|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-254 |
1.55e-148 |
|
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441625 Cd Length: 259 Bit Score: 414.81 E-value: 1.55e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 1 MSLTPLTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGTP----IFPLLQKLNIAPLPNTAGCRTA 76
Cdd:COG2022 1 MMDDPLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPggdnLLDYLDPLGVTLLPNTAGCRTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 77 ADAVMTAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPI 156
Cdd:COG2022 81 EEAVRTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 157 GTGLGILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGR 236
Cdd:COG2022 161 GSGLGLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGR 240
|
250
....*....|....*...
gi 491652295 237 IPVREHAKASSPSEGFVS 254
Cdd:COG2022 241 MPKRDYASASSPLTGFLH 258
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
5-251 |
9.09e-145 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 405.21 E-value: 9.09e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 5 PLTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGTP---IFPLLQKLNIAPLPNTAGCRTAADAVM 81
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGgdnLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 82 TAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPIGTGLG 161
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 162 ILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGRIPVRE 241
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
250
....*....|
gi 491652295 242 HAKASSPSEG 251
Cdd:PRK00208 241 YASASSPLTG 250
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
6-248 |
7.72e-128 |
|
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).
Pssm-ID: 240079 Cd Length: 248 Bit Score: 362.19 E-value: 7.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 6 LTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRR----HAAGTPIFPLLQKLNIAPLPNTAGCRTAADAVM 81
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRvnigDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 82 TAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPIGTGLG 161
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 162 ILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGRIPVRE 241
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*..
gi 491652295 242 HAKASSP 248
Cdd:cd04728 241 YASASSP 247
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
7-248 |
1.70e-126 |
|
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.
Pssm-ID: 428589 Cd Length: 247 Bit Score: 358.87 E-value: 1.70e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 7 TIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGTP-----IFPLLQKLNIAPLPNTAGCRTAADAVM 81
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAKpggdnILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 82 TAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPIGTGLG 161
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 162 ILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGRIPVRE 241
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 491652295 242 HAKASSP 248
Cdd:pfam05690 241 YASASSP 247
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-254 |
1.55e-148 |
|
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441625 Cd Length: 259 Bit Score: 414.81 E-value: 1.55e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 1 MSLTPLTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGTP----IFPLLQKLNIAPLPNTAGCRTA 76
Cdd:COG2022 1 MMDDPLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPggdnLLDYLDPLGVTLLPNTAGCRTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 77 ADAVMTAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPI 156
Cdd:COG2022 81 EEAVRTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 157 GTGLGILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGR 236
Cdd:COG2022 161 GSGLGLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGR 240
|
250
....*....|....*...
gi 491652295 237 IPVREHAKASSPSEGFVS 254
Cdd:COG2022 241 MPKRDYASASSPLTGFLH 258
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
5-251 |
9.09e-145 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 405.21 E-value: 9.09e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 5 PLTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGTP---IFPLLQKLNIAPLPNTAGCRTAADAVM 81
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGgdnLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 82 TAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPIGTGLG 161
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 162 ILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGRIPVRE 241
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
250
....*....|
gi 491652295 242 HAKASSPSEG 251
Cdd:PRK00208 241 YASASSPLTG 250
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
6-248 |
7.72e-128 |
|
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).
Pssm-ID: 240079 Cd Length: 248 Bit Score: 362.19 E-value: 7.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 6 LTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRR----HAAGTPIFPLLQKLNIAPLPNTAGCRTAADAVM 81
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRvnigDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 82 TAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPIGTGLG 161
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 162 ILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGRIPVRE 241
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*..
gi 491652295 242 HAKASSP 248
Cdd:cd04728 241 YASASSP 247
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
7-248 |
1.70e-126 |
|
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.
Pssm-ID: 428589 Cd Length: 247 Bit Score: 358.87 E-value: 1.70e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 7 TIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGTP-----IFPLLQKLNIAPLPNTAGCRTAADAVM 81
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAKpggdnILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 82 TAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPIGTGLG 161
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 162 ILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGRIPVRE 241
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 491652295 242 HAKASSP 248
Cdd:pfam05690 241 YASASSP 247
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
4-251 |
2.36e-102 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 300.51 E-value: 2.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 4 TPLTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGTPIFPLLQKLnIAP-----LPNTAGCRTAAD 78
Cdd:PRK11840 73 DSWTVAGKTFSSRLLVGTGKYKDFEETAAAVEASGAEIVTVAVRRVNVSDPGAPMLTDY-IDPkkytyLPNTAGCYTAEE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 79 AVMTAMLAREALGTSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPIGT 158
Cdd:PRK11840 152 AVRTLRLAREAGGWDLVKLEVLGDAKTLYPDMVETLKATEILVKEGFQVMVYCSDDPIAAKRLEDAGAVAVMPLGAPIGS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 159 GLGILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALAREAGRIP 238
Cdd:PRK11840 232 GLGIQNPYTIRLIVEGATVPVLVDAGVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLAYLAGRMP 311
|
250
....*....|...
gi 491652295 239 VREHAKASSPSEG 251
Cdd:PRK11840 312 RRRYADPSSPLAG 324
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
5-252 |
2.29e-86 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 257.71 E-value: 2.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 5 PLTIGDRTFTSRLIMGSGGATSMDLLEQALIASGTEMTTVAMRRHAAGT--PIFPLLQKLN---IAPLPNTAGCRTAADA 79
Cdd:CHL00162 7 KLKIGNKSFNSRLMLGTGKYKSLKDAIQSIEASGCEIVTVAIRRLNNNLlnDNSNLLNGLDwnkLWLLPNTAGCQTAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 80 VMTAMLARE---ALG---TSWVKVEIIHDEDTLLPDTVELLNACEQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLG 153
Cdd:CHL00162 87 IRMAFLGRElakQLGqedNNFVKLEVISDPKYLLPDPIGTLKAAEFLVKKGFTVLPYINADPMLAKHLEDIGCATVMPLG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 154 APIGTGLGILNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAVQAGALARE 233
Cdd:CHL00162 167 SPIGSGQGLQNLLNLQIIIENAKIPVIIDAGIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAVQAGRLAYL 246
|
250
....*....|....*....
gi 491652295 234 AGRIPVREHAKASSPSEGF 252
Cdd:CHL00162 247 AGRMPKKKYAQASSPIEGI 265
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
76-206 |
1.11e-08 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 53.74 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 76 AADAVMTAMLAREALGTSWVkveIIHDEDTLLPDtvELLNACEQL--VAEDFTVLAYTSDDPV-AAARLEDAGVAAVMPL 152
Cdd:cd04722 69 AAAAVDIAAAAARAAGADGV---EIHGAVGYLAR--EDLELIRELreAVPDVKVVVKLSPTGElAAAAAEEAGVDEVGLG 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491652295 153 GAPIGTGLGILNPHNIEL---IASRAQVPVVLDAGVGTASDAALAMELGCDAVLLAS 206
Cdd:cd04722 144 NGGGGGGGRDAVPIADLLlilAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
168-225 |
1.51e-07 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 51.09 E-value: 1.51e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 168 IELIASRAQVPVVLDA--GVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMKFAV 225
Cdd:cd04727 186 VKETAKLGRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARAIVEAV 245
|
|
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
168-227 |
8.31e-07 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 48.98 E-value: 8.31e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491652295 168 IELIASRAQVPVVLDA--GVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMkfaVQA 227
Cdd:PRK04180 195 VKEVAELGRLPVVNFAagGIATPADAALMMQLGADGVFVGSGIFKSGDPEKRARAI---VEA 253
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
101-216 |
6.38e-06 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 46.01 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 101 HDEDTLLPDTVE-LLNACEQLvaeDFTVLAYTSDDPV--AAARLEDAGVAAVMPlgAPIGTGLGI--LNPHNIELIASRA 175
Cdd:PRK04302 93 HSERRLTLADIEaVVERAKKL---GLESVVCVNNPETsaAAAALGPDYVAVEPP--ELIGTGIPVskAKPEVVEDAVEAV 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 491652295 176 Q-----VPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVA 216
Cdd:PRK04302 168 KkvnpdVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEA 213
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
149-216 |
6.36e-05 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 43.03 E-value: 6.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491652295 149 VMPLGApIGTGLGIlNPHNIELIASRAQVPVVLDAGVGTASDAALAMELGCDAVLLASAVNRAEDPVA 216
Cdd:cd04723 164 VLDIDR-VGSGQGP-DLELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLTLE 229
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| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
136-204 |
2.48e-03 |
|
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.
Pssm-ID: 239238 [Multi-domain] Cd Length: 344 Bit Score: 38.73 E-value: 2.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491652295 136 VAAARLEDAGVAAVMPLGAPIGTGLGI---LNPHNIELIASRAQVPVVLDaGVGTASDAALAMELGCDAVLL 204
Cdd:cd02922 170 EAVSDGPAGKKTKAKGGGAGRAMSGFIdptLTWDDIKWLRKHTKLPIVLK-GVQTVEDAVLAAEYGVDGIVL 240
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| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
162-222 |
8.12e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 36.34 E-value: 8.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491652295 162 ILNPHNIELIASRAQVPVVLDAGVgTASDAALAMELGCDAVLLASAVNRAEDPVAMAQAMK 222
Cdd:cd00564 136 PLGLELLREIAELVEIPVVAIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
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| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
118-239 |
9.34e-03 |
|
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240088 [Multi-domain] Cd Length: 351 Bit Score: 37.04 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 118 EQLVAEDFTVLAYTSDDPVAAARLEDAGVAAVMPLGAPI--------GTGLGI----------LNPHNIELIASRAQVPV 179
Cdd:cd04737 145 DRAKAAGAKAIILTADATVGGNREADIRNKFQFPFGMPNlnhfsegtGKGKGIseiyaaakqkLSPADIEFIAKISGLPV 224
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491652295 180 VLDaGVGTASDAALAMELGCDAVLLASAVNRAEDPVAMAqamkFAVQAGALAREAGRIPV 239
Cdd:cd04737 225 IVK-GIQSPEDADVAINAGADGIWVSNHGGRQLDGGPAS----FDSLPEIAEAVNHRVPI 279
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