVRVP----PSAIAFSTDPA-ALATADL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 495054616 79 ILVVVPSHVFGQVLRQIKPLMRPDARVVWATKGLEAEtgrllqDVAREALGDEIPLA 135
Cdd:PRK08229 77 VLVTVKSAATADAAAALAGHARPGAVVVSFQNGVRNA------DVLRAALPGATVLA 127
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
9-148 |
3.04e-05 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 45.40 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 9 TVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRcnvaflpdVPF--P------------DTLHLESDLATALA 74
Cdd:COG1004 4 AVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGE--------IPIyePgleelvarnvaaGRLRFTTDLAEAVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 75 ASRNILVVVP-----------SHVFgQVLRQIKPLMRPDARVVwaTK-----GleaeTGRLLQDVAREAL-GDEIPLAVI 137
Cdd:COG1004 76 EADVVFIAVGtpsdedgsadlSYVL-AAARSIGEALKGYKVVV--TKstvpvG----TADRVRAIIAEELrGAGVDFDVV 148
|
170
....*....|.
gi 495054616 138 SGPTFAKELAA 148
Cdd:COG1004 149 SNPEFLREGSA 159
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
9-106 |
4.41e-05 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 44.46 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 9 TVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNV----AFLPDVPFPDTLHL-ESDLatalaasrnILVVV 83
Cdd:PRK06522 4 AILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLedgeITVPVLAADDPAELgPQDL---------VILAV 74
|
90 100
....*....|....*....|...
gi 495054616 84 PSHVFGQVLRQIKPLMRPDARVV 106
Cdd:PRK06522 75 KAYQLPAALPSLAPLLGPDTPVL 97
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
10-106 |
6.61e-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: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 10 VIGAGSYGTALAITLARNGHHVV-LWGHDPAHIATLqadrcnVAFLPDVPFPDTLHL--ESDLatalaasrnILVVVPSH 86
Cdd:COG5495 8 IIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERA------AALLGAVPALDLEELaaEADL---------VLLAVPDD 72
|
90 100
....*....|....*....|..
gi 495054616 87 VFGQVLRQIK--PLMRPDARVV 106
Cdd:COG5495 73 AIAEVAAGLAaaGALRPGQLVV 94
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
6-47 |
1.72e-04 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 42.72 E-value: 1.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 495054616 6 ASMTVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQAD 47
Cdd:PRK06129 3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAY 44
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
10-106 |
5.51e-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: 40.82 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 10 VIGAGSYGTALAITLARNG---HHVVLWGHDPAHIATLqADRCNVaflpdvpfpdtlHLESDLATALAASRNILVVVPSH 86
Cdd:COG0345 7 FIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEAL-AERYGV------------RVTTDNAEAAAQADVVVLAVKPQ 73
|
90 100
....*....|....*....|
gi 495054616 87 VFGQVLRQIKPLMRPDARVV 106
Cdd:COG0345 74 DLAEVLEELAPLLDPDKLVI 93
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
9-106 |
7.17e-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: 41.06 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 9 TVIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNV------AFLPDVPFPDTLHLESDLATALAASRNILVV 82
Cdd:TIGR03026 4 AVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIyepgldELLAKALKAGRLRATTDYEEAIRDADVIIIC 83
|
90 100 110
....*....|....*....|....*....|....*
gi 495054616 83 VP-----------SHVFgQVLRQIKPLMRPDARVV 106
Cdd:TIGR03026 84 VPtplkedgspdlSYVE-SAAETIAKHLRKGATVV 117
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
7-102 |
9.37e-04 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 40.74 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 7 SMTVIGA-GSYGTALAITLARNGHHVVLWGHDPaHIATLQADRCNVAFLPDvpfpdtlhlesdlATALAASRNILVV-VP 84
Cdd:PRK08655 2 KISIIGGtGGLGKWFARFLKEKGFEVIVTGRDP-KKGKEVAKELGVEYAND-------------NIDAAKDADIVIIsVP 67
|
90
....*....|....*...
gi 495054616 85 SHVFGQVLRQIKPLMRPD 102
Cdd:PRK08655 68 INVTEDVIKEVAPHVKEG 85
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
10-102 |
2.30e-03 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 39.35 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 10 VIGAGSYGTALAITLARNGHHVVLWGHDPAHIATLQADRCNVAflpdvpfpDTLhleSDLATALAASRNILVVVPS-HVF 88
Cdd:PRK09599 5 MIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGA--------DSL---EELVAKLPAPRVVWLMVPAgEIT 73
|
90
....*....|....
gi 495054616 89 GQVLRQIKPLMRPD 102
Cdd:PRK09599 74 DATIDELAPLLSPG 87
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
9-105 |
4.76e-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: 38.18 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495054616 9 TVIGAGSYGTALAITLARNG--HHVVLWGHDPAHIAtlQADRCNVAflpDvpfpdtlHLESDLATALAASRNILVVVPSH 86
Cdd:COG0287 5 AIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLE--RALELGVI---D-------RAATDLEEAVADADLVVLAVPVG 72
|
90
....*....|....*....
gi 495054616 87 VFGQVLRQIKPLMRPDARV 105
Cdd:COG0287 73 ATIEVLAELAPHLKPGAIV 91
|
|
|