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Conserved domains on  [gi|446866847|ref|WP_000944103|]
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MULTISPECIES: thiazole synthase [Enterobacteriaceae]

Protein Classification

thiazole synthase( domain architecture ID 18578739)

thiazole synthase (ThiG) catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine

EC:  2.8.1.10
Gene Ontology:  GO:1990107

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiG COG2022
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ...
 1-254 3.22e-164

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: 454.49  E-value: 3.22e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHN-DAILEPLIAAGVTLLPNTSGAKTAEEAI 79
Cdd:COG2022    5 PLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGgDNLLDYLDPLGVTLLPNTAGCRTAEEAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  80 FAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQ 159
Cdd:COG2022   85 RTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGSGL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 160 GLETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRS 239
Cdd:COG2022  165 GLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKR 244

                        250
                 ....*....|....*
gi 446866847 240 HFAHATSPLTGFLEA 254
Cdd:COG2022  245 DYASASSPLTGFLHQ 259
 
Name Accession Description Interval E-value
ThiG COG2022
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ...
 1-254 3.22e-164

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: 454.49  E-value: 3.22e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHN-DAILEPLIAAGVTLLPNTSGAKTAEEAI 79
Cdd:COG2022    5 PLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGgDNLLDYLDPLGVTLLPNTAGCRTAEEAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  80 FAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQ 159
Cdd:COG2022   85 RTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGSGL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 160 GLETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRS 239
Cdd:COG2022  165 GLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKR 244

                        250
                 ....*....|....*
gi 446866847 240 HFAHATSPLTGFLEA 254
Cdd:COG2022  245 DYASASSPLTGFLHQ 259
thiG PRK00208
thiazole synthase; Reviewed
 1-250 2.93e-163

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 451.82  E-value: 2.93e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK00208   1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:PRK00208  81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 161 LETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240

                        250
                 ....*....|
gi 446866847 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 2.39e-146

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: 408.80  E-value: 2.39e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDL-RQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:cd04728    1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:cd04728   81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 161 LETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:cd04728  161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240


                 ....*...
gi 446866847 241 FAHATSPL 248
Cdd:cd04728  241 YASASSPL 248
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 3-247 1.37e-144

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: 404.71  E-value: 1.37e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847    3 RIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQ--HNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:pfam05690   1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAkpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:pfam05690  81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  161 LETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240


                  ....*..
gi 446866847  241 FAHATSP 247
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 3.22e-164

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: 454.49  E-value: 3.22e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHN-DAILEPLIAAGVTLLPNTSGAKTAEEAI 79
Cdd:COG2022    5 PLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGgDNLLDYLDPLGVTLLPNTAGCRTAEEAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  80 FAAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQ 159
Cdd:COG2022   85 RTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGSGL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 160 GLETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRS 239
Cdd:COG2022  165 GLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRMPKR 244

                        250
                 ....*....|....*
gi 446866847 240 HFAHATSPLTGFLEA 254
Cdd:COG2022  245 DYASASSPLTGFLHQ 259
thiG PRK00208
thiazole synthase; Reviewed
 1-250 2.93e-163

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 451.82  E-value: 2.93e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   1 MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK00208   1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:PRK00208  81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 161 LETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240

                        250
                 ....*....|
gi 446866847 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 2.39e-146

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: 408.80  E-value: 2.39e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDL-RQHNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:cd04728    1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:cd04728   81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 161 LETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:cd04728  161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240


                 ....*...
gi 446866847 241 FAHATSPL 248
Cdd:cd04728  241 YASASSPL 248
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 3-247 1.37e-144

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: 404.71  E-value: 1.37e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847    3 RIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQ--HNDAILEPLIAAGVTLLPNTSGAKTAEEAIF 80
Cdd:pfam05690   1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAkpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:pfam05690  81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  161 LETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240


                  ....*..
gi 446866847  241 FAHATSP 247
Cdd:pfam05690 241 YASASSP 247
thiG CHL00162
thiamin biosynthesis protein G; Validated
 2-252 3.70e-106

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 308.18  E-value: 3.70e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHND--AILEPLIAAGVTLLPNTSGAKTAEEAI 79
Cdd:CHL00162   8 LKIGNKSFNSRLMLGTGKYKSLKDAIQSIEASGCEIVTVAIRRLNNNLLNDnsNLLNGLDWNKLWLLPNTAGCQTAEEAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  80 FAAHLARE---ALG---TNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGA 153
Cdd:CHL00162  88 RMAFLGRElakQLGqedNNFVKLEVISDPKYLLPDPIGTLKAAEFLVKKGFTVLPYINADPMLAKHLEDIGCATVMPLGS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 154 PIGSNQGLETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQS 233
Cdd:CHL00162 168 PIGSGQGLQNLLNLQIIIENAKIPVIIDAGIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAVQAGRLAYLA 247

                        250
                 ....*....|....*....
gi 446866847 234 GPGSRSHFAHATSPLTGFL 252
Cdd:CHL00162 248 GRMPKKKYAQASSPIEGIS 266
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 2-250 5.47e-96

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 284.33  E-value: 5.47e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847   2 LRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIA-AGVTLLPNTSGAKTAEEAIF 80
Cdd:PRK11840  75 WTVAGKTFSSRLLVGTGKYKDFEETAAAVEASGAEIVTVAVRRVNVSDPGAPMLTDYIDpKKYTYLPNTAGCYTAEEAVR 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  81 AAHLAREALGTNWLKLEIHPDARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQG 160
Cdd:PRK11840 155 TLRLAREAGGWDLVKLEVLGDAKTLYPDMVETLKATEILVKEGFQVMVYCSDDPIAAKRLEDAGAVAVMPLGAPIGSGLG 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 161 LETRAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGLLARQSGPGSRSH 240
Cdd:PRK11840 235 IQNPYTIRLIVEGATVPVLVDAGVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLAYLAGRMPRRR 314

                        250
                 ....*....|
gi 446866847 241 FAHATSPLTG 250
Cdd:PRK11840 315 YADPSSPLAG 324
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 165-207 8.12e-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: 8.12e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446866847 165 AMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAI 207
Cdd:cd04729  167 ELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAI 209
PRK07695 PRK07695
thiazole tautomerase TenI;
154-224 9.02e-06

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 45.40  E-value: 9.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446866847 154 PIGSNQGLETRAMLEI--IIQQATVPVVVDAGIgVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAV 224
Cdd:PRK07695 126 PTDCKKGVPARGLEELsdIARALSIPVIAIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESI 197
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 26-205 1.76e-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: 44.50  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  26 MVEAIRASGSQLVTLAMKRVDLRQHNDAILEPLIAA----GVTLLPNTSGAKTAEEAIFAAHLAREAlGTNWLKL-EIHP 100
Cdd:cd04722   17 LAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVaaetDLPLGVQLAINDAAAAVDIAAAAARAA-GADGVEIhGAVG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 101 DARWLLPDPIETLKAAETLVQQGFVVLPYCGADPVLCKRL--EEVGCAAVMPLGAPIGSNqgLETRAMLEIIIQQATVPV 178
Cdd:cd04722   96 YLAREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAgvDEVGLGNGGGGGGGRDAV--PIADLLLILAKRGSKVPV 173

                        170       180
                 ....*....|....*....|....*..
gi 446866847 179 VVDAGIGVPSHAAQALEMGADAVLVNT 205
Cdd:cd04722  174 IAGGGINDPEDAAEALALGADGVIVGS 200
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
165-207 3.41e-05

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 43.60  E-value: 3.41e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446866847 165 AMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAI 207
Cdd:PRK01130 163 ALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAI 205
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 159-221 1.38e-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: 1.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446866847 159 QGLEtraMLEIIIQQATVPVVVDAGIGvPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFR 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 446866847 177 PVVVDA--GIGVPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAV 224
Cdd:cd04727  196 PVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARAIVEAV 245
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 148-207 2.57e-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: 38.02  E-value: 2.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847 148 VMPLGApIGSNQGLETrAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAI 207
Cdd:cd04723  164 VLDIDR-VGSGQGPDL-ELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 159-227 2.79e-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: 2.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446866847 159 QGLEtraMLEIIIQQATVPVVVDAGIGvPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAG 227
Cdd:COG0352  142 LGLE---GLAWWAELVEIPVVAIGGIT-PENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 124-211 6.54e-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: 37.07  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866847  124 FVVLPYCGaDPV-LCKRLEEvgcaavmpLGAPI-------GSNQGLET-RAMLEIIIQQATVPVVVDAGIGVPSHAAQAL 194
Cdd:pfam00977  22 FQNTVYAG-DPVeLAKRYEE--------EGADElhfvdldAAKEGRPVnLDVVEEIAEEVFIPVQVGGGIRSLEDVERLL 92

                          90
                  ....*....|....*..
gi 446866847  195 EMGADAVLVNTAiAVAD 211
Cdd:pfam00977  93 SAGADRVIIGTA-AVKN 108
thiE PRK00043
thiamine phosphate synthase;
175-228 6.89e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 36.70  E-value: 6.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446866847 175 TVPVVVDAGIGvPSHAAQALEMGADAVLVNTAIAVADDPVNMAKAFRLAVEAGL 228
Cdd:PRK00043 160 DIPIVAIGGIT-PENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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