|
Name |
Accession |
Description |
Interval |
E-value |
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
4-325 |
2.21e-171 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 478.79 E-value: 2.21e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 4 QQPIAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFVALP 83
Cdd:PRK00094 1 MMKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALADADLILVAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 84 SSALRKVLQPHQAALT-DKLLVSLTKGIEAHTFKLMSEILEEIAPQ-ARIGVISGPNLAREIAEHELTATVVASEDDELC 161
Cdd:PRK00094 81 SQALREVLKQLKPLLPpDAPIVWATKGIEPGTGKLLSEVLEEELPDlAPIAVLSGPSFAKEVARGLPTAVVIASTDEELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 162 ARVQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPMTFLGLAG 241
Cdd:PRK00094 161 ERVQELFHSPYFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEITRLGVALGANPETFLGLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 242 VGDLIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLAQVIQ 321
Cdd:PRK00094 241 LGDLVLTCTSPLSRNRRFGLALGQGKSLEEALAEIGMVAEGVRTAKAVYELAKKLGVEMPITEAVYAVLYEGKDPREAVE 320
|
....
gi 489177971 322 LLMR 325
Cdd:PRK00094 321 DLMG 324
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
7-329 |
9.22e-170 |
|
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: 474.91 E-value: 9.22e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFVALPSSA 86
Cdd:COG0240 3 IAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAGADLVLLAVPSQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 87 LRKVLQPHQAALT-DKLLVSLTKGIEAHTFKLMSEILEEIAPQA-RIGVISGPNLAREIAEHELTATVVASEDDELCARV 164
Cdd:COG0240 83 LREVLEQLAPLLPpGAPVVSATKGIEPGTGLLMSEVIAEELPGAlRIAVLSGPSFAEEVARGLPTAVVVASEDEEVAERL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 165 QAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPMTFLGLAGVGD 244
Cdd:COG0240 163 QELLSTPYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEMTRLGVALGARPETFMGLAGLGD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 245 LIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLAQVIQLLM 324
Cdd:COG0240 243 LVLTCTSDLSRNRRFGLALGKGKSLEEALAEMGMVAEGVYTAKAVYELAEKLGVEMPITEAVYAVLYEGKSPREAVEALM 322
|
....*
gi 489177971 325 RGEPK 329
Cdd:COG0240 323 ARPLK 327
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
6-161 |
2.13e-69 |
|
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: 213.59 E-value: 2.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 6 PIAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFVALPSS 85
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKGADIIVIVVPSQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489177971 86 ALRKVLQPHQAAL-TDKLLVSLTKGIEAHTFKLMSEILEEIAP-QARIGVISGPNLAREIAEHELTATVVASEDDELC 161
Cdd:pfam01210 81 ALREVLKQLKGLLkPDAILVSLSKGIEPGTLKLLSEVIEEELGiQPPIAVLSGPSHAEEVAQGLPTATVIASKDEEAA 158
|
|
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
7-323 |
2.14e-56 |
|
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: 186.78 E-value: 2.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQA--------VRQWMRDPE-----QAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLA 73
Cdd:TIGR03376 2 VAVVGSGNWGTAIAKIVAENARAlpelfeesVRMWVFEEEiegrnLTEIINTTHENVKYLPGIKLPANLVAVPDLVEAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 74 DCQLIFVALPSSALRKVLQPHQAALTDKLL-VSLTKGIE--AHTFKLMSEILEEiAPQARIGVISGPNLAREIAEHELTA 150
Cdd:TIGR03376 82 GADILVFVIPHQFLEGICKQLKGHVKPNARaISCIKGLEvsKDGVKLLSDIIEE-ELGIPCGVLSGANLANEVAKEKFSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 151 TVVA----SEDDELCARVQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFA 226
Cdd:TIGR03376 161 TTVGyrdpADFDVDARVLKALFHRPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEMIKFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 227 VKLG--ANPMTFLGLAGVGDLIVTCSSpkSRNYQVGHALGE-GLSLEEAVSRM--GETAEGVNTLKVLKE--KSDEMQVY 299
Cdd:TIGR03376 241 RMFFptGEVTFTFESCGVADLITTCLG--GRNFKVGRAFAKtGKSLEELEKELlnGQSLQGVATAKEVHEllKNKNKDDE 318
|
330 340
....*....|....*....|....
gi 489177971 300 MPLVAGLHAILFEGRTLAQVIQLL 323
Cdd:TIGR03376 319 FPLFEAVYQILYEGLPPKKLPECL 342
|
|
| NmrA_TMR_like_1_SDR_a |
cd05231 |
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ... |
7-83 |
1.13e-03 |
|
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187542 [Multi-domain] Cd Length: 259 Bit Score: 40.00 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489177971 7 IAVLGG-GSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRrenprylkGVKVHPG-VEPVTDLERTLADCQLIFVALP 83
Cdd:cd05231 1 ILVTGAtGRIGSKVATTLLEAGRPVRALVRSDERAAALAAR--------GAEVVVGdLDDPAVLAAALAGVDAVFFLAP 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
4-325 |
2.21e-171 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 478.79 E-value: 2.21e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 4 QQPIAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFVALP 83
Cdd:PRK00094 1 MMKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALADADLILVAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 84 SSALRKVLQPHQAALT-DKLLVSLTKGIEAHTFKLMSEILEEIAPQ-ARIGVISGPNLAREIAEHELTATVVASEDDELC 161
Cdd:PRK00094 81 SQALREVLKQLKPLLPpDAPIVWATKGIEPGTGKLLSEVLEEELPDlAPIAVLSGPSFAKEVARGLPTAVVIASTDEELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 162 ARVQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPMTFLGLAG 241
Cdd:PRK00094 161 ERVQELFHSPYFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEITRLGVALGANPETFLGLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 242 VGDLIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLAQVIQ 321
Cdd:PRK00094 241 LGDLVLTCTSPLSRNRRFGLALGQGKSLEEALAEIGMVAEGVRTAKAVYELAKKLGVEMPITEAVYAVLYEGKDPREAVE 320
|
....
gi 489177971 322 LLMR 325
Cdd:PRK00094 321 DLMG 324
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
7-329 |
9.22e-170 |
|
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: 474.91 E-value: 9.22e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFVALPSSA 86
Cdd:COG0240 3 IAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAGADLVLLAVPSQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 87 LRKVLQPHQAALT-DKLLVSLTKGIEAHTFKLMSEILEEIAPQA-RIGVISGPNLAREIAEHELTATVVASEDDELCARV 164
Cdd:COG0240 83 LREVLEQLAPLLPpGAPVVSATKGIEPGTGLLMSEVIAEELPGAlRIAVLSGPSFAEEVARGLPTAVVVASEDEEVAERL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 165 QAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPMTFLGLAGVGD 244
Cdd:COG0240 163 QELLSTPYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEMTRLGVALGARPETFMGLAGLGD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 245 LIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLAQVIQLLM 324
Cdd:COG0240 243 LVLTCTSDLSRNRRFGLALGKGKSLEEALAEMGMVAEGVYTAKAVYELAEKLGVEMPITEAVYAVLYEGKSPREAVEALM 322
|
....*
gi 489177971 325 RGEPK 329
Cdd:COG0240 323 ARPLK 327
|
|
| PRK12439 |
PRK12439 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-332 |
8.24e-94 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 171500 [Multi-domain] Cd Length: 341 Bit Score: 282.83 E-value: 8.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 1 MTEQQPIAVLGGGSFGTAIANLLAENGQAVrQWMRDPEQAEAIRTRRENPRYL-KGVKVHPGVEPVTDLERTLADCQLIF 79
Cdd:PRK12439 4 AKREPKVVVLGGGSWGTTVASICARRGPTL-QWVRSAETADDINDNHRNSRYLgNDVVLSDTLRATTDFAEAANCADVVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 80 VALPSSALRKVLqphqAALTDKL-----LVSLTKGIEAHTFKLMSEILEEIAPQARIGVISGPNLAREIAEHELTATVVA 154
Cdd:PRK12439 83 MGVPSHGFRGVL----TELAKELrpwvpVVSLVKGLEQGTNMRMSQIIEEVLPGHPAGILAGPNIAREVAEGYAAAAVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 155 SEDDELCARVQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPM 234
Cdd:PRK12439 159 MPDQHLATRLSPLFRTRRFRVYTTDDVVGVEMAGALKNVFAIAVGMGYSLGIGENTRAMVIARALREMTKLGVAMGGNPE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 235 TFLGLAGVGDLIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGR 314
Cdd:PRK12439 239 TFAGLAGMGDLIVTCTSQRSRNRHVGEQLGAGKPIDEIIASMNQVAEGVKAASVVMEFADEYGLNMPIAREVDAVINHGS 318
|
330
....*....|....*...
gi 489177971 315 TLAQVIQLLMRGEPKTDV 332
Cdd:PRK12439 319 TVEQAYRGLIAEVPGHEV 336
|
|
| PRK14619 |
PRK14619 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-333 |
7.61e-88 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237771 [Multi-domain] Cd Length: 308 Bit Score: 266.47 E-value: 7.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 1 MTEQQPIAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQaeairtrrenprylkgvkvhpgvepvtDLERTLADCQLIFV 80
Cdd:PRK14619 1 TTQPKTIAILGAGAWGSTLAGLASANGHRVRVWSRRSGL---------------------------SLAAVLADADVIVS 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 81 ALPSSALRKVLQPHQA--ALTDKLLVSLTKGIEAHTFKLMSEILEEIAPQARIGVISGPNLAREIAEHELTATVVASEDD 158
Cdd:PRK14619 54 AVSMKGVRPVAEQVQAlnLPPETIIVTATKGLDPETTRTPSQIWQAAFPNHPVVVLSGPNLSKEIQQGLPAATVVASRDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 159 ELCARVQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPMTFLG 238
Cdd:PRK14619 134 AAAETVQQIFSSERFRVYTNSDPLGTELGGTLKNVIAIAAGVCDGLQLGTNAKAALVTRALPEMIRVGTHLGAQTETFYG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 239 LAGVGDLIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLAQ 318
Cdd:PRK14619 214 LSGLGDLLATCTSPLSRNYQVGYGLAQGKSLEQILAELEGTAEGVNTANVLVQLAQQQNIAVPITEQVYRLLQGEITPQQ 293
|
330
....*....|....*
gi 489177971 319 VIQLLMRGEPKTDVD 333
Cdd:PRK14619 294 ALEELMERDLKPEFN 308
|
|
| PRK14618 |
PRK14618 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-331 |
1.92e-84 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237770 [Multi-domain] Cd Length: 328 Bit Score: 258.26 E-value: 1.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 1 MTEQQPIAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFV 80
Cdd:PRK14618 1 MHHGMRVAVLGAGAWGTALAVLAASKGVPVRLWARRPEFAAALAAERENREYLPGVALPAELYPTADPEEALAGADFAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 81 ALPSSALRKVLqphqAALTDKL-LVSLTKGIEAHTFKL--MSEILEEIApQARIGVISGPNLAREIAEHELTATVVASED 157
Cdd:PRK14618 81 AVPSKALRETL----AGLPRALgYVSCAKGLAPDGGRLseLARVLEFLT-QARVAVLSGPNHAEEIARFLPAATVVASPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 158 DELCARVQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPMTFL 237
Cdd:PRK14618 156 PGLARRVQAAFSGPSFRVYTSRDRVGVELGGALKNVIALAAGMVDGLKLGDNAKAALITRGLREMVRFGVALGAEEATFY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 238 GLAGVGDLIVTCSSPKSRNYQVGHALGEGLSLEEAVSRmGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLA 317
Cdd:PRK14618 236 GLSGLGDLIATATSPHSRNRAAGEAIVRGVDREHLEAG-GKVVEGLYTVKALDAWAKAHGHDLPIVEAVARVARGGWDPL 314
|
330
....*....|....
gi 489177971 318 QVIQLLMRGEPKTD 331
Cdd:PRK14618 315 AGLRSLMGREAKEE 328
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
6-161 |
2.13e-69 |
|
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: 213.59 E-value: 2.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 6 PIAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFVALPSS 85
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKGADIIVIVVPSQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489177971 86 ALRKVLQPHQAAL-TDKLLVSLTKGIEAHTFKLMSEILEEIAP-QARIGVISGPNLAREIAEHELTATVVASEDDELC 161
Cdd:pfam01210 81 ALREVLKQLKGLLkPDAILVSLSKGIEPGTLKLLSEVIEEELGiQPPIAVLSGPSHAEEVAQGLPTATVIASKDEEAA 158
|
|
| NAD_Gly3P_dh_C |
pfam07479 |
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent ... |
180-321 |
2.07e-68 |
|
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: 210.71 E-value: 2.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 180 DRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFAVKLGANPMTFLGLAGVGDLIVTCSSPKSRNYQV 259
Cdd:pfam07479 1 DVIGVELGGALKNVIAIAAGIADGLGLGDNAKAALITRGLAEMIRLGKALGAKPETFFGLAGLGDLIVTCTSGLSRNRRF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489177971 260 GHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLAQVIQ 321
Cdd:pfam07479 81 GEALGKGKSLEEAEKELGQVAEGVYTAKAVYELAKKLGVEMPIFEAVYRILYEGKSPEEALE 142
|
|
| PRK14620 |
PRK14620 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
7-324 |
1.44e-63 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173083 [Multi-domain] Cd Length: 326 Bit Score: 204.68 E-value: 1.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLAD-CQLIFVALPSS 85
Cdd:PRK14620 3 ISILGAGSFGTAIAIALSSKKISVNLWGRNHTTFESINTKRKNLKYLPTCHLPDNISVKSAIDEVLSDnATCIILAVPTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 86 ALRKV-LQPHQAALTDKLLVSL-TKGIEAHTFKLMSEILEEIAPQARIGVISGPNLAREIAEHELTATVVASEDDELCAR 163
Cdd:PRK14620 83 QLRTIcQQLQDCHLKKNTPILIcSKGIEKSSLKFPSEIVNEILPNNPIAILSGPSFAKEIAEKLPCSIVLAGQNETLGSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 164 VQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEM-TRFAVKLGA-NPMTFLGLAG 241
Cdd:PRK14620 163 LISKLSNENLKIIYSQDIIGVQIGAALKNIIAIACGIVLGKNLGNNAHAAVITKGMNEIkTLYSAKNGSiDLNTLIGPSC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 242 VGDLIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMGETAEGVNTLKVLKEKSDEMQVYMPLVAGLHAILFEGRTLAQVIQ 321
Cdd:PRK14620 243 LGDLILTCTTLHSRNMSFGFKIGNGFNINQILSEGKSVIEGFSTVKPLISLAKKLNIELPICESIYNLLYENISLEKTIS 322
|
...
gi 489177971 322 LLM 324
Cdd:PRK14620 323 VIL 325
|
|
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
7-323 |
2.14e-56 |
|
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: 186.78 E-value: 2.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQA--------VRQWMRDPE-----QAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLA 73
Cdd:TIGR03376 2 VAVVGSGNWGTAIAKIVAENARAlpelfeesVRMWVFEEEiegrnLTEIINTTHENVKYLPGIKLPANLVAVPDLVEAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 74 DCQLIFVALPSSALRKVLQPHQAALTDKLL-VSLTKGIE--AHTFKLMSEILEEiAPQARIGVISGPNLAREIAEHELTA 150
Cdd:TIGR03376 82 GADILVFVIPHQFLEGICKQLKGHVKPNARaISCIKGLEvsKDGVKLLSDIIEE-ELGIPCGVLSGANLANEVAKEKFSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 151 TVVA----SEDDELCARVQAALHGRTFRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFA 226
Cdd:TIGR03376 161 TTVGyrdpADFDVDARVLKALFHRPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEMIKFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 227 VKLG--ANPMTFLGLAGVGDLIVTCSSpkSRNYQVGHALGE-GLSLEEAVSRM--GETAEGVNTLKVLKE--KSDEMQVY 299
Cdd:TIGR03376 241 RMFFptGEVTFTFESCGVADLITTCLG--GRNFKVGRAFAKtGKSLEELEKELlnGQSLQGVATAKEVHEllKNKNKDDE 318
|
330 340
....*....|....*....|....
gi 489177971 300 MPLVAGLHAILFEGRTLAQVIQLL 323
Cdd:TIGR03376 319 FPLFEAVYQILYEGLPPKKLPECL 342
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
7-327 |
1.70e-40 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 145.55 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQ-------AVRQWMRDPE-----QAEAIRTRRENPRYLKGVKVHPGVEPVTDLERTLAD 74
Cdd:PTZ00345 14 VSVIGSGNWGSAISKVVGENTQrnyifhnEVRMWVLEEIvegekLSDIINTKHENVKYLPGIKLPDNIVAVSDLKEAVED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 75 CQL-IFVaLPSSALRKVL-QPHQAALTDK--LLVSLTKGIEAHTFK--LMSEILEEiAPQARIGVISGPNLAREIAEHEL 148
Cdd:PTZ00345 94 ADLlIFV-IPHQFLESVLsQIKENNNLKKhaRAISLTKGIIVENGKpvLCSDVIEE-ELGIPCCALSGANVANDVAREEF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 149 T-ATVVASEDDElcARVQAALHGRT-FRVYASRDRFGVELGGALKNVYAIMAGLAAAMDMGENTRSMLITRALAEMTRFA 226
Cdd:PTZ00345 172 SeATIGCEDKDD--ALIWQRLFDRPyFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMKLFG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 227 VKLGANPM--TFLGLAGVGDLIVTCSSpkSRNYQVGH--ALGEGL-SLEEAVSRM--GETAEGVNTLKVLKE--KSDEMQ 297
Cdd:PTZ00345 250 KIFFPNVMdeTFFESCGLADLITTCLG--GRNVRCAAefAKRNGKkSWEEIEAELlnGQKLQGTVTLKEVYEvlESHDLK 327
|
330 340 350
....*....|....*....|....*....|
gi 489177971 298 VYMPLVAGLHAILFEGRTLAQVIQLLMRGE 327
Cdd:PTZ00345 328 KEFPLFTVTYKIAFEGADPSSLIDVLSTNE 357
|
|
| GPD_NAD_C_bact |
pfam20618 |
Bacterial GPD, NAD-dependent C-terminal; This is the C-terminal domain of NAD-dependent ... |
240-303 |
3.20e-16 |
|
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: 72.14 E-value: 3.20e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489177971 240 AGVGDLIVTCSSPKSRNYQVGHALGEGLSLEEAVSRMgeTAEGVNTLK-VLKEKSDEMQVYMPLV 303
Cdd:pfam20618 1 AGLGDLVLTCTSDLSRNRTFGLLLGKGMTLAEAGNGQ--VAEGVRTAKaVAAILARAHNVEMPIL 63
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
8-109 |
9.13e-06 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 43.76 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 8 AVLGGGSFGTAIANLLAENG--QAVRQWMRDPEQAEAIRTRrenprylkgvkVHPGVEPVTDLErTLADCQLIFVALPSS 85
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAGphEVVVANSRNPEKAEELAEE-----------YGVGATAVDNEE-AAEEADVVFLAVKPE 68
|
90 100
....*....|....*....|....
gi 489177971 86 ALRKVLQPHQAALTDKLLVSLTKG 109
Cdd:pfam03807 69 DAPDVLSELSDLLKGKIVISIAAG 92
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
7-131 |
1.05e-05 |
|
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: 46.21 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENG---QAVRQWMRDPEQAEAIRTRrenprylkgvkvhPGVEPVTDLERTLADCQLIFVALP 83
Cdd:COG0345 5 IGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAER-------------YGVRVTTDNAEAAAQADVVVLAVK 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489177971 84 SSALRKVLQPHQAALT-DKLLVSLTKGIeahTFKLMSEILEEIAPQARI 131
Cdd:COG0345 72 PQDLAEVLEELAPLLDpDKLVISIAAGV---TLATLEEALGGGAPVVRA 117
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
7-135 |
4.40e-05 |
|
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: 42.99 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAeAIRT---RRENPRylkGVKVHPgVEPVTDLERTLADCQLIFVALP 83
Cdd:pfam02558 1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA-AIKKnglRLTSPG---GERIVP-PPAVTSASESLGPIDLVIVTVK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489177971 84 SSALRKVLQPHQAALTDK-LLVSLTKGIEAHtfklmsEILEEIAPQARI--GVIS 135
Cdd:pfam02558 76 AYQTEEALEDIAPLLGPNtVVLLLQNGLGHE------EVLREAVPRERVlgGVTT 124
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
7-180 |
5.26e-05 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 44.46 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRRENpryLKGVKVHPGVEPVTDLERtLADCQLIFVALPSSA 86
Cdd:PRK06522 3 IAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLR---LEDGEITVPVLAADDPAE-LGPQDLVILAVKAYQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 87 LRKVLQPHQAALT-DKLLVSLTKGIEAHtfklmsEILEEIAPQARI--GV------ISGPNLAREIAEHELTATVVASED 157
Cdd:PRK06522 79 LPAALPSLAPLLGpDTPVLFLQNGVGHL------EELAAYIGPERVlgGVvthaaeLEGPGVVRHTGGGRLKIGEPDGES 152
|
170 180
....*....|....*....|...
gi 489177971 158 DElCARVQAALHGRTFRVYASRD 180
Cdd:PRK06522 153 AA-AEALADLLNAAGLDVEWSPD 174
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
7-131 |
7.26e-05 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 43.99 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 7 IAVLGGGSFGTAIANLLAENGQAvrqwmrDPEQAeAIRTRRENPRYLKGVKVHPGVEPVTDLERTLADCQLIFVALPSSA 86
Cdd:PRK06928 4 IGFIGYGSMADMIATKLLETEVA------TPEEI-ILYSSSKNEHFNQLYDKYPTVELADNEAEIFTKCDHSFICVPPLA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489177971 87 LRKVLQPHQAALT-DKLLVSLTKGIEahtfklMSEILeEIAPQARI 131
Cdd:PRK06928 77 VLPLLKDCAPVLTpDRHVVSIAAGVS------LDDLL-EITPGLQV 115
|
|
| NmrA_TMR_like_1_SDR_a |
cd05231 |
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ... |
7-83 |
1.13e-03 |
|
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187542 [Multi-domain] Cd Length: 259 Bit Score: 40.00 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489177971 7 IAVLGG-GSFGTAIANLLAENGQAVRQWMRDPEQAEAIRTRrenprylkGVKVHPG-VEPVTDLERTLADCQLIFVALP 83
Cdd:cd05231 1 ILVTGAtGRIGSKVATTLLEAGRPVRALVRSDERAAALAAR--------GAEVVVGdLDDPAVLAAALAGVDAVFFLAP 71
|
|
| PRK13302 |
PRK13302 |
aspartate dehydrogenase; |
3-105 |
6.66e-03 |
|
aspartate dehydrogenase;
Pssm-ID: 237341 [Multi-domain] Cd Length: 271 Bit Score: 37.91 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489177971 3 EQQPIAVLGGGSFGTAIANLLAENGQAVRQ---WMRDPEQAEAirtrrenprYLKGVKVHPgvePVTDLERTLADCQLIF 79
Cdd:PRK13302 5 PELRVAIAGLGAIGKAIAQALDRGLPGLTLsavAVRDPQRHAD---------FIWGLRRPP---PVVPLDQLATHADIVV 72
|
90 100
....*....|....*....|....*.
gi 489177971 80 VALPSSALRKVLQPHQAALTDKLLVS 105
Cdd:PRK13302 73 EAAPASVLRAIVEPVLAAGKKAIVLS 98
|
|
| |
