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Conserved domains on  [gi|1603117214|emb|VGG64730|]
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phosphoheptose isomerase 1 [Klebsiella pneumoniae]

Protein Classification

D-sedoheptulose 7-phosphate isomerase( domain architecture ID 10791952)

D-sedoheptulose 7-phosphate isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-manno-heptose 7-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gmhA PRK00414
D-sedoheptulose 7-phosphate isomerase;
1-192 4.85e-156

D-sedoheptulose 7-phosphate isomerase;


:

Pssm-ID: 179012 [Multi-domain]  Cd Length: 192  Bit Score: 428.39  E-value: 4.85e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214   1 MYQDLIRNELNEAAETLANFLQDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
Cdd:PRK00414    1 MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  81 AISDVSHLSCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEI 160
Cdd:PRK00414   81 AISDVSHLSCVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGLADIEI 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1603117214 161 RVPHFGYADRIQEIHIKVIHILIMLIEKEMAK 192
Cdd:PRK00414  161 RVPHFGYADRIQEIHIKVIHILIQLIEKEMVK 192
 
Name Accession Description Interval E-value
gmhA PRK00414
D-sedoheptulose 7-phosphate isomerase;
1-192 4.85e-156

D-sedoheptulose 7-phosphate isomerase;


Pssm-ID: 179012 [Multi-domain]  Cd Length: 192  Bit Score: 428.39  E-value: 4.85e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214   1 MYQDLIRNELNEAAETLANFLQDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
Cdd:PRK00414    1 MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  81 AISDVSHLSCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEI 160
Cdd:PRK00414   81 AISDVSHLSCVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGLADIEI 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1603117214 161 RVPHFGYADRIQEIHIKVIHILIMLIEKEMAK 192
Cdd:PRK00414  161 RVPHFGYADRIQEIHIKVIHILIQLIEKEMVK 192
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
3-190 1.67e-99

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 285.47  E-value: 1.67e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214   3 QDLIRNELNEAAETLANFlqDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI 82
Cdd:COG0279     2 LDRIKQYFEESIEALQAL--AEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  83 -SDVSHLSCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIR 161
Cdd:COG0279    80 tTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGLADIEIR 159
                         170       180
                  ....*....|....*....|....*....
gi 1603117214 162 VPHfGYADRIQEIHIKVIHILIMLIEKEM 190
Cdd:COG0279   160 VPS-DSTARIQEVHLLIIHILCELIEAAL 187
gmhA TIGR00441
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ...
34-187 1.51e-97

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: 279.44  E-value: 1.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  34 AVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHLSCVSNDFGYEYVFSRYVESVGRAG 112
Cdd:TIGR00441   1 VVLLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSaDVSHLTCVSNDYGYEDVFSRQVEALGQKG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1603117214 113 DVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPHFgYADRIQEIHIKVIHILIMLIE 187
Cdd:TIGR00441  81 DVLLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGLADIELRVPHF-YTPRIQEIHIKVIHILCQLIE 154
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
10-188 5.87e-82

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: 240.49  E-value: 5.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  10 LNEAAETLANFLQDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHL 88
Cdd:cd05006     1 FQESIQLKEALLELLAE--AIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTtDTSIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  89 SCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPHFGYA 168
Cdd:cd05006    79 TAIANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPSDDTP 158
                         170       180
                  ....*....|....*....|
gi 1603117214 169 dRIQEIHIKVIHILIMLIEK 188
Cdd:cd05006   159 -RIQEVHLLIGHILCELVEE 177
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
10-146 1.12e-31

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: 111.53  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  10 LNEAAETLANFLQDEAniHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI---SDVS 86
Cdd:pfam13580   3 LDEVRALLERVVETQA--DAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALhtdASAT 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  87 HLSCVSNDFGYEYVFSRYVEsvGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTG 146
Cdd:pfam13580  81 ISTALERDEGYARQILALYP--GRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
 
Name Accession Description Interval E-value
gmhA PRK00414
D-sedoheptulose 7-phosphate isomerase;
1-192 4.85e-156

D-sedoheptulose 7-phosphate isomerase;


Pssm-ID: 179012 [Multi-domain]  Cd Length: 192  Bit Score: 428.39  E-value: 4.85e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214   1 MYQDLIRNELNEAAETLANFLQDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
Cdd:PRK00414    1 MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  81 AISDVSHLSCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEI 160
Cdd:PRK00414   81 AISDVSHLSCVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGLADIEI 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1603117214 161 RVPHFGYADRIQEIHIKVIHILIMLIEKEMAK 192
Cdd:PRK00414  161 RVPHFGYADRIQEIHIKVIHILIQLIEKEMVK 192
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
3-190 1.67e-99

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 285.47  E-value: 1.67e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214   3 QDLIRNELNEAAETLANFlqDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI 82
Cdd:COG0279     2 LDRIKQYFEESIEALQAL--AEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  83 -SDVSHLSCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIR 161
Cdd:COG0279    80 tTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGLADIEIR 159
                         170       180
                  ....*....|....*....|....*....
gi 1603117214 162 VPHfGYADRIQEIHIKVIHILIMLIEKEM 190
Cdd:COG0279   160 VPS-DSTARIQEVHLLIIHILCELIEAAL 187
gmhA TIGR00441
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ...
34-187 1.51e-97

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: 279.44  E-value: 1.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  34 AVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHLSCVSNDFGYEYVFSRYVESVGRAG 112
Cdd:TIGR00441   1 VVLLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSaDVSHLTCVSNDYGYEDVFSRQVEALGQKG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1603117214 113 DVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPHFgYADRIQEIHIKVIHILIMLIE 187
Cdd:TIGR00441  81 DVLLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGLADIELRVPHF-YTPRIQEIHIKVIHILCQLIE 154
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
10-188 5.87e-82

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: 240.49  E-value: 5.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  10 LNEAAETLANFLQDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHL 88
Cdd:cd05006     1 FQESIQLKEALLELLAE--AIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTtDTSIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  89 SCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPHFGYA 168
Cdd:cd05006    79 TAIANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPSDDTP 158
                         170       180
                  ....*....|....*....|
gi 1603117214 169 dRIQEIHIKVIHILIMLIEK 188
Cdd:cd05006   159 -RIQEVHLLIGHILCELVEE 177
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
5-192 9.81e-75

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 222.81  E-value: 9.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214   5 LIRNELNEAAETLANFLqdEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS- 83
Cdd:PRK13937    1 LITKHFRESQAVMEAFL--ESLLEAIAKVAEALIEALANGGKILLCGNGGSAADAQHIAAELVGRFKKERPALPAIALTt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  84 DVSHLSCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVP 163
Cdd:PRK13937   79 DTSALTAIGNDYGFERVFSRQVEALGRPGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIVP 158
                         170       180
                  ....*....|....*....|....*....
gi 1603117214 164 HFGYAdRIQEIHIKVIHILIMLIEKEMAK 192
Cdd:PRK13937  159 SDDTP-RIQEMHITIGHILCDLVERALFE 186
PRK13936 PRK13936
phosphoheptose isomerase; Provisional
11-187 2.70e-64

phosphoheptose isomerase; Provisional


Pssm-ID: 237567  Cd Length: 197  Bit Score: 196.80  E-value: 2.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  11 NEAAETLANFlqdeanihaIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI-SDVSHLS 89
Cdd:PRK13936   19 QQAMEVLAPP---------IAQAVELMVQALLNEGKILACGNGGSAADAQHFSAELLNRFERERPSLPAIALtTDTSTLT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  90 CVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMA---GSADVEIRVPHFG 166
Cdd:PRK13936   90 AIANDYSYNEVFSKQVRALGQPGDVLLAISTSGNSANVIQAIQAAHEREMHVVALTGRDGGKMAsllLPEDVEIRVPAER 169
                         170       180
                  ....*....|....*....|.
gi 1603117214 167 YAdRIQEIHIKVIHILIMLIE 187
Cdd:PRK13936  170 TA-RIQEVHLLAIHCLCDLID 189
PRK10886 PRK10886
DnaA initiator-associating protein DiaA; Provisional
24-190 8.66e-45

DnaA initiator-associating protein DiaA; Provisional


Pssm-ID: 182811  Cd Length: 196  Bit Score: 147.00  E-value: 8.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  24 EANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAIS-DVSHLSCVSNDFGYEYVFS 102
Cdd:PRK10886   21 EALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNtDNVVLTAIANDRLHDEVYA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214 103 RYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMA---GSADVEIRVPHFGYAdRIQEIHIKVI 179
Cdd:PRK10886  101 KQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAgllGPQDVEIRIPSHRSA-RIQEMHMLTV 179
                         170
                  ....*....|.
gi 1603117214 180 HILIMLIEKEM 190
Cdd:PRK10886  180 NCLCDLIDNTL 190
PRK13938 PRK13938
phosphoheptose isomerase; Provisional
15-190 1.52e-38

phosphoheptose isomerase; Provisional


Pssm-ID: 139997 [Multi-domain]  Cd Length: 196  Bit Score: 131.01  E-value: 1.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  15 ETLA---NFLQDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI-SDVSHLSC 90
Cdd:PRK13938   13 ETIAvktRILNDRVLLEAARAIGDRLIAGYRAGARVFMCGNGGSAADAQHFAAELTGHLIFDRPPLGAEALhANSSHLTA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  91 VSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPHFGyADR 170
Cdd:PRK13938   93 VANDYDYDTVFARALEGSARPGDTLFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEFADFLINVPSRD-TGR 171
                         170       180
                  ....*....|....*....|
gi 1603117214 171 IQEIHIKVIHILIMLIEKEM 190
Cdd:PRK13938  172 IQESHIVFIHAISEHVEHAL 191
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
10-146 1.12e-31

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: 111.53  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  10 LNEAAETLANFLQDEAniHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI---SDVS 86
Cdd:pfam13580   3 LDEVRALLERVVETQA--DAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALhtdASAT 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  87 HLSCVSNDFGYEYVFSRYVEsvGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTG 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 ...
29-184 2.48e-11

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: 58.78  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  29 AIQRAAVLLADSfkagGKVLSCGNGGSHCDAMHFAeeltgrYRENRPGYPAIAISDVSHLSCVSNDFGyeyvfsryvesv 108
Cdd:cd05013     2 ALEKAVDLLAKA----RRIYIFGVGSSGLVAEYLA------YKLLRLGKPVVLLSDPHLQLMSAANLT------------ 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1603117214 109 grAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPHFGYADRIQEIHIKVIHILIM 184
Cdd:cd05013    60 --PGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALI 133
PRK02947 PRK02947
sugar isomerase domain-containing protein;
10-145 2.61e-11

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 60.65  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  10 LNEAAETLANFLQDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCdamhFAEELTGRYrenrPGYP---AIAISDVS 86
Cdd:PRK02947    8 FDAVIELLERVRETQAE--AIEKAADLIADSIRNGGLIYVFGTGHSHI----LAEEVFYRA----GGLApvnPILEPSLM 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1603117214  87 HLSCVSNDFGYEYV---FSRYVESVG-RAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLT 145
Cdd:PRK02947   78 LHEGAVASSYLERVegyAKAILDRYDiRPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVT 140
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
3-186 5.92e-11

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 59.94  E-value: 5.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214   3 QDLIRNELNEAAETLANFLQdEANIHAIQRAAVLLADSfkagGKVLSCGNGGSHCDAMHFAeeltgrYRENRPGYPAIAI 82
Cdd:COG1737    98 EDILAKVLEAEIANLEETLE-LLDEEALERAVDLLAKA----RRIYIFGVGASAPVAEDLA------YKLLRLGKNVVLL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  83 SDVSHLscvsndfgyeyvFSRYVESVGrAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRV 162
Cdd:COG1737   167 DGDGHL------------QAESAALLG-PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYV 233
                         170       180
                  ....*....|....*....|....*....
gi 1603117214 163 PHFGYADRIQEI-----HIKVIHILIMLI 186
Cdd:COG1737   234 PSEEPTLRSSAFssrvaQLALIDALAAAV 262
COG4821 COG4821
Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain ...
10-145 1.92e-09

Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain [General function prediction only];


Pssm-ID: 443849 [Multi-domain]  Cd Length: 250  Bit Score: 55.21  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  10 LNEAAETLANFLQDEANihAIQRAAVLLADSFKAGGKVLSCGNGGSHCdamhFAEELTGRYrenrPGYPAI-AISDVSHL 88
Cdd:COG4821     9 LDEVRELLDRIEETQAE--AIEKAADLIADSIAAGGLVHLFGTGHSHL----LAEEVFYRA----GGLVGFnPILDPSLM 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1603117214  89 scVSNDFGYEYVFSRY--VESVG---------RAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLT 145
Cdd:COG4821    79 --LHNGAPGVLQSSFLerVEGYAeiilenypiRPGDVLIVISNSGRNAVPIEMALEAKERGLKVIAIT 144
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
111-163 3.35e-08

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: 51.04  E-value: 3.35e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1603117214 111 AGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVP 163
Cdd:cd05005    75 PGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIP 127
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
112-160 2.45e-07

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 49.37  E-value: 2.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1603117214 112 GDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEI 160
Cdd:PRK11337  188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
110-164 7.93e-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: 46.38  E-value: 7.93e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1603117214 110 RAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPH 164
Cdd:cd05014    46 TPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPV 100
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
100-158 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 1603117214 100 VFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADV 158
Cdd:cd05008    35 SEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADY 93
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
110-168 4.40e-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: 44.21  E-value: 4.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1603117214 110 RAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIR---VPHFGYA 168
Cdd:pfam01380  52 DEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYinaGPETGVA 113
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
24-163 1.30e-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: 44.44  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  24 EANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRP--------GYPAIAISDVshlscvsndf 95
Cdd:cd05007    29 EAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPErvvgliagGEPALTRAVE---------- 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1603117214  96 GYEYVFSRYVESVGRAG----DVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVP 163
Cdd:cd05007    99 GAEDDEEAGAADLQAINlterDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALI 170
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
50-145 2.58e-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: 41.21  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  50 CGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHLScvsndfgyeyvfsryvesVGRAGDVLLGISTSGNSGNVIK 129
Cdd:cd04795     4 IGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLS------------------LLRKGDVVIALSYSGRTEELLA 65
                          90
                  ....*....|....*.
gi 1603117214 130 AIEAARAQGMKVITLT 145
Cdd:cd04795    66 ALEIAKELGIPVIAIT 81
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
111-163 3.56e-05

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 43.23  E-value: 3.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1603117214 111 AGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVP 163
Cdd:PRK05441  131 AKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVV 183
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
110-163 1.55e-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: 41.12  E-value: 1.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1603117214 110 RAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVP 163
Cdd:COG0794    90 TPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLP 143
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
110-145 2.62e-03

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 37.76  E-value: 2.62e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1603117214 110 RAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLT 145
Cdd:PRK15482  181 KKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAIT 216
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
24-162 3.08e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 37.36  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  24 EANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRY---------------------RENRPGYPAIAI 82
Cdd:PRK12570   38 EKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASECPPTFsvspemvigliaggpeamftaVEGAEDDPELGA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  83 SDVSHLSCVSNDfgyeyvfsryvesvgragdVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRV 162
Cdd:PRK12570  118 QDLKAIGLTADD-------------------VVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISP 178
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
99-183 3.13e-03

Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 36.75  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  99 YVFSRYVESVGRAGDVLLgistsgnSGNVIKAIEAARAQGMKVITLTGkdGGKMAGSAdveIRvphfgyADRIQEIHIKV 178
Cdd:COG0262    70 IVLSRTLDEADWEGVTVV-------SGDLEEALAALKAAGGKDIWVIG--GGELYRQL---LP------AGLVDELYLTV 131

                  ....*
gi 1603117214 179 IHILI 183
Cdd:COG0262   132 VPVVL 136
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
21-186 3.42e-03

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 37.59  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214  21 LQDEANIHAIQRAAVLLADSFKAggKVLSCGNGGSHCDAMHfaeeltgrYRENRPGYPAIAISDvSHLSCVSNDFgyeyv 100
Cdd:PRK14101  449 LREHLNFEHVEQAIDILNNARRI--EFYGLGNSNIVAQDAH--------YKFFRFGIPTIAYGD-LYMQAASAAL----- 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603117214 101 fsryvesVGRaGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDgGKMAGSADVEIRVPHFGYADRIQEIHIKVIH 180
Cdd:PRK14101  513 -------LGK-GDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSSN-TPLAKRATVALETDHIEMRESQLSMISRILH 583

                  ....*.
gi 1603117214 181 ILIMLI 186
Cdd:PRK14101  584 LVMIDI 589
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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