|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-255 |
5.77e-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: 443.70 E-value: 5.77e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 1 MDKLNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDLNSR-EENILNYIK-DDCVLLPNTSGARNAEE 78
Cdd:COG2022 3 DDPLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPgGDNLLDYLDpLGVTLLPNTAGCRTAEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 79 AVRLARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGT 158
Cdd:COG2022 83 AVRTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 159 NKGLKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFG 238
Cdd:COG2022 163 GLGLLNPYNLRIIIEQAD-VPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRM 241
|
250
....*....|....*..
gi 499412473 239 TEAKFANASSPLIGFLR 255
Cdd:COG2022 242 PKRDYASASSPLTGFLH 258
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
3-252 |
1.38e-153 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 427.17 E-value: 1.38e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 3 KLNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDLNSREENILNYIKD-DCVLLPNTSGARNAEEAVR 81
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPlGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 82 LARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTNKG 161
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 162 LKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGTEA 241
Cdd:PRK00208 161 LLNPYNLRIIIEQAD-VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKR 239
|
250
....*....|.
gi 499412473 242 KFANASSPLIG 252
Cdd:PRK00208 240 DYASASSPLTG 250
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
4-250 |
4.53e-138 |
|
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: 388.00 E-value: 4.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 4 LNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDL-NSREENILNYI-KDDCVLLPNTSGARNAEEAVR 81
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLdKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 82 LARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTNKG 161
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 162 LKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGTEA 241
Cdd:cd04728 161 LLNPYNLRIIIERAD-VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKR 239
|
....*....
gi 499412473 242 KFANASSPL 250
Cdd:cd04728 240 DYASASSPL 248
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
6-249 |
1.02e-132 |
|
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: 374.28 E-value: 1.02e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 6 IGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDLNSR--EENILNYIK-DDCVLLPNTSGARNAEEAVRL 82
Cdd:pfam05690 2 IGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAKpgGDNILDLLPpKGITLLPNTAGCRTAEEAVRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 83 ARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTNKGL 162
Cdd:pfam05690 82 ARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 163 KTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGTEAK 242
Cdd:pfam05690 162 LNPYNLKIIIEEAD-VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 499412473 243 FANASSP 249
Cdd:pfam05690 241 YASASSP 247
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-255 |
5.77e-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: 443.70 E-value: 5.77e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 1 MDKLNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDLNSR-EENILNYIK-DDCVLLPNTSGARNAEE 78
Cdd:COG2022 3 DDPLVIAGRTFSSRLLLGTGKYPSPEVMREAIEASGAEIVTVALRRVNLQDPgGDNLLDYLDpLGVTLLPNTAGCRTAEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 79 AVRLARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGT 158
Cdd:COG2022 83 AVRTARLAREALGTDWVKLEVIGDPKTLLPDPIETLKAAEILVKEGFVVLPYTTDDPVLAKRLEDAGCAAVMPLGAPIGS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 159 NKGLKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFG 238
Cdd:COG2022 163 GLGLLNPYNLRIIIEQAD-VPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAVEAGRLAYLAGRM 241
|
250
....*....|....*..
gi 499412473 239 TEAKFANASSPLIGFLR 255
Cdd:COG2022 242 PKRDYASASSPLTGFLH 258
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
3-252 |
1.38e-153 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 427.17 E-value: 1.38e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 3 KLNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDLNSREENILNYIKD-DCVLLPNTSGARNAEEAVR 81
Cdd:PRK00208 1 MLTIAGKTFSSRLLLGTGKYPSPQVMQEAIEASGAEIVTVALRRVNLGQGGDNLLDLLPPlGVTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 82 LARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTNKG 161
Cdd:PRK00208 81 TARLAREALGTNWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFVVLPYCTDDPVLAKRLEEAGCAAVMPLGAPIGSGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 162 LKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGTEA 241
Cdd:PRK00208 161 LLNPYNLRIIIEQAD-VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVEAGRLAYLAGRIPKR 239
|
250
....*....|.
gi 499412473 242 KFANASSPLIG 252
Cdd:PRK00208 240 DYASASSPLTG 250
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
4-250 |
4.53e-138 |
|
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: 388.00 E-value: 4.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 4 LNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDL-NSREENILNYI-KDDCVLLPNTSGARNAEEAVR 81
Cdd:cd04728 1 LTIGGKTFSSRLLLGTGKYPSPAIMKEAIEASGAEIVTVALRRVNIgDPGGESFLDLLdKSGYTLLPNTAGCRTAEEAVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 82 LARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTNKG 161
Cdd:cd04728 81 TARLAREALGTDWIKLEVIGDDKTLLPDPIETLKAAEILVKEGFTVLPYCTDDPVLAKRLEDAGCAAVMPLGSPIGSGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 162 LKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGTEA 241
Cdd:cd04728 161 LLNPYNLRIIIERAD-VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVEAGRLAYLAGRMPKR 239
|
....*....
gi 499412473 242 KFANASSPL 250
Cdd:cd04728 240 DYASASSPL 248
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
6-249 |
1.02e-132 |
|
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: 374.28 E-value: 1.02e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 6 IGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDLNSR--EENILNYIK-DDCVLLPNTSGARNAEEAVRL 82
Cdd:pfam05690 2 IGGKTFDSRLILGTGKYPSLEVLKEALRASGAQIVTVALRRVNLGAKpgGDNILDLLPpKGITLLPNTAGCRTAEEAVRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 83 ARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTNKGL 162
Cdd:pfam05690 82 ARLAREALGTNWIKLEVIGDEKTLLPDPVETLKAAEILVKEGFIVLPYTSDDPVLARRLEEAGCAAVMPLGAPIGSGLGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 163 KTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGTEAK 242
Cdd:pfam05690 162 LNPYNLKIIIEEAD-VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLAYLAGRMPRRD 240
|
....*..
gi 499412473 243 FANASSP 249
Cdd:pfam05690 241 YASASSP 247
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
2-252 |
1.77e-95 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 283.18 E-value: 1.77e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 2 DKLNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDL-NSREENILNYIKDDCV-LLPNTSGARNAEEA 79
Cdd:PRK11840 73 DSWTVAGKTFSSRLLVGTGKYKDFEETAAAVEASGAEIVTVAVRRVNVsDPGAPMLTDYIDPKKYtYLPNTAGCYTAEEA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 80 VRLARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTN 159
Cdd:PRK11840 153 VRTLRLAREAGGWDLVKLEVLGDAKTLYPDMVETLKATEILVKEGFQVMVYCSDDPIAAKRLEDAGAVAVMPLGAPIGSG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 160 KGLKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGT 239
Cdd:PRK11840 233 LGIQNPYTIRLIVEGAT-VPVLVDAGVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLAYLAGRMP 311
|
250
....*....|...
gi 499412473 240 EAKFANASSPLIG 252
Cdd:PRK11840 312 RRRYADPSSPLAG 324
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
1-255 |
1.30e-92 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 273.51 E-value: 1.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 1 MDKLNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRV--DLNSREENILNYIK-DDCVLLPNTSGARNAE 77
Cdd:CHL00162 5 TDKLKIGNKSFNSRLMLGTGKYKSLKDAIQSIEASGCEIVTVAIRRLnnNLLNDNSNLLNGLDwNKLWLLPNTAGCQTAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 78 EAVRLARLSKAAGC------GNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMP 151
Cdd:CHL00162 85 EAIRMAFLGRELAKqlgqedNNFVKLEVISDPKYLLPDPIGTLKAAEFLVKKGFTVLPYINADPMLAKHLEDIGCATVMP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 152 LGAPIGTNKGLKTEEMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRK 231
Cdd:CHL00162 165 LGSPIGSGQGLQNLLNLQIIIENAK-IPVIIDAGIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAVQAGRL 243
|
250 260
....*....|....*....|....
gi 499412473 232 AYLAGFGTEAKFANASSPLIGFLR 255
Cdd:CHL00162 244 AYLAGRMPKKKYAQASSPIEGISK 267
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
137-209 |
3.55e-05 |
|
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240087 Cd Length: 361 Bit Score: 44.44 E-value: 3.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499412473 137 DAKRFVAAGAAAVmplgapIGTNKGLKTEEMIKILIEEIKEV------PIIVDAGIGKPSDACKAMEMGADAVLLNTAI 209
Cdd:cd04736 249 DAKRCIELGADGV------ILSNHGGRQLDDAIAPIEALAEIvaatykPVLIDSGIRRGSDIVKALALGANAVLLGRAT 321
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
66-207 |
6.11e-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: 42.96 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 66 LLPNTSGARNAEEAVRLARLSKAAGCGnwiKIEAISDNKYLLPDNYETIKATEIlAKEGFYVFPYMNPDLMDAKRFVA-A 144
Cdd:cd04722 60 LGVQLAINDAAAAVDIAAAAARAAGAD---GVEIHGAVGYLAREDLELIRELRE-AVPDVKVVVKLSPTGELAAAAAEeA 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499412473 145 GAAAVMPLGAPIGTNKGLKTEEMI--KILIEEIKEVPIIVDAGIGKPSDACKAMEMGADAVLLNT 207
Cdd:cd04722 136 GVDEVGLGNGGGGGGGRDAVPIADllLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
131-205 |
2.12e-04 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 41.66 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 131 MNPDlmDAKRFVAAGAAAVM--------PLGAPiGTnkglkteemIKILiEEIKE-----VPIIVDAGIGKPSDACKAME 197
Cdd:cd02809 181 LTPE--DALRAVDAGADGIVvsnhggrqLDGAP-AT---------IDAL-PEIVAavggrIEVLLDGGIRRGTDVLKALA 247
|
....*...
gi 499412473 198 MGADAVLL 205
Cdd:cd02809 248 LGADAVLI 255
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
118-226 |
2.24e-04 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 41.64 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 118 EILAKEGFYVFPyMNPDLMDAKRFVAAGAAAVMPLGA---------PIGTnkglkteemiKILIEEIKE---VPIIVDAG 185
Cdd:COG2070 98 ERLKEAGIKVIP-IVTSVREARKAEKAGADAVVAEGAeagghrgadEVST----------FALVPEVRDavdIPVIAAGG 166
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499412473 186 IGKPSDACKAMEMGADAVLLNTA-IATAENPIlmGEAFKNAV 226
Cdd:COG2070 167 IADGRGIAAALALGADGVQMGTRfLATEESPA--HEAYKQAL 206
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
176-215 |
2.81e-04 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 41.01 E-value: 2.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 499412473 176 KEVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENP 215
Cdd:PRK04302 172 PDVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKDP 211
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
137-226 |
3.29e-04 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 40.93 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 137 DAKRFVAAGAAAVMPLGAPIG---TNKGLKTEEmikiLIEEIKE---VPIIVDAGIGKPSDACKAMEMGADAVLLNTA-I 209
Cdd:cd04730 114 EARKAEAAGADALVAQGAEAGghrGTFDIGTFA----LVPEVRDavdIPVIAAGGIADGRGIAAALALGADGVQMGTRfL 189
|
90
....*....|....*..
gi 499412473 210 ATAENPIlmGEAFKNAV 226
Cdd:cd04730 190 ATEESGA--SPAYKQAL 204
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
129-226 |
4.69e-04 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 40.18 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 129 PYMNPDLmdakrfVAAGAAAVMPLGAPI------GTNKGLKTEEMIKILIEEIKEVPIIVDAGIGKPSDACKAMEMGADA 202
Cdd:PRK04169 136 PLDKPDI------AAYAALAAEYLGMPIvyleygGGAGDPVPPEMVKAVKKALDITPLIYGGGIRSPEQARELMAAGADT 209
|
90 100
....*....|....*....|....
gi 499412473 203 VLLNTAIatAENPILMGEAFKNAV 226
Cdd:PRK04169 210 IVVGNII--EEDPKKTVKAIKKAI 231
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
171-209 |
5.29e-04 |
|
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: 40.25 E-value: 5.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 499412473 171 LIEEIKE---VPIIVDAGIGKPSDACKAMEMGADAVLLNTAI 209
Cdd:cd04729 168 LLKELRKalgIPVIAEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
178-215 |
8.12e-04 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 40.19 E-value: 8.12e-04
10 20 30
....*....|....*....|....*....|....*....
gi 499412473 178 VPIIVDAGIGKPSDACKAMEMGADAVLLNTAIA-TAENP 215
Cdd:cd00381 198 VPVIADGGIRTSGDIVKALAAGADAVMLGSLLAgTDESP 236
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
178-238 |
1.65e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 39.18 E-value: 1.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499412473 178 VPIIVDAGIGKPSDACKAMEMGADAVLLNTAIA-TAENPilmGEA-FKNAVEAgrKAY--LAGFG 238
Cdd:PTZ00314 345 VPCIADGGIKNSGDICKALALGADCVMLGSLLAgTEEAP---GEYfFKDGVRL--KVYrgMGSLE 404
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
131-205 |
4.51e-03 |
|
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.
Pssm-ID: 239448 [Multi-domain] Cd Length: 383 Bit Score: 38.03 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 131 MNPDlmDAKRFVAAGAAAVmplgapIGTNKG-------LKTEEMIKILIEEIK-EVPIIVDAGIGKPSDACKAMEMGADA 202
Cdd:cd03332 262 LHPD--DARRAVEAGVDGV------VVSNHGgrqvdgsIAALDALPEIVEAVGdRLTVLFDSGVRTGADIMKALALGAKA 333
|
...
gi 499412473 203 VLL 205
Cdd:cd03332 334 VLI 336
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
178-215 |
4.74e-03 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 37.75 E-value: 4.74e-03
10 20 30
....*....|....*....|....*....|....*....
gi 499412473 178 VPIIVDAGIGKPSDACKAMEMGADAVLLNTAIA-TAENP 215
Cdd:pfam00478 324 VPVIADGGIKYSGDIVKALAAGADAVMLGSLLAgTDESP 362
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
131-205 |
8.60e-03 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 36.74 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412473 131 MNPDlmDAKRFVAAGAAAVMpL---------GAPiGTnkglkteemIKILiEEIKE-----VPIIVDAGIGKPSDACKAM 196
Cdd:pfam01070 227 LSPE--DAKRAVEAGVDGIV-VsnhggrqldGAP-AT---------IDAL-PEIVAavggrIPVLVDGGIRRGTDVLKAL 292
|
....*....
gi 499412473 197 EMGADAVLL 205
Cdd:pfam01070 293 ALGADAVLL 301
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
166-209 |
9.40e-03 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 36.28 E-value: 9.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 499412473 166 EMIKILIEEIKeVPIIVDAGIGKPSDACKAMEMGADAVLLNTAI 209
Cdd:PRK01130 163 ALLKELLKAVG-CPVIAEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| |
