|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-254 |
1.09e-162 |
|
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: 450.64 E-value: 1.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHN-DAILEPLIAAGVTLLPNTSGAKTAEEAI 79
Cdd:COG2022 5 PLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGgDNLLDYLDPLGVTLLPNTAGCRTAEEAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 80 FAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQ 159
Cdd:COG2022 85 RTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGSGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 160 GLETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRS 239
Cdd:COG2022 165 GLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKR 244
|
250
....*....|....*
gi 446866837 240 HFAHATSPLTGFLEA 254
Cdd:COG2022 245 DYASASSPLTGFLHQ 259
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
1-250 |
8.49e-162 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 447.97 E-value: 8.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 161 LETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
250
....*....|
gi 446866837 241 FAHATSPLTG 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 |
3.54e-145 |
|
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: 406.10 E-value: 3.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDL-RQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 161 LETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*...
gi 446866837 241 FAHATSPL 248
Cdd:cd04728 241 YASASSPL 248
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
3-247 |
1.60e-143 |
|
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: 402.01 E-value: 1.60e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 3 RIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQ--HNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAkpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 161 LETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 446866837 241 FAHATSP 247
Cdd:pfam05690 241 YASASSP 247
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
124-211 |
9.67e-03 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 36.58 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 124 FVVLPYCGaDPV-LCKRLEEVGCAAVMPLGApIGSNQGLETcaMLEIIIQQAT---VPVVVDAGIGVPSHAAQALEMGAD 199
Cdd:TIGR00735 23 FLNLRDAG-DPVeLAQRYDEEGADELVFLDI-TASSEGRTT--MIDVVERTAEtvfIPLTVGGGIKSIEDVDKLLRAGAD 98
|
90
....*....|..
gi 446866837 200 AVLVNTAiAVAD 211
Cdd:TIGR00735 99 KVSINTA-AVKN 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-254 |
1.09e-162 |
|
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: 450.64 E-value: 1.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHN-DAILEPLIAAGVTLLPNTSGAKTAEEAI 79
Cdd:COG2022 5 PLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGgDNLLDYLDPLGVTLLPNTAGCRTAEEAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 80 FAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQ 159
Cdd:COG2022 85 RTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGSGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 160 GLETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRS 239
Cdd:COG2022 165 GLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKR 244
|
250
....*....|....*
gi 446866837 240 HFAHATSPLTGFLEA 254
Cdd:COG2022 245 DYASASSPLTGFLHQ 259
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
1-250 |
8.49e-162 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 447.97 E-value: 8.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 161 LETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
250
....*....|
gi 446866837 241 FAHATSPLTG 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 |
3.54e-145 |
|
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: 406.10 E-value: 3.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDL-RQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 161 LETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*...
gi 446866837 241 FAHATSPL 248
Cdd:cd04728 241 YASASSPL 248
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
3-247 |
1.60e-143 |
|
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: 402.01 E-value: 1.60e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 3 RIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQ--HNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAkpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 161 LETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 446866837 241 FAHATSP 247
Cdd:pfam05690 241 YASASSP 247
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
2-252 |
1.34e-106 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 309.33 E-value: 1.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHND--AILEPLIAAGVTLLPNTSGAKTAEEAI 79
Cdd:CHL00162 8 LKIGNKSFNSRLMLGTGKYKSLKDAIQSIEASGCEIVTVAIRRLNNNLLNDnsNLLNGLDWNKLWLLPNTAGCQTAEEAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 80 FAAHLARE---ALG---TNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGA 153
Cdd:CHL00162 88 RMAFLGRElakQLGqedNNFVKLEVISDPKYLLPDPIGTLKAAEFLVKKGFTVLPYINADPMLAKHLEDIGCATVMPLGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 154 PIGSNQGLETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQS 233
Cdd:CHL00162 168 PIGSGQGLQNLLNLQIIIENAKIPVIIDAGIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAVQAGRLAYLA 247
|
250
....*....|....*....
gi 446866837 234 GPGSRSHFAHATSPLTGFL 252
Cdd:CHL00162 248 GRMPKKKYAQASSPIEGIS 266
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
2-250 |
2.07e-95 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 282.79 E-value: 2.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIA-AGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK11840 75 WTVAGKTFSSRLLVGTGKYKDFEETAAAVEASGAEIVTVAVRRVNVSDPGAPMLTDYIDpKKYTYLPNTAGCYTAEEAVR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:PRK11840 155 TLRLAREAGGWDLVKLEVLGDAKTLYPDMVETLKATEILVKEGFQVMVYCSDDPIAAKRLEDAGAVAVMPLGAPIGSGLG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 161 LETCAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:PRK11840 235 IQNPYTIRLIVEGATVPVLVDAGVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLAYLAGRMPRRR 314
|
250
....*....|
gi 446866837 241 FAHATSPLTG 250
Cdd:PRK11840 315 YADPSSPLAG 324
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
165-207 |
7.39e-06 |
|
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: 45.64 E-value: 7.39e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446866837 165 AMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAI 207
Cdd:cd04729 167 ELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
26-205 |
2.67e-05 |
|
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: 43.73 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 26 MVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIAA----GVTLLPNTSGAKTAEEAIFAAHLAREAlGTNWLKL-EIHP 100
Cdd:cd04722 17 LAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVaaetDLPLGVQLAINDAAAAVDIAAAAARAA-GADGVEIhGAVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 101 DARWLLPDPIETLKAAEMLVQQGFVVLPYCGADPVLCKRL--EEVGCAAVMPLGAPIGSNqgLETCAMLEIIIQQATVPV 178
Cdd:cd04722 96 YLAREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAgvDEVGLGNGGGGGGGRDAV--PIADLLLILAKRGSKVPV 173
|
170 180
....*....|....*....|....*..
gi 446866837 179 VVDAGIGVPSHAAQALEMGADAVLVNT 205
Cdd:cd04722 174 IAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
154-224 |
2.88e-05 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 43.86 E-value: 2.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446866837 154 PIGSNQGLETCAMLEI--IIQQATVPVVVDAGIgVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAV 224
Cdd:PRK07695 126 PTDCKKGVPARGLEELsdIARALSIPVIAIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESI 197
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
164-207 |
3.19e-05 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 43.60 E-value: 3.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446866837 164 CAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAI 207
Cdd:PRK01130 162 FALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
159-221 |
1.24e-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: 38.65 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446866837 159 QGLEtcaMLEIIIQQATVPVVVDAGIGvPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFR 221
Cdd:cd00564 137 LGLE---LLREIAELVEIPVVAIGGIT-PENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
177-224 |
1.60e-03 |
|
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: 39.15 E-value: 1.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446866837 177 PVVVDA--GIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAV 224
Cdd:cd04727 196 PVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARAIVEAV 245
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
148-207 |
2.32e-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: 2.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 148 VMPLGApIGSNQGLETcAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAI 207
Cdd:cd04723 164 VLDIDR-VGSGQGPDL-ELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
159-227 |
2.45e-03 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 37.86 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446866837 159 QGLEtcaMLEIIIQQATVPVVVDAGIGvPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAG 227
Cdd:COG0352 142 LGLE---GLAWWAELVEIPVVAIGGIT-PENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
175-228 |
6.40e-03 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 36.70 E-value: 6.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446866837 175 TVPVVVDAGIGvPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGL 228
Cdd:PRK00043 160 DIPIVAIGGIT-PENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
124-211 |
9.67e-03 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 36.58 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 124 FVVLPYCGaDPV-LCKRLEEVGCAAVMPLGApIGSNQGLETcaMLEIIIQQAT---VPVVVDAGIGVPSHAAQALEMGAD 199
Cdd:TIGR00735 23 FLNLRDAG-DPVeLAQRYDEEGADELVFLDI-TASSEGRTT--MIDVVERTAEtvfIPLTVGGGIKSIEDVDKLLRAGAD 98
|
90
....*....|..
gi 446866837 200 AVLVNTAiAVAD 211
Cdd:TIGR00735 99 KVSINTA-AVKN 109
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
124-211 |
9.69e-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: 36.30 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866837 124 FVVLPYCGaDPV-LCKRLEEVGCAAVMPL---GAPIGSNQGLEtcaMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGAD 199
Cdd:pfam00977 22 FQNTVYAG-DPVeLAKRYEEEGADELHFVdldAAKEGRPVNLD---VVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGAD 97
|
90
....*....|..
gi 446866837 200 AVLVNTAiAVAD 211
Cdd:pfam00977 98 RVIIGTA-AVKN 108
|
|
| |
