|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-254 |
3.15e-160 |
|
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: 444.47 E-value: 3.15e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHN-DAILAPLVEAGVTLLPNTSGAKTAEEAI 79
Cdd:COG2022 5 PLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGgDNLLDYLDPLGVTLLPNTAGCRTAEEAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 80 FAAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQ 159
Cdd:COG2022 85 RTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGSGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 160 GLETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKS 239
Cdd:COG2022 165 GLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKR 244
|
250
....*....|....*
gi 1100259256 240 SQASPTSPLTGFLEA 254
Cdd:COG2022 245 DYASASSPLTGFLHQ 259
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
1-250 |
7.20e-159 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 440.65 E-value: 7.20e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLVEAGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 81 AAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQG 160
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 161 LETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKSS 240
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
250
....*....|
gi 1100259256 241 QASPTSPLTG 250
Cdd:PRK00208 241 YASASSPLTG 250
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
2-248 |
1.34e-139 |
|
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: 391.85 E-value: 1.34e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDL-RQHNDAILAPLVEAGVTLLPNTSGAKTAEEAIF 80
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 81 AAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQG 160
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 161 LETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKSS 240
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*...
gi 1100259256 241 QASPTSPL 248
Cdd:cd04728 241 YASASSPL 248
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
3-247 |
1.04e-137 |
|
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: 386.99 E-value: 1.04e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 3 RIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQ--HNDAILAPLVEAGVTLLPNTSGAKTAEEAIF 80
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAkpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 81 AAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQG 160
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 161 LETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKSS 240
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 1100259256 241 QASPTSP 247
Cdd:pfam05690 241 YASASSP 247
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
110-211 |
2.80e-03 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 38.12 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 110 IETLKAAEALVKKG--FVVLPYCGaDPV-LCKRLEEVGCSAVMPLGAPIGSNQGLETKAMLEIIIQQATVPVVVDAGIGV 186
Cdd:TIGR00735 7 IPCLDVRDGRVVKGvqFLNLRDAG-DPVeLAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGGIKS 85
|
90 100
....*....|....*....|....*
gi 1100259256 187 PSHATQALEMGADAVLVNTAiAVAD 211
Cdd:TIGR00735 86 IEDVDKLLRAGADKVSINTA-AVKN 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-254 |
3.15e-160 |
|
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: 444.47 E-value: 3.15e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHN-DAILAPLVEAGVTLLPNTSGAKTAEEAI 79
Cdd:COG2022 5 PLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGgDNLLDYLDPLGVTLLPNTAGCRTAEEAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 80 FAAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQ 159
Cdd:COG2022 85 RTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGSGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 160 GLETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKS 239
Cdd:COG2022 165 GLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKR 244
|
250
....*....|....*
gi 1100259256 240 SQASPTSPLTGFLEA 254
Cdd:COG2022 245 DYASASSPLTGFLHQ 259
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
1-250 |
7.20e-159 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 440.65 E-value: 7.20e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLVEAGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 81 AAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQG 160
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 161 LETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKSS 240
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
250
....*....|
gi 1100259256 241 QASPTSPLTG 250
Cdd:PRK00208 241 YASASSPLTG 250
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
2-248 |
1.34e-139 |
|
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: 391.85 E-value: 1.34e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDL-RQHNDAILAPLVEAGVTLLPNTSGAKTAEEAIF 80
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 81 AAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQG 160
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 161 LETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKSS 240
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*...
gi 1100259256 241 QASPTSPL 248
Cdd:cd04728 241 YASASSPL 248
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
3-247 |
1.04e-137 |
|
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: 386.99 E-value: 1.04e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 3 RIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQ--HNDAILAPLVEAGVTLLPNTSGAKTAEEAIF 80
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAkpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 81 AAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQG 160
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 161 LETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKSS 240
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 1100259256 241 QASPTSP 247
Cdd:pfam05690 241 YASASSP 247
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
2-252 |
7.28e-103 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 299.70 E-value: 7.28e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHND--AILAPLVEAGVTLLPNTSGAKTAEEAI 79
Cdd:CHL00162 8 LKIGNKSFNSRLMLGTGKYKSLKDAIQSIEASGCEIVTVAIRRLNNNLLNDnsNLLNGLDWNKLWLLPNTAGCQTAEEAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 80 FAAQLARE---ALG---TNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGA 153
Cdd:CHL00162 88 RMAFLGRElakQLGqedNNFVKLEVISDPKYLLPDPIGTLKAAEFLVKKGFTVLPYINADPMLAKHLEDIGCATVMPLGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 154 PIGSNQGLETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQA 233
Cdd:CHL00162 168 PIGSGQGLQNLLNLQIIIENAKIPVIIDAGIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAVQAGRLAYLA 247
|
250
....*....|....*....
gi 1100259256 234 VPGSKSSQASPTSPLTGFL 252
Cdd:CHL00162 248 GRMPKKKYAQASSPIEGIS 266
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
2-250 |
3.96e-94 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 279.71 E-value: 3.96e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLVE-AGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK11840 75 WTVAGKTFSSRLLVGTGKYKDFEETAAAVEASGAEIVTVAVRRVNVSDPGAPMLTDYIDpKKYTYLPNTAGCYTAEEAVR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 81 AAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRLEEVGCSAVMPLGAPIGSNQG 160
Cdd:PRK11840 155 TLRLAREAGGWDLVKLEVLGDAKTLYPDMVETLKATEILVKEGFQVMVYCSDDPIAAKRLEDAGAVAVMPLGAPIGSGLG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 161 LETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADSPVMMATAFRLAVEAGLLARQAVPGSKSS 240
Cdd:PRK11840 235 IQNPYTIRLIVEGATVPVLVDAGVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLAYLAGRMPRRR 314
|
250
....*....|
gi 1100259256 241 QASPTSPLTG 250
Cdd:PRK11840 315 YADPSSPLAG 324
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
26-205 |
2.06e-06 |
|
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: 47.20 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 26 MVEAIRASGSQLV---TLAMKRVDLRQHNDAILAPLV-EAGVTLLPNTSGAKTAEEAIFAAQLAREAlGTNWLKL-EIHP 100
Cdd:cd04722 17 LAKAAAEAGADAIivgTRSSDPEEAETDDKEVLKEVAaETDLPLGVQLAINDAAAAVDIAAAAARAA-GADGVEIhGAVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 101 DARWLLPDPIETLKAAEALVKKGFVVLPYCGADPVLCKRL--EEVGCSAVMPLGAPIGSNqgLETKAMLEIIIQQATVPV 178
Cdd:cd04722 96 YLAREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAgvDEVGLGNGGGGGGGRDAV--PIADLLLILAKRGSKVPV 173
|
170 180
....*....|....*....|....*..
gi 1100259256 179 VVDAGIGVPSHATQALEMGADAVLVNT 205
Cdd:cd04722 174 IAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
165-207 |
4.89e-05 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 43.33 E-value: 4.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1100259256 165 AMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAI 207
Cdd:cd04729 167 ELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
165-207 |
2.54e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 40.90 E-value: 2.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1100259256 165 AMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAI 207
Cdd:PRK01130 163 ALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
27-207 |
2.41e-03 |
|
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: 38.41 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 27 VEAIRASGSQLVTLAM--KRVDLRQHNDAI--LAPLVEAGVTLLPNTSGAKTAEEAifaaqLAREA----LGTNWLKLEI 98
Cdd:cd04723 41 ARAYKELGFRGLYIADldAIMGRGDNDEAIreLAAAWPLGLWVDGGIRSLENAQEW-----LKRGAsrviVGTETLPSDD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 99 hpdarwlLPDPIETLKAAEALV----KKGFVVLPYCGADPV-----LCKRLEEVgcsAVMPLGApIGSNQGLETkAMLEI 169
Cdd:cd04723 116 -------DEDRLAALGEQRLVLsldfRGGQLLKPTDFIGPEellrrLAKWPEEL---IVLDIDR-VGSGQGPDL-ELLER 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1100259256 170 IIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAI 207
Cdd:cd04723 184 LAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
110-211 |
2.80e-03 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 38.12 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 110 IETLKAAEALVKKG--FVVLPYCGaDPV-LCKRLEEVGCSAVMPLGAPIGSNQGLETKAMLEIIIQQATVPVVVDAGIGV 186
Cdd:TIGR00735 7 IPCLDVRDGRVVKGvqFLNLRDAG-DPVeLAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGGIKS 85
|
90 100
....*....|....*....|....*
gi 1100259256 187 PSHATQALEMGADAVLVNTAiAVAD 211
Cdd:TIGR00735 86 IEDVDKLLRAGADKVSINTA-AVKN 109
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
121-212 |
3.80e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 37.46 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259256 121 KKG--FVVLPYCGaDPV-LCKRLEEVGCSAVMPL---GAPIGSNQGLEtkaMLEIIIQQATVPVVVDAGIGVPSHATQAL 194
Cdd:pfam00977 17 VKGdyFQNTVYAG-DPVeLAKRYEEEGADELHFVdldAAKEGRPVNLD---VVEEIAEEVFIPVQVGGGIRSLEDVERLL 92
|
90
....*....|....*...
gi 1100259256 195 EMGADAVLVNTAiAVADS 212
Cdd:pfam00977 93 SAGADRVIIGTA-AVKNP 109
|
|
| |
