|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13936 |
PRK13936 |
phosphoheptose isomerase; Provisional |
1-197 |
1.57e-147 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 237567 Cd Length: 197 Bit Score: 407.51 E-value: 1.57e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 1 MDMQSRIRQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIA 80
Cdd:PRK13936 1 MDLQSRIRQHFEDSIDTKQQAMEVLAPPIAQAVELMVQALLNEGKILACGNGGSAADAQHFSAELLNRFERERPSLPAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 81 LTTDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLLPED 160
Cdd:PRK13936 81 LTTDTSTLTAIANDYSYNEVFSKQVRALGQPGDVLLAISTSGNSANVIQAIQAAHEREMHVVALTGRDGGKMASLLLPED 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 949219391 161 VEIRVPANVTARIQEVHLLTIHCLCDLIDSQLFGSEE 197
Cdd:PRK13936 161 VEIRVPAERTARIQEVHLLAIHCLCDLIDSQLLGSEE 197
|
|
| GmhA |
COG0279 |
Phosphoheptose isomerase [Carbohydrate transport and metabolism]; |
3-194 |
7.14e-119 |
|
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
Pssm-ID: 440048 [Multi-domain] Cd Length: 189 Bit Score: 334.78 E-value: 7.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 3 MQSRIRQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALT 82
Cdd:COG0279 1 MLDRIKQYFEESIEALQALAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIALT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 83 TDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVE 162
Cdd:COG0279 81 TDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGL---ADIE 157
|
170 180 190
....*....|....*....|....*....|..
gi 949219391 163 IRVPANVTARIQEVHLLTIHCLCDLIDSQLFG 194
Cdd:COG0279 158 IRVPSDSTARIQEVHLLIIHILCELIEAALFG 189
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
11-189 |
2.32e-96 |
|
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).
Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 277.08 E-value: 2.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 11 FQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITS 90
Cdd:cd05006 1 FQESIQLKEALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTTDTSILTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 91 IANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVEIRVPANVT 170
Cdd:cd05006 81 IANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLEL---ADIEIHVPSDDT 157
|
170
....*....|....*....
gi 949219391 171 ARIQEVHLLTIHCLCDLID 189
Cdd:cd05006 158 PRIQEVHLLIGHILCELVE 176
|
|
| gmhA |
TIGR00441 |
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ... |
35-189 |
1.44e-71 |
|
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely related paralo in Escherichia coli differs in function (DnaA initiator-associating protein diaA), this model has been rebuilt with a high stringency, and is likely to miss many true examples for phosphoheptose isomerase. Involved in lipopolysaccharide biosynthesis it may have a role in virulence in Haemophilus ducreyi. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129533 Cd Length: 154 Bit Score: 213.96 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 35 VMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITSIANDYSYNEIFSKQIRALGQPGDV 114
Cdd:TIGR00441 3 LLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSADVSHLTCVSNDYGYEDVFSRQVEALGQKGDV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949219391 115 LLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVEIRVPANVTARIQEVHLLTIHCLCDLID 189
Cdd:TIGR00441 83 LLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGL---ADIELRVPHFYTPRIQEIHIKVIHILCQLIE 154
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
9-146 |
2.14e-39 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 433326 [Multi-domain] Cd Length: 138 Bit Score: 131.56 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 9 QLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSti 88
Cdd:pfam13580 1 QYLDEVRALLERVVETQADAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALHTDAS-- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 89 TSIANDYSYNEIFSKQIRAL--GQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTG 146
Cdd:pfam13580 79 ATISTALERDEGYARQILALypGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13936 |
PRK13936 |
phosphoheptose isomerase; Provisional |
1-197 |
1.57e-147 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 237567 Cd Length: 197 Bit Score: 407.51 E-value: 1.57e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 1 MDMQSRIRQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIA 80
Cdd:PRK13936 1 MDLQSRIRQHFEDSIDTKQQAMEVLAPPIAQAVELMVQALLNEGKILACGNGGSAADAQHFSAELLNRFERERPSLPAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 81 LTTDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLLPED 160
Cdd:PRK13936 81 LTTDTSTLTAIANDYSYNEVFSKQVRALGQPGDVLLAISTSGNSANVIQAIQAAHEREMHVVALTGRDGGKMASLLLPED 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 949219391 161 VEIRVPANVTARIQEVHLLTIHCLCDLIDSQLFGSEE 197
Cdd:PRK13936 161 VEIRVPAERTARIQEVHLLAIHCLCDLIDSQLLGSEE 197
|
|
| GmhA |
COG0279 |
Phosphoheptose isomerase [Carbohydrate transport and metabolism]; |
3-194 |
7.14e-119 |
|
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
Pssm-ID: 440048 [Multi-domain] Cd Length: 189 Bit Score: 334.78 E-value: 7.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 3 MQSRIRQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALT 82
Cdd:COG0279 1 MLDRIKQYFEESIEALQALAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIALT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 83 TDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVE 162
Cdd:COG0279 81 TDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGL---ADIE 157
|
170 180 190
....*....|....*....|....*....|..
gi 949219391 163 IRVPANVTARIQEVHLLTIHCLCDLIDSQLFG 194
Cdd:COG0279 158 IRVPSDSTARIQEVHLLIIHILCELIEAALFG 189
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
11-189 |
2.32e-96 |
|
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).
Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 277.08 E-value: 2.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 11 FQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITS 90
Cdd:cd05006 1 FQESIQLKEALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTTDTSILTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 91 IANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVEIRVPANVT 170
Cdd:cd05006 81 IANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLEL---ADIEIHVPSDDT 157
|
170
....*....|....*....
gi 949219391 171 ARIQEVHLLTIHCLCDLID 189
Cdd:cd05006 158 PRIQEVHLLIGHILCELVE 176
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
11-194 |
7.65e-91 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 263.64 E-value: 7.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 11 FQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITS 90
Cdd:PRK13937 6 FRESQAVMEAFLESLLEAIAKVAEALIEALANGGKILLCGNGGSAADAQHIAAELVGRFKKERPALPAIALTTDTSALTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 91 IANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLlpeDVEIRVPANVT 170
Cdd:PRK13937 86 IGNDYGFERVFSRQVEALGRPGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELC---DHLLIVPSDDT 162
|
170 180
....*....|....*....|....
gi 949219391 171 ARIQEVHLLTIHCLCDLIDSQLFG 194
Cdd:PRK13937 163 PRIQEMHITIGHILCDLVERALFE 186
|
|
| PRK10886 |
PRK10886 |
DnaA initiator-associating protein DiaA; Provisional |
3-193 |
2.78e-82 |
|
DnaA initiator-associating protein DiaA; Provisional
Pssm-ID: 182811 Cd Length: 196 Bit Score: 242.53 E-value: 2.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 3 MQSRIRQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALT 82
Cdd:PRK10886 1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 83 TDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVE 162
Cdd:PRK10886 81 TDNVVLTAIANDRLHDEVYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160
|
170 180 190
....*....|....*....|....*....|.
gi 949219391 163 IRVPANVTARIQEVHLLTIHCLCDLIDSQLF 193
Cdd:PRK10886 161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLF 191
|
|
| gmhA |
TIGR00441 |
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ... |
35-189 |
1.44e-71 |
|
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely related paralo in Escherichia coli differs in function (DnaA initiator-associating protein diaA), this model has been rebuilt with a high stringency, and is likely to miss many true examples for phosphoheptose isomerase. Involved in lipopolysaccharide biosynthesis it may have a role in virulence in Haemophilus ducreyi. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129533 Cd Length: 154 Bit Score: 213.96 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 35 VMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITSIANDYSYNEIFSKQIRALGQPGDV 114
Cdd:TIGR00441 3 LLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSADVSHLTCVSNDYGYEDVFSRQVEALGQKGDV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949219391 115 LLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVEIRVPANVTARIQEVHLLTIHCLCDLID 189
Cdd:TIGR00441 83 LLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGL---ADIELRVPHFYTPRIQEIHIKVIHILCQLIE 154
|
|
| gmhA |
PRK00414 |
D-sedoheptulose 7-phosphate isomerase; |
29-192 |
5.73e-63 |
|
D-sedoheptulose 7-phosphate isomerase;
Pssm-ID: 179012 [Multi-domain] Cd Length: 192 Bit Score: 193.41 E-value: 5.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 29 IEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTtDSSTITSIANDYSYNEIFSKQIRAL 108
Cdd:PRK00414 30 IQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHLSCVSNDFGYDYVFSRYVEAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 109 GQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVEIRVP-ANVTARIQEVHLLTIHCLCDL 187
Cdd:PRK00414 109 GREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGL---ADIEIRVPhFGYADRIQEIHIKVIHILIQL 185
|
....*
gi 949219391 188 IDSQL 192
Cdd:PRK00414 186 IEKEM 190
|
|
| PRK13938 |
PRK13938 |
phosphoheptose isomerase; Provisional |
44-197 |
7.44e-40 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 139997 [Multi-domain] Cd Length: 196 Bit Score: 134.48 E-value: 7.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 44 GKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGN 123
Cdd:PRK13938 46 ARVFMCGNGGSAADAQHFAAELTGHLIFDRPPLGAEALHANSSHLTAVANDYDYDTVFARALEGSARPGDTLFAISTSGN 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949219391 124 SANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVEIRVPANVTARIQEVHLLTIHCLCDLIDSQLFGSEE 197
Cdd:PRK13938 126 SMSVLRAAKTARELGVTVVAMTGESGGQLAEF---ADFLINVPSRDTGRIQESHIVFIHAISEHVEHALFAPRQ 196
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
9-146 |
2.14e-39 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 433326 [Multi-domain] Cd Length: 138 Bit Score: 131.56 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 9 QLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSti 88
Cdd:pfam13580 1 QYLDEVRALLERVVETQADAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALHTDAS-- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 89 TSIANDYSYNEIFSKQIRAL--GQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTG 146
Cdd:pfam13580 79 ATISTALERDEGYARQILALypGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
49-145 |
2.93e-09 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 51.99 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 49 CGNGGSAGDAQHFSSELLNRFererpSLPAIALTTDSSTITSIAndysyneifskqirALGQPGDVLLAISTSGNSANII 128
Cdd:cd04795 4 IGIGGSGAIAAYFALELLELT-----GIEVVALIATELEHASLL--------------SLLRKGDVVIALSYSGRTEELL 64
|
90
....*....|....*..
gi 949219391 129 QAIQAAHDREMIVVALT 145
Cdd:cd04795 65 AALEIAKELGIPVIAIT 81
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
2-188 |
5.24e-08 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 51.47 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 2 DMQSRIRQLFQASIDTKQQAMDVLAP-HIEQASQVMVNAllneGKMLSCGNGGSAGDAQHFSsellNRFERERPslPAIA 80
Cdd:COG1737 96 SLEDILAKVLEAEIANLEETLELLDEeALERAVDLLAKA----RRIYIFGVGASAPVAEDLA----YKLLRLGK--NVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 81 LTTDSSTITSIANDYSyneifskqiralgqPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMAS-----L 155
Cdd:COG1737 166 LDGDGHLQAESAALLG--------------PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKladvvL 231
|
170 180 190
....*....|....*....|....*....|...
gi 949219391 156 LLPEDVEIRVPANVTARIqeVHLLTIHCLCDLI 188
Cdd:COG1737 232 YVPSEEPTLRSSAFSSRV--AQLALIDALAAAV 262
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
111-148 |
8.20e-06 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 43.76 E-value: 8.20e-06
10 20 30
....*....|....*....|....*....|....*...
gi 949219391 111 PGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRD 148
Cdd:cd05013 60 PGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSA 97
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
110-167 |
4.94e-05 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 42.18 E-value: 4.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 949219391 110 QPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLlpeDVEIRVPA 167
Cdd:cd05005 74 GPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLA---DVVVVIPA 128
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
110-146 |
7.42e-05 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 40.99 E-value: 7.42e-05
10 20 30
....*....|....*....|....*....|....*..
gi 949219391 110 QPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTG 146
Cdd:cd05014 46 TPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITG 82
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
88-167 |
6.19e-04 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 38.43 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 88 ITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMAS-----LLLPEDVE 162
Cdd:pfam01380 30 IGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAReadhvLYINAGPE 109
|
....*
gi 949219391 163 IRVPA 167
Cdd:pfam01380 110 TGVAS 114
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
19-167 |
6.33e-04 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 39.50 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 19 QQAMDVLAPHIEQASQVMVNAllNEGKMLSCGNGGSagdaqHFSSELLNRFERERPSLPAIALTTdssTITSIANDYsyn 98
Cdd:COG2222 12 RRALAALAAAIAALLARLRAK--PPRRVVLVGAGSS-----DHAAQAAAYLLERLLGIPVAALAP---SELVVYPAY--- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949219391 99 eifskqiraLGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMA-----SLLLPEDVEIRVPA 167
Cdd:COG2222 79 ---------LKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAeaadrVLPLPAGPEKSVAA 143
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
107-179 |
7.21e-04 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 39.36 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 107 ALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLllpEDVEIRVPA--------NVTARIQEVHL 178
Cdd:PRK11337 183 ALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKL---ADYVICSTAqgspllgeNAAARIAQLNI 259
|
.
gi 949219391 179 L 179
Cdd:PRK11337 260 L 260
|
|
| PRK02947 |
PRK02947 |
sugar isomerase domain-containing protein; |
1-145 |
1.50e-03 |
|
sugar isomerase domain-containing protein;
Pssm-ID: 179510 [Multi-domain] Cd Length: 246 Bit Score: 38.31 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949219391 1 MDMQSrirQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQhfssELLNR---FERERP-SL 76
Cdd:PRK02947 1 TDMID---EYFDAVIELLERVRETQAEAIEKAADLIADSIRNGGLIYVFGTGHSHILAE----EVFYRaggLAPVNPiLE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949219391 77 PAIALTTDSSTITSIANDYSYNEIF--SKQIRalgqPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALT 145
Cdd:PRK02947 74 PSLMLHEGAVASSYLERVEGYAKAIldRYDIR----PGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVT 140
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
108-147 |
2.17e-03 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 38.03 E-value: 2.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 949219391 108 LG--QPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGR 147
Cdd:COG0794 86 LGmiTPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGN 127
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
111-167 |
4.17e-03 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 35.94 E-value: 4.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949219391 111 PGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMA-----SLLLPEDVEIRVPA 167
Cdd:cd05008 46 EDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAreadyVLYLRAGPEISVAA 107
|
|
| |
