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Conserved domains on  [gi|1004804859|gb|AMP60742|]
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phosphoheptose isomerase [Enterococcus faecium]

Protein Classification

SIS domain-containing protein( domain architecture ID 10785231)

SIS (sugar isomerase) domain-containing protein similar to Fusobacterium nucleatum phosphoheptose isomerase (GmhA) that 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 COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
2-215 1.19e-69

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


:

Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 210.74  E-value: 1.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   2 LAEKLNKHIDLLIKrypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadkl 81
Cdd:COG0279     5 IKQYFEESIEALQA---LAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERP--------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  82 vaidpvrgpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARAL 161
Cdd:COG0279    73 -----------------GLPAIALTTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARER 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1004804859 162 GIKVIGLTGAKGGELATVADVCVKAPEVETYMIQEYHLPIYHCWCLMLEDKFFG 215
Cdd:COG0279   136 GMTTIALTGRDGGKLAGLADIEIRVPSDSTARIQEVHLLIIHILCELIEAALFG 189
 
Name Accession Description Interval E-value
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
2-215 1.19e-69

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 210.74  E-value: 1.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   2 LAEKLNKHIDLLIKrypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadkl 81
Cdd:COG0279     5 IKQYFEESIEALQA---LAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERP--------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  82 vaidpvrgpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARAL 161
Cdd:COG0279    73 -----------------GLPAIALTTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARER 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1004804859 162 GIKVIGLTGAKGGELATVADVCVKAPEVETYMIQEYHLPIYHCWCLMLEDKFFG 215
Cdd:COG0279   136 GMTTIALTGRDGGKLAGLADIEIRVPSDSTARIQEVHLLIIHILCELIEAALFG 189
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 9-210 2.38e-60

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: 186.95  E-value: 2.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   9 HIDLLIKrypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadklvaidpvr 88
Cdd:cd05006     4 SIQLKEA---LLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERP---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  89 gpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGL 168
Cdd:cd05006    65 ----------GLPAIALTTDTSILTAIANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIAL 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1004804859 169 TGAKGGELATVADVCVKAPEVETYMIQEYHLPIYHCWCLMLE 210
Cdd:cd05006   135 TGRDGGKLLELADIEIHVPSDDTPRIQEVHLLIGHILCELVE 176
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 1-217 1.99e-52

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 166.96  E-value: 1.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   1 MLAEKLNKHIDLLIKrypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadk 80
Cdd:PRK13937    1 LITKHFRESQAVMEA---FLESLLEAIAKVAEALIEALANGGKILLCGNGGSAADAQHIAAELVGRFKKERP-------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  81 lvaidpvrgpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARA 160
Cdd:PRK13937   70 ------------------ALPAIALTTDTSALTAIGNDYGFERVFSRQVEALGRPGDVLIGISTSGNSPNVLAALEKARE 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1004804859 161 LGIKVIGLTGAKGGELATVADVCVKAPEVETYMIQEYHLPIYHCWCLMLEDKFFGNE 217
Cdd:PRK13937  132 LGMKTIGLTGRDGGKMKELCDHLLIVPSDDTPRIQEMHITIGHILCDLVERALFEKV 188
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 10-170 1.06e-17

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: 76.09  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  10 IDLLIKRypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadklvaIDPvrg 89
Cdd:pfam13580   6 VRALLER--VVETQADAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPI-----------LLP--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  90 pelaknlecgltaiPLVAHEALSTAYINDVDGLGVFAQQL--FGFGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIG 167
Cdd:pfam13580  70 --------------ALALHTDASATISTALERDEGYARQIlaLYPGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIA 135


                  ...
gi 1004804859 168 LTG 170
Cdd:pfam13580 136 LTS 138
 
Name Accession Description Interval E-value
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
2-215 1.19e-69

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 210.74  E-value: 1.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   2 LAEKLNKHIDLLIKrypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadkl 81
Cdd:COG0279     5 IKQYFEESIEALQA---LAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERP--------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  82 vaidpvrgpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARAL 161
Cdd:COG0279    73 -----------------GLPAIALTTDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARER 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1004804859 162 GIKVIGLTGAKGGELATVADVCVKAPEVETYMIQEYHLPIYHCWCLMLEDKFFG 215
Cdd:COG0279   136 GMTTIALTGRDGGKLAGLADIEIRVPSDSTARIQEVHLLIIHILCELIEAALFG 189
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 9-210 2.38e-60

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: 186.95  E-value: 2.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   9 HIDLLIKrypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadklvaidpvr 88
Cdd:cd05006     4 SIQLKEA---LLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERP---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  89 gpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGL 168
Cdd:cd05006    65 ----------GLPAIALTTDTSILTAIANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIAL 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1004804859 169 TGAKGGELATVADVCVKAPEVETYMIQEYHLPIYHCWCLMLE 210
Cdd:cd05006   135 TGRDGGKLLELADIEIHVPSDDTPRIQEVHLLIGHILCELVE 176
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 1-217 1.99e-52

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 166.96  E-value: 1.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   1 MLAEKLNKHIDLLIKrypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadk 80
Cdd:PRK13937    1 LITKHFRESQAVMEA---FLESLLEAIAKVAEALIEALANGGKILLCGNGGSAADAQHIAAELVGRFKKERP-------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  81 lvaidpvrgpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARA 160
Cdd:PRK13937   70 ------------------ALPAIALTTDTSALTAIGNDYGFERVFSRQVEALGRPGDVLIGISTSGNSPNVLAALEKARE 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1004804859 161 LGIKVIGLTGAKGGELATVADVCVKAPEVETYMIQEYHLPIYHCWCLMLEDKFFGNE 217
Cdd:PRK13937  132 LGMKTIGLTGRDGGKMKELCDHLLIVPSDDTPRIQEMHITIGHILCDLVERALFEKV 188
PRK13936 PRK13936
phosphoheptose isomerase; Provisional
 1-217 7.10e-41

phosphoheptose isomerase; Provisional


Pssm-ID: 237567  Cd Length: 197  Bit Score: 137.87  E-value: 7.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   1 MLAEKLNKH-IDLLIKRYPTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefad 79
Cdd:PRK13936    2 DLQSRIRQHfEDSIDTKQQAMEVLAPPIAQAVELMVQALLNEGKILACGNGGSAADAQHFSAELLNRFERERP------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  80 klvaidpvrgpelaknlecGLTAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVAR 159
Cdd:PRK13936   75 -------------------SLPAIALTTDTSTLTAIANDYSYNEVFSKQVRALGQPGDVLLAISTSGNSANVIQAIQAAH 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004804859 160 ALGIKVIGLTGAKGGELATV---ADVCVKAPEVETYMIQEYHLPIYHCWCLMLEDKFFGNE 217
Cdd:PRK13936  136 EREMHVVALTGRDGGKMASLllpEDVEIRVPAERTARIQEVHLLAIHCLCDLIDSQLLGSE 196
gmhA PRK00414
D-sedoheptulose 7-phosphate isomerase;
6-210 1.53e-30

D-sedoheptulose 7-phosphate isomerase;


Pssm-ID: 179012 [Multi-domain]  Cd Length: 192  Bit Score: 110.98  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   6 LNKHIDLLIKRYPTLETIKQdIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadklvaid 85
Cdd:PRK00414   10 LNEAAETLANFLKDDANIHA-IQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRP------------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  86 pvrgpelaknlecGLTAIPLVAHEALStAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARALGIKV 165
Cdd:PRK00414   76 -------------GYPAIAISDVSHLS-CVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKV 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1004804859 166 IGLTGAKGGELATVADVCVKAPEVEtYM--IQEYHLPIYHCWCLMLE 210
Cdd:PRK00414  142 ITLTGKDGGKMAGLADIEIRVPHFG-YAdrIQEIHIKVIHILIQLIE 187
PRK10886 PRK10886
DnaA initiator-associating protein DiaA; Provisional
 21-214 1.86e-30

DnaA initiator-associating protein DiaA; Provisional


Pssm-ID: 182811  Cd Length: 196  Bit Score: 111.18  E-value: 1.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  21 ETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadklvaidpvrgpelaknlecGL 100
Cdd:PRK10886   21 EALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERP--------------------------SL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859 101 TAIPLVAHEALSTAYINDVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATV- 179
Cdd:PRK10886   75 PAIALNTDNVVLTAIANDRLHDEVYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLl 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1004804859 180 --ADVCVKAPEVETYMIQEYHLPIYHCWCLMLEDKFF 214
Cdd:PRK10886  155 gpQDVEIRIPSHRSARIQEMHMLTVNCLCDLIDNTLF 191
PRK13938 PRK13938
phosphoheptose isomerase; Provisional
 38-215 2.42e-26

phosphoheptose isomerase; Provisional


Pssm-ID: 139997 [Multi-domain]  Cd Length: 196  Bit Score: 100.58  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  38 YLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadklvaidpvrgpelaknlecGLTAIPLVAHEALSTAYIN 117
Cdd:PRK13938   42 YRAGARVFMCGNGGSAADAQHFAAELTGHLIFDRP--------------------------PLGAEALHANSSHLTAVAN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859 118 DVDGLGVFAQQLFGFGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKAPEVETYMIQEY 197
Cdd:PRK13938   96 DYDYDTVFARALEGSARPGDTLFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEFADFLINVPSRDTGRIQES 175

                         170
                  ....*....|....*...
gi 1004804859 198 HLPIYHCWCLMLEDKFFG 215
Cdd:PRK13938  176 HIVFIHAISEHVEHALFA 193
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 10-170 1.06e-17

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: 76.09  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  10 IDLLIKRypTLETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAGELMKRFKTPRPvskefadklvaIDPvrg 89
Cdd:pfam13580   6 VRALLER--VVETQADAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPI-----------LLP--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  90 pelaknlecgltaiPLVAHEALSTAYINDVDGLGVFAQQL--FGFGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIG 167
Cdd:pfam13580  70 --------------ALALHTDASATISTALERDEGYARQIlaLYPGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIA 135


                  ...
gi 1004804859 168 LTG 170
Cdd:pfam13580 136 LTS 138
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 115-194 1.53e-09

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: 54.16  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859 115 YINDVDGLGVFAQQLfgfgRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKAPEVETYMI 194
Cdd:cd05013    44 LLSDPHLQLMSAANL----TPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFR 119
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 136-184 3.02e-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: 51.42  E-value: 3.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1004804859 136 GDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCV 184
Cdd:cd05005    76 GDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 112-194 3.64e-08

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 52.24  E-value: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859 112 STAYINDVDGLGVFAQQLfgfgRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKAPEVET 191
Cdd:COG1737   163 VVLLDGDGHLQAESAALL----GPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEP 238


                  ...
gi 1004804859 192 YMI 194
Cdd:COG1737   239 TLR 241
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 132-184 5.12e-07

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: 49.13  E-value: 5.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1004804859 132 FGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCV 184
Cdd:COG2222    79 LKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL 131
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 131-190 6.85e-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: 46.77  E-value: 6.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859 131 GFGRSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKAPEVE 190
Cdd:cd05014    43 GMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEE 102
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 134-187 1.60e-06

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: 47.66  E-value: 1.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1004804859 134 RSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKAP 187
Cdd:COG0794    90 TPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLP 143
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 134-190 6.95e-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: 6.95e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1004804859 134 RSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKAPEVE 190
Cdd:pfam01380  52 DEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGP 108
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 117-189 2.75e-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: 43.67  E-value: 2.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1004804859 117 NDVDGLGVFAQQLFGFGrSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKA---PEV 189
Cdd:cd05007   101 EDDEEAGAADLQAINLT-ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALitgPEV 175
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 135-184 5.08e-05

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: 41.33  E-value: 5.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1004804859 135 SGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCV 184
Cdd:cd05008    46 EDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVL 95
PRK02947 PRK02947
sugar isomerase domain-containing protein;
7-182 1.58e-04

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 41.39  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859   7 NKHIDLLIKRYPTL-ETIKQDIIDGYLIMEECYLNGGKLLVAGNGGSAADSEHIAgelmkrfktPRpvskefADKLVAID 85
Cdd:PRK02947    5 DEYFDAVIELLERVrETQAEAIEKAADLIADSIRNGGLIYVFGTGHSHILAEEVF---------YR------AGGLAPVN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004804859  86 PVRGPELaknlecgltaipLVAHEALSTAYINDVDGLGVFAQQLFGFgRSGDVFLGISTSGNSKNIMSATVVARALGIKV 165
Cdd:PRK02947   70 PILEPSL------------MLHEGAVASSYLERVEGYAKAILDRYDI-RPGDVLIVVSNSGRNPVPIEMALEAKERGAKV 136

                         170       180
                  ....*....|....*....|....*...
gi 1004804859 166 IGLTG-----------AKGGELATVADV 182
Cdd:PRK02947  137 IAVTSlaysasvasrhSSGKRLAEVADV 164
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
136-196 2.22e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 41.28  E-value: 2.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004804859 136 GDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKAPEVETYMIQE 196
Cdd:PRK11337  188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGE 248
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 143-184 3.30e-03

A subgroup of the 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: 240214 [Multi-domain]  Cd Length: 120  Bit Score: 36.40  E-value: 3.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1004804859 143 STSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCV 184
Cdd:cd05710    55 SHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 135-189 5.25e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 37.07  E-value: 5.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1004804859 135 SGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTGAKGGELATVADVCVKA---PEV 189
Cdd:PRK05441  131 AKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVvvgPEV 188
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 134-193 6.65e-03

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 36.51  E-value: 6.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1004804859 134 RSGDVFLGISTSGNSKNIMSATVVARALGIKVIGLTgAKGGELA---TVAdVCVKAPE-VETYM 193
Cdd:PRK11302  174 SDGDVVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPLAreaTLA-LTLDVPEdTDIYM 235
 
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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