|
Name |
Accession |
Description |
Interval |
E-value |
| gmhA |
PRK00414 |
D-sedoheptulose 7-phosphate isomerase; |
1-192 |
4.51e-154 |
|
D-sedoheptulose 7-phosphate isomerase;
Pssm-ID: 179012 [Multi-domain] Cd Length: 192 Bit Score: 423.76 E-value: 4.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 1 MYQDLIRNELNEAAETLANFLKDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
Cdd:PRK00414 1 MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 81 AISDVSHISCVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEI 160
Cdd:PRK00414 81 AISDVSHLSCVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGLADIEI 160
|
170 180 190
....*....|....*....|....*....|..
gi 494972086 161 RVPHFGYADRIQEIHIKVIHILIQLIEKEMVK 192
Cdd:PRK00414 161 RVPHFGYADRIQEIHIKVIHILIQLIEKEMVK 192
|
|
| GmhA |
COG0279 |
Phosphoheptose isomerase [Carbohydrate transport and metabolism]; |
3-190 |
6.82e-101 |
|
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
Pssm-ID: 440048 [Multi-domain] Cd Length: 189 Bit Score: 288.94 E-value: 6.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 3 QDLIRNELNEAAETLANFlkDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI 82
Cdd:COG0279 2 LDRIKQYFEESIEALQAL--AEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 83 -SDVSHISCVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIR 161
Cdd:COG0279 80 tTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGLADIEIR 159
|
170 180
....*....|....*....|....*....
gi 494972086 162 VPHfGYADRIQEIHIKVIHILIQLIEKEM 190
Cdd:COG0279 160 VPS-DSTARIQEVHLLIIHILCELIEAAL 187
|
|
| gmhA |
TIGR00441 |
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ... |
34-187 |
8.34e-98 |
|
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: 279.83 E-value: 8.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 34 AVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHISCVGNDFGYDHIFSRYVEAVGREG 112
Cdd:TIGR00441 1 VVLLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSaDVSHLTCVSNDYGYEDVFSRQVEALGQKG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494972086 113 DVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVPHFgYADRIQEIHIKVIHILIQLIE 187
Cdd:TIGR00441 81 DVLLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGLADIELRVPHF-YTPRIQEIHIKVIHILCQLIE 154
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
10-188 |
3.68e-83 |
|
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: 243.57 E-value: 3.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 10 LNEAAETLANFLKDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHI 88
Cdd:cd05006 1 FQESIQLKEALLELLAE--AIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTtDTSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 89 SCVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVPHFGYA 168
Cdd:cd05006 79 TAIANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPSDDTP 158
|
170 180
....*....|....*....|
gi 494972086 169 dRIQEIHIKVIHILIQLIEK 188
Cdd:cd05006 159 -RIQEVHLLIGHILCELVEE 177
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
10-146 |
1.73e-32 |
|
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: 113.46 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 10 LNEAAETLANFLKDEAniHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI---SDVS 86
Cdd:pfam13580 3 LDEVRALLERVVETQA--DAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALhtdASAT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 87 HISCVGNDFGYDHIFSRYVEavGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTG 146
Cdd:pfam13580 81 ISTALERDEGYARQILALYP--GRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gmhA |
PRK00414 |
D-sedoheptulose 7-phosphate isomerase; |
1-192 |
4.51e-154 |
|
D-sedoheptulose 7-phosphate isomerase;
Pssm-ID: 179012 [Multi-domain] Cd Length: 192 Bit Score: 423.76 E-value: 4.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 1 MYQDLIRNELNEAAETLANFLKDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
Cdd:PRK00414 1 MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 81 AISDVSHISCVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEI 160
Cdd:PRK00414 81 AISDVSHLSCVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGLADIEI 160
|
170 180 190
....*....|....*....|....*....|..
gi 494972086 161 RVPHFGYADRIQEIHIKVIHILIQLIEKEMVK 192
Cdd:PRK00414 161 RVPHFGYADRIQEIHIKVIHILIQLIEKEMVK 192
|
|
| GmhA |
COG0279 |
Phosphoheptose isomerase [Carbohydrate transport and metabolism]; |
3-190 |
6.82e-101 |
|
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
Pssm-ID: 440048 [Multi-domain] Cd Length: 189 Bit Score: 288.94 E-value: 6.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 3 QDLIRNELNEAAETLANFlkDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI 82
Cdd:COG0279 2 LDRIKQYFEESIEALQAL--AEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 83 -SDVSHISCVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIR 161
Cdd:COG0279 80 tTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGLADIEIR 159
|
170 180
....*....|....*....|....*....
gi 494972086 162 VPHfGYADRIQEIHIKVIHILIQLIEKEM 190
Cdd:COG0279 160 VPS-DSTARIQEVHLLIIHILCELIEAAL 187
|
|
| gmhA |
TIGR00441 |
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ... |
34-187 |
8.34e-98 |
|
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: 279.83 E-value: 8.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 34 AVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHISCVGNDFGYDHIFSRYVEAVGREG 112
Cdd:TIGR00441 1 VVLLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSaDVSHLTCVSNDYGYEDVFSRQVEALGQKG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494972086 113 DVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVPHFgYADRIQEIHIKVIHILIQLIE 187
Cdd:TIGR00441 81 DVLLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGLADIELRVPHF-YTPRIQEIHIKVIHILCQLIE 154
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
10-188 |
3.68e-83 |
|
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: 243.57 E-value: 3.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 10 LNEAAETLANFLKDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHI 88
Cdd:cd05006 1 FQESIQLKEALLELLAE--AIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTtDTSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 89 SCVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVPHFGYA 168
Cdd:cd05006 79 TAIANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPSDDTP 158
|
170 180
....*....|....*....|
gi 494972086 169 dRIQEIHIKVIHILIQLIEK 188
Cdd:cd05006 159 -RIQEVHLLIGHILCELVEE 177
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
5-189 |
4.95e-76 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 225.89 E-value: 4.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 5 LIRNELNEAAETLANFLkdEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS- 83
Cdd:PRK13937 1 LITKHFRESQAVMEAFL--ESLLEAIAKVAEALIEALANGGKILLCGNGGSAADAQHIAAELVGRFKKERPALPAIALTt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 84 DVSHISCVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVP 163
Cdd:PRK13937 79 DTSALTAIGNDYGFERVFSRQVEALGRPGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIVP 158
|
170 180
....*....|....*....|....*.
gi 494972086 164 HFGYAdRIQEIHIKVIHILIQLIEKE 189
Cdd:PRK13937 159 SDDTP-RIQEMHITIGHILCDLVERA 183
|
|
| PRK13936 |
PRK13936 |
phosphoheptose isomerase; Provisional |
11-187 |
4.84e-67 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 237567 Cd Length: 197 Bit Score: 203.74 E-value: 4.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 11 NEAAETLANFlkdeanihaIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI-SDVSHIS 89
Cdd:PRK13936 19 QQAMEVLAPP---------IAQAVELMVQALLNEGKILACGNGGSAADAQHFSAELLNRFERERPSLPAIALtTDTSTLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 90 CVGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMA---GTADVEIRVPHFG 166
Cdd:PRK13936 90 AIANDYSYNEVFSKQVRALGQPGDVLLAISTSGNSANVIQAIQAAHEREMHVVALTGRDGGKMAsllLPEDVEIRVPAER 169
|
170 180
....*....|....*....|.
gi 494972086 167 YAdRIQEIHIKVIHILIQLIE 187
Cdd:PRK13936 170 TA-RIQEVHLLAIHCLCDLID 189
|
|
| PRK10886 |
PRK10886 |
DnaA initiator-associating protein DiaA; Provisional |
24-190 |
1.38e-45 |
|
DnaA initiator-associating protein DiaA; Provisional
Pssm-ID: 182811 Cd Length: 196 Bit Score: 148.93 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 24 EANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHISCVGNDFGYDHIFS 102
Cdd:PRK10886 21 EALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNtDNVVLTAIANDRLHDEVYA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 103 RYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMA---GTADVEIRVPHFGYAdRIQEIHIKVI 179
Cdd:PRK10886 101 KQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAgllGPQDVEIRIPSHRSA-RIQEMHMLTV 179
|
170
....*....|.
gi 494972086 180 HILIQLIEKEM 190
Cdd:PRK10886 180 NCLCDLIDNTL 190
|
|
| PRK13938 |
PRK13938 |
phosphoheptose isomerase; Provisional |
15-190 |
7.20e-39 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 139997 [Multi-domain] Cd Length: 196 Bit Score: 131.78 E-value: 7.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 15 ETLA---NFLKDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI-SDVSHISC 90
Cdd:PRK13938 13 ETIAvktRILNDRVLLEAARAIGDRLIAGYRAGARVFMCGNGGSAADAQHFAAELTGHLIFDRPPLGAEALhANSSHLTA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 91 VGNDFGYDHIFSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVPHFGyADR 170
Cdd:PRK13938 93 VANDYDYDTVFARALEGSARPGDTLFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEFADFLINVPSRD-TGR 171
|
170 180
....*....|....*....|
gi 494972086 171 IQEIHIKVIHILIQLIEKEM 190
Cdd:PRK13938 172 IQESHIVFIHAISEHVEHAL 191
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
10-146 |
1.73e-32 |
|
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: 113.46 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 10 LNEAAETLANFLKDEAniHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI---SDVS 86
Cdd:pfam13580 3 LDEVRALLERVVETQA--DAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALhtdASAT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 87 HISCVGNDFGYDHIFSRYVEavGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTG 146
Cdd:pfam13580 81 ISTALERDEGYARQILALYP--GRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
29-183 |
1.02e-10 |
|
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: 56.85 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 29 AIQRAAVLLADSfkagGKVLSCGNGGSHCDAMHFAeeltgrYRENRPGYPAIAISDvSHIScvgndfgydhifsRYVEAV 108
Cdd:cd05013 2 ALEKAVDLLAKA----RRIYIFGVGSSGLVAEYLA------YKLLRLGKPVVLLSD-PHLQ-------------LMSAAN 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494972086 109 GREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVPHFGYADRIQEIHIKVIHILI 183
Cdd:cd05013 58 LTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| PRK02947 |
PRK02947 |
sugar isomerase domain-containing protein; |
10-145 |
1.18e-10 |
|
sugar isomerase domain-containing protein;
Pssm-ID: 179510 [Multi-domain] Cd Length: 246 Bit Score: 58.73 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 10 LNEAAETLANFLKDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCdamhFAEELTGRYrenrPGYP---AIAISD-V 85
Cdd:PRK02947 8 FDAVIELLERVRETQAE--AIEKAADLIADSIRNGGLIYVFGTGHSHI----LAEEVFYRA----GGLApvnPILEPSlM 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494972086 86 SHISCVGNDF-----GYDHIFsrYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLT 145
Cdd:PRK02947 78 LHEGAVASSYlerveGYAKAI--LDRYDIRPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVT 140
|
|
| COG4821 |
COG4821 |
Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain ... |
10-145 |
1.83e-10 |
|
Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain [General function prediction only];
Pssm-ID: 443849 [Multi-domain] Cd Length: 250 Bit Score: 58.29 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 10 LNEAAETLANFLKDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCdamhFAEELTGRYrenrPGYPAI-AISDVS-- 86
Cdd:COG4821 9 LDEVRELLDRIEETQAE--AIEKAADLIADSIAAGGLVHLFGTGHSHL----LAEEVFYRA----GGLVGFnPILDPSlm 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494972086 87 -HISCVG--------NDFGYDHIFSRYVEAvgREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLT 145
Cdd:COG4821 79 lHNGAPGvlqssfleRVEGYAEIILENYPI--RPGDVLIVISNSGRNAVPIEMALEAKERGLKVIAIT 144
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
3-186 |
2.99e-10 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 58.02 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 3 QDLIRNELNEAAETLANFLkDEANIHAIQRAAVLLADSfkagGKVLSCGNGGSHCDAMHFAeeltgrYRENRPGYPAIAI 82
Cdd:COG1737 98 EDILAKVLEAEIANLEETL-ELLDEEALERAVDLLAKA----RRIYIFGVGASAPVAEDLA------YKLLRLGKNVVLL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 83 SDVSHIscvgndfgydhiFSRYVEAVGrEGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRV 162
Cdd:COG1737 167 DGDGHL------------QAESAALLG-PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYV 233
|
170 180
....*....|....*....|....*
gi 494972086 163 PHFGYADRIQEIHIKV-IHILIQLI 186
Cdd:COG1737 234 PSEEPTLRSSAFSSRVaQLALIDAL 258
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
111-163 |
1.88e-07 |
|
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: 48.73 E-value: 1.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 494972086 111 EGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVP 163
Cdd:cd05005 75 PGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIP 127
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
110-164 |
8.96e-07 |
|
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: 46.00 E-value: 8.96e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 494972086 110 REGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVPH 164
Cdd:cd05014 46 TPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPV 100
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
107-160 |
9.22e-07 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 47.83 E-value: 9.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 494972086 107 AVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEI 160
Cdd:PRK11337 183 ALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
101-158 |
1.62e-06 |
|
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: 45.18 E-value: 1.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 494972086 101 FSRYVEAVGREGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADV 158
Cdd:cd05008 36 EFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADY 93
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
110-168 |
5.76e-06 |
|
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: 43.83 E-value: 5.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494972086 110 REGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIR---VPHFGYA 168
Cdd:pfam01380 52 DEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYinaGPETGVA 113
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
111-163 |
1.65e-05 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 44.05 E-value: 1.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 494972086 111 EGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVP 163
Cdd:cd05007 118 ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALI 170
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
50-145 |
9.77e-05 |
|
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: 39.66 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 50 CGNGGSHCDAMHFAEELtgryrENRPGYPAIAISDVshiscvgndfGYDHIFSRyveAVGREGDVLLGISTSGNSGNVIK 129
Cdd:cd04795 4 IGIGGSGAIAAYFALEL-----LELTGIEVVALIAT----------ELEHASLL---SLLRKGDVVIALSYSGRTEELLA 65
|
90
....*....|....*.
gi 494972086 130 AIDAARAKGMKVITLT 145
Cdd:cd04795 66 ALEIAKELGIPVIAIT 81
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
111-163 |
1.41e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 41.31 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 494972086 111 EGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVP 163
Cdd:PRK05441 131 AKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVV 183
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
110-163 |
1.42e-04 |
|
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: 41.50 E-value: 1.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 494972086 110 REGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRVP 163
Cdd:COG0794 90 TPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLP 143
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
24-162 |
1.08e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 38.90 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 24 EANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTgryrenrpgyPAIAISDVSHISCVGNdfGYDHIFsR 103
Cdd:PRK12570 38 EKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASECP----------PTFSVSPEMVIGLIAG--GPEAMF-T 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494972086 104 YVEA------VGREG---------DVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDGGKMAGTADVEIRV 162
Cdd:PRK12570 105 AVEGaeddpeLGAQDlkaigltadDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISP 178
|
|
| PRK14101 |
PRK14101 |
bifunctional transcriptional regulator/glucokinase; |
21-186 |
3.06e-03 |
|
bifunctional transcriptional regulator/glucokinase;
Pssm-ID: 184507 [Multi-domain] Cd Length: 638 Bit Score: 37.59 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 21 LKDEANIHAIQRAAVLLADSFKAggKVLSCGNGGSHCDAMHfaeeltgrYRENRPGYPAIAISDVshiscvgndfgydhi 100
Cdd:PRK14101 449 LREHLNFEHVEQAIDILNNARRI--EFYGLGNSNIVAQDAH--------YKFFRFGIPTIAYGDL--------------- 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494972086 101 fsrYVEAVGR----EGDVLLGISTSGNSGNVIKAIDAARAKGMKVITLTGKDgGKMAGTADVEIRVPHFgyadRIQEIHI 176
Cdd:PRK14101 504 ---YMQAASAallgKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSSN-TPLAKRATVALETDHI----EMRESQL 575
|
170
....*....|
gi 494972086 177 KVIHILIQLI 186
Cdd:PRK14101 576 SMISRILHLV 585
|
|
| |
