|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-250 |
5.53e-144 |
|
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: 403.26 E-value: 5.53e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 1 MAESKLVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDADGGTG--LLDLLNRLGITPLPNTAGCRSA 78
Cdd:COG2022 1 MMDDPLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGGdnLLDYLDPLGVTLLPNTAGCRTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 79 AEAVLTAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPI 158
Cdd:COG2022 81 EEAVRTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 159 GTGLGIANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGR 238
Cdd:COG2022 161 GSGLGLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGR 240
|
250
....*....|..
gi 489497213 239 IPKRFWAQASSP 250
Cdd:COG2022 241 MPKRDYASASSP 252
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
5-250 |
7.81e-141 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 394.81 E-value: 7.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 5 KLVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDA-DGGTGLLDLLNRLGITPLPNTAGCRSAAEAVL 83
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLgQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 84 TAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPIGTGLG 163
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 164 IANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGRIPKRF 243
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
....*..
gi 489497213 244 WAQASSP 250
Cdd:PRK00208 241 YASASSP 247
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
6-250 |
6.62e-129 |
|
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: 364.50 E-value: 6.62e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 6 LVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVD--ADGGTGLLDLLNRLGITPLPNTAGCRSAAEAVL 83
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNigDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 84 TAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPIGTGLG 163
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 164 IANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGRIPKRF 243
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*..
gi 489497213 244 WAQASSP 250
Cdd:cd04728 241 YASASSP 247
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
7-250 |
4.63e-128 |
|
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: 362.72 E-value: 4.63e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 7 VIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDAD---GGTGLLDLLNRLGITPLPNTAGCRSAAEAVL 83
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGakpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 84 TAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPIGTGLG 163
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 164 IANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGRIPKRF 243
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 489497213 244 WAQASSP 250
Cdd:pfam05690 241 YASASSP 247
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-250 |
5.53e-144 |
|
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: 403.26 E-value: 5.53e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 1 MAESKLVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDADGGTG--LLDLLNRLGITPLPNTAGCRSA 78
Cdd:COG2022 1 MMDDPLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPGGdnLLDYLDPLGVTLLPNTAGCRTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 79 AEAVLTAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPI 158
Cdd:COG2022 81 EEAVRTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 159 GTGLGIANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGR 238
Cdd:COG2022 161 GSGLGLLNPYNLRIIIEQADVPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGR 240
|
250
....*....|..
gi 489497213 239 IPKRFWAQASSP 250
Cdd:COG2022 241 MPKRDYASASSP 252
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
5-250 |
7.81e-141 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 394.81 E-value: 7.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 5 KLVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDA-DGGTGLLDLLNRLGITPLPNTAGCRSAAEAVL 83
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLgQGGDNLLDLLPPLGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 84 TAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPIGTGLG 163
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 164 IANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGRIPKRF 243
Cdd:PRK00208 161 LLNPYNLRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKRD 240
|
....*..
gi 489497213 244 WAQASSP 250
Cdd:PRK00208 241 YASASSP 247
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
6-250 |
6.62e-129 |
|
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: 364.50 E-value: 6.62e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 6 LVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVD--ADGGTGLLDLLNRLGITPLPNTAGCRSAAEAVL 83
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNigDPGGESFLDLLDKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 84 TAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPIGTGLG 163
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 164 IANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGRIPKRF 243
Cdd:cd04728 161 LLNPYNLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKRD 240
|
....*..
gi 489497213 244 WAQASSP 250
Cdd:cd04728 241 YASASSP 247
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
7-250 |
4.63e-128 |
|
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: 362.72 E-value: 4.63e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 7 VIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDAD---GGTGLLDLLNRLGITPLPNTAGCRSAAEAVL 83
Cdd:pfam05690 1 TIGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGakpGGDNILDLLPPKGITLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 84 TAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPIGTGLG 163
Cdd:pfam05690 81 TARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 164 IANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGRIPKRF 243
Cdd:pfam05690 161 LLNPYNLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 489497213 244 WAQASSP 250
Cdd:pfam05690 241 YASASSP 247
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
1-252 |
2.87e-95 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 282.41 E-value: 2.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 1 MAESKLVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDAD--GGTGLLDLLNRLGITPLPNTAGCRSA 78
Cdd:PRK11840 70 VADDSWTVAGKTFSSRLLVGTGKYKDFEETAAAVEASGAEIVTVAVRRVNVSdpGAPMLTDYIDPKKYTYLPNTAGCYTA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 79 AEAVLTAQLAREALNTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPI 158
Cdd:PRK11840 150 EEAVRTLRLAREAGGWDLVKLEVLGDAKTLYPDMVETLKATEILVKEGFQVMVYCSDDPIAAKRLEDAGAVAVMPLGAPI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 159 GTGLGIANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARCAGR 238
Cdd:PRK11840 230 GSGLGIQNPYTIRLIVEGATVPVLVDAGVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLAYLAGR 309
|
250
....*....|....
gi 489497213 239 IPKRFWAQASSPAR 252
Cdd:PRK11840 310 MPRRRYADPSSPLA 323
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
5-250 |
3.70e-92 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 272.35 E-value: 3.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 5 KLVIGDRSFASRLIMGTGGATNLAVLEQALIASGTELTTVAIRRVDAD---GGTGLLDLLNRLGITPLPNTAGCRSAAEA 81
Cdd:CHL00162 7 KLKIGNKSFNSRLMLGTGKYKSLKDAIQSIEASGCEIVTVAIRRLNNNllnDNSNLLNGLDWNKLWLLPNTAGCQTAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 82 VLTAQLAREAL------NTNWVKLEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLG 155
Cdd:CHL00162 87 IRMAFLGRELAkqlgqeDNNFVKLEVISDPKYLLPDPIGTLKAAEFLVKKGFTVLPYINADPMLAKHLEDIGCATVMPLG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 156 SPIGTGLGIANPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTRAADPPAMAAAMAAAVTAGYLARC 235
Cdd:CHL00162 167 SPIGSGQGLQNLLNLQIIIENAKIPVIIDAGIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAVQAGRLAYL 246
|
250
....*....|....*
gi 489497213 236 AGRIPKRFWAQASSP 250
Cdd:CHL00162 247 AGRMPKKKYAQASSP 261
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
20-208 |
4.51e-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: 51.82 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 20 GTGGATNLAVLEQALIASGTELTTV----AIRRVDADGGTGLLDLLNRLGITPLPNTAgCRSAAEAVLTAQLAREALNTN 95
Cdd:cd04722 8 GGPSGDPVELAKAAAEAGADAIIVGtrssDPEEAETDDKEVLKEVAAETDLPLGVQLA-INDAAAAVDIAAAAARAAGAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 96 WVklEVIADERTLWPDAVELVRAAEQLVDDGFVVLPYTTDDPVLARRLEDTGCAAVMPLGSPIGTGLGIANPHNIEM--- 172
Cdd:cd04722 87 GV--EIHGAVGYLAREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLlil 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 489497213 173 IVAGARVPVVLDAGIGTASDAALAMELGCDAVLLAS 208
Cdd:cd04722 165 AKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
158-210 |
2.07e-06 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 47.17 E-value: 2.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 158 IGTGLGI--ANPHNIEMIVAGAR-----VPVVLDAGIGTASDAALAMELGCDAVLLASAV 210
Cdd:PRK04302 146 IGTGIPVskAKPEVVEDAVEAVKkvnpdVKVLCGAGISTGEDVKAALELGADGVLLASGV 205
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
114-206 |
1.16e-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: 39.50 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 114 ELVRAAEQLVDDGFVVlpyTTDDPVLARRLED----------TGCAAVMPLGSPIGTGLGIANPHN-------IEMIVAG 176
Cdd:cd02922 135 ELLKRAEKLGAKAIFL---TVDAPVLGKRERDerlkaeeavsDGPAGKKTKAKGGGAGRAMSGFIDptltwddIKWLRKH 211
|
90 100 110
....*....|....*....|....*....|
gi 489497213 177 ARVPVVLDaGIGTASDAALAMELGCDAVLL 206
Cdd:cd02922 212 TKLPIVLK-GVQTVEDAVLAAEYGVDGIVL 240
|
|
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
178-208 |
1.48e-03 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 38.97 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|...
gi 489497213 178 RVPVVLDA--GIGTASDAALAMELGCDAVLLAS 208
Cdd:PRK04180 203 RLPVVNFAagGIATPADAALMMQLGADGVFVGS 235
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
178-210 |
2.06e-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: 38.77 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|....*
gi 489497213 178 RVPVVLDA--GIGTASDAALAMELGCDAVLLASAV 210
Cdd:cd04727 194 RLPVVNFAagGVATPADAALMMQLGADGVFVGSGI 228
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| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
170-212 |
3.19e-03 |
|
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: 37.94 E-value: 3.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 489497213 170 IEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAVTR 212
Cdd:cd04729 169 LKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITR 211
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| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
151-210 |
8.76e-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: 36.48 E-value: 8.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497213 151 VMPLGSpIGTGLGIaNPHNIEMIVAGARVPVVLDAGIGTASDAALAMELGCDAVLLASAV 210
Cdd:cd04723 164 VLDIDR-VGSGQGP-DLELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
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