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Conserved domains on  [gi|489005730|ref|WP_002916321|]
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MULTISPECIES: MurR/RpiR family transcriptional regulator [Klebsiella]

Protein Classification

MurR/RpiR family transcriptional regulator( domain architecture ID 11448252)

MurR/RpiR family transcriptional regulator similar to Escherichia coli MurR, which represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid

CATH:  1.10.10.10
Gene Ontology:  GO:0006355|GO:0003700|GO:0003677
PubMed:  15808743|8576032
SCOP:  4000148

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 8-240 3.99e-56

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


:

Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 180.51  E-value: 3.99e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730   8 ASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEPQQANIG------ 81
Cdd:COG1737   16 PSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYERLRrlspdd 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  82 ---------ASEIMSFFKSVNNDEFDELLEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPYFPVT 151
Cdd:COG1737   96 sledilakvLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGHLQAE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 152 --NDMARNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIPVIYI 229
Cdd:COG1737  176 saALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVAQLAL 254

                        250
                 ....*....|.
gi 489005730 230 LESLGRKLARK 240
Cdd:COG1737  255 IDALAAAVAQR 265
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 8-240 3.99e-56

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 180.51  E-value: 3.99e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730   8 ASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEPQQANIG------ 81
Cdd:COG1737   16 PSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYERLRrlspdd 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  82 ---------ASEIMSFFKSVNNDEFDELLEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPYFPVT 151
Cdd:COG1737   96 sledilakvLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGHLQAE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 152 --NDMARNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIPVIYI 229
Cdd:COG1737  176 saALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVAQLAL 254

                        250
                 ....*....|.
gi 489005730 230 LESLGRKLARK 240
Cdd:COG1737  255 IDALAAAVAQR 265
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 99-233 6.79e-31

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: 111.17  E-value: 6.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  99 ELLEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVT--NDMARNALAIVLSVSGETEEILRFA 176
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMsaANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489005730 177 SQFSLHHCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIPVIYILESL 233
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRS-SAFSSRIAQLALIDAL 136
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
8-205 3.53e-14

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 70.17  E-value: 3.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730   8 ASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNE------------P 75
Cdd:PRK11337  24 EGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEqvlhselsfddaP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  76 QQA-----NIGASEIMSFFKSVNNDEFDelleQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPV 150
Cdd:PRK11337 104 QDVvnkvfNTSLQAIEETQSILDVDEFH----RAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIML 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489005730 151 TND--MARNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNL 205
Cdd:PRK11337 180 MSAalLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 107-230 8.89e-11

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: 58.08  E-value: 8.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  107 IILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHI-------DDPYFPVTNDMarnaLAIVLSVSGETEEILRFASQF 179
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVelaselrHGVLALVDEDD----LVIAISYSGETKDLLAAAELA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489005730  180 SLHHCKVMSITSHEHSRLAKLADFNLSWHV-PQTRIGGVYDITTQIPVIYIL 230
Cdd:pfam01380  77 KARGAKIIAITDSPGSPLAREADHVLYINAgPETGVASTKSITAQLAALDAL 128
G6PI_arch TIGR02128
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ...
 96-201 1.53e-03

bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea.


Pssm-ID: 273988 [Multi-domain]  Cd Length: 308  Bit Score: 38.96  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730   96 EFDELLEQAV--DIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHI--DDPYFPVTNDmaRNALAIVLSVSGETEE 171
Cdd:TIGR02128   4 EFLEALDIVNidEILKIYDEIVICGMGGSGIAGRIISILLLEKSFQGPVFvvKDYRLPRFVD--GKTLLIAVSYSGNTEE 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 489005730  172 ILRFASQFSLHHCKVMSITSheHSRLAKLA 201
Cdd:TIGR02128  82 TLSAVEEAKKKGAKVIAITS--GGRLEEMA 109
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 8-240 3.99e-56

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 180.51  E-value: 3.99e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730   8 ASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEPQQANIG------ 81
Cdd:COG1737   16 PSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYERLRrlspdd 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  82 ---------ASEIMSFFKSVNNDEFDELLEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPYFPVT 151
Cdd:COG1737   96 sledilakvLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGHLQAE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 152 --NDMARNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIPVIYI 229
Cdd:COG1737  176 saALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVAQLAL 254

                        250
                 ....*....|.
gi 489005730 230 LESLGRKLARK 240
Cdd:COG1737  255 IDALAAAVAQR 265
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 99-233 6.79e-31

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: 111.17  E-value: 6.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  99 ELLEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVT--NDMARNALAIVLSVSGETEEILRFA 176
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMsaANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489005730 177 SQFSLHHCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIPVIYILESL 233
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRS-SAFSSRIAQLALIDAL 136
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
8-205 3.53e-14

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 70.17  E-value: 3.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730   8 ASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNE------------P 75
Cdd:PRK11337  24 EGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEqvlhselsfddaP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  76 QQA-----NIGASEIMSFFKSVNNDEFDelleQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPV 150
Cdd:PRK11337 104 QDVvnkvfNTSLQAIEETQSILDVDEFH----RAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIML 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489005730 151 TND--MARNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNL 205
Cdd:PRK11337 180 MSAalLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
33-213 4.77e-13

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 68.02  E-value: 4.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  33 IRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEP---QQANIG--ASEIMSffKSVNND-----EFDELL- 101
Cdd:PRK14101 377 IVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPmshSQVHLGdtATDFGA--KVLDNTvsailQLREHLn 454

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 102 ----EQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVTND--MARNALAIVLSVSGETEEILRF 175
Cdd:PRK14101 455 fehvEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLYMQAASAalLGKGDVIVAVSKSGRAPELLRV 534

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489005730 176 ASQFSLHHCKVMSITShEHSRLAKLADFNLSWHVPQTR 213
Cdd:PRK14101 535 LDVAMQAGAKVIAITS-SNTPLAKRATVALETDHIEMR 571
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 95-211 9.78e-13

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: 66.15  E-value: 9.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  95 DEFDELLEQAVDIILASE-RIIFVGAGTSGALAKYGARFFSNVGKfsnhiddPYFPV-TND--------MARNALAIVLS 164
Cdd:COG0794   27 ERLDESFEKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGT-------PAFFLhPAEashgdlgmITPGDVVIAIS 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489005730 165 VSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNLSWHVPQ 211
Cdd:COG0794  100 NSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVER 146
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 82-205 9.72e-12

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: 63.38  E-value: 9.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  82 ASEIMSFFKSVNN--DEFDELLEQAVDIILAS--ERIIFVGAGTSGALAKYGARFFSNVGKF-------SNHIDDPYFPV 150
Cdd:COG2222    1 AREIAQQPEAWRRalAALAAAIAALLARLRAKppRRVVLVGAGSSDHAAQAAAYLLERLLGIpvaalapSELVVYPAYLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489005730 151 TndmaRNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNL 205
Cdd:COG2222   81 L----EGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL 131
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 113-211 8.15e-11

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: 57.94  E-value: 8.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 113 RIIFVGAGTSGALAKYGARFFSNVGKFSnhiddpYF--PVT---NDM---ARNALAIVLSVSGETEEILRFASQFSLHHC 184
Cdd:cd05014    2 KVVVTGVGKSGHIARKIAATLSSTGTPA------FFlhPTEalhGDLgmvTPGDVVIAISNSGETDELLNLLPHLKRRGA 75

                         90       100
                 ....*....|....*....|....*..
gi 489005730 185 KVMSITSHEHSRLAKLADFNLSWHVPQ 211
Cdd:cd05014   76 PIIAITGNPNSTLAKLSDVVLDLPVEE 102
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 107-230 8.89e-11

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: 58.08  E-value: 8.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  107 IILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHI-------DDPYFPVTNDMarnaLAIVLSVSGETEEILRFASQF 179
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVelaselrHGVLALVDEDD----LVIAISYSGETKDLLAAAELA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489005730  180 SLHHCKVMSITSHEHSRLAKLADFNLSWHV-PQTRIGGVYDITTQIPVIYIL 230
Cdd:pfam01380  77 KARGAKIIAITDSPGSPLAREADHVLYINAgPETGVASTKSITAQLAALDAL 128
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 9-72 1.60e-10

Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best characterized member of this family is Swiss:P39266. RpiR is a regulator of the expression of rpiB gene.


Pssm-ID: 334531 [Multi-domain]  Cd Length: 77  Bit Score: 55.80  E-value: 1.60e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489005730    9 SLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQ 72
Cdd:pfam01418  13 KLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 113-205 3.26e-10

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: 56.35  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 113 RIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDP----YFPVTNDmaRNALAIVLSVSGETEEILRFASQFSLHHCKVMS 188
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAAsefrYRRPLLD--EDTLVIAISQSGETADTLAALRLAKEKGAKTVA 78

                         90
                 ....*....|....*..
gi 489005730 189 ITSHEHSRLAKLADFNL 205
Cdd:cd05008   79 ITNVVGSTLAREADYVL 95
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 82-203 1.27e-09

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: 55.66  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  82 ASEIMSFFKSVNNDEFDELLEQAVDIILASERIIFVGAGTSGalakYGARFFSN----VGKFSNHIDDPyfpVTNDMARN 157
Cdd:cd05005    4 LSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSG----LVAKAFAMrlmhLGLNVYVVGET---TTPAIGPG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489005730 158 ALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADF 203
Cdd:cd05005   77 DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADV 122
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 10-127 3.35e-08

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 53.07  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  10 LNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRF-------KLYLEQN-------EP 75
Cdd:PRK11302  14 LSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLaqslangTPYVNRNveeddsvEA 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489005730  76 QQANIGASEIMSFFKSVNNdeFDE-LLEQAVDIILASERIIFVGAGTSGALAK 127
Cdd:PRK11302  94 YTGKIFESAMASLDHARQS--LDPsAINRAVDLLTQAKKISFFGLGASAAVAH 144
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 113-232 4.76e-06

The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.


Pssm-ID: 240148 [Multi-domain]  Cd Length: 119  Bit Score: 44.56  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 113 RIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFpVTNDMARNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSh 192
Cdd:cd05017    1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYVVKDYT-LPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAITS- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489005730 193 eHSRLAKLADFN--LSWHVP---QTRIGGVYDITtqiPVIYILES 232
Cdd:cd05017   79 -GGKLLEMAREHgvPVIIIPkglQPRAAFPYLFT---ALLNILNK 119
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 114-190 8.99e-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: 40.05  E-value: 8.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 114 IIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVTND----MARNALAIVLSVSGETEEILRFASQFSLHHCKVMSI 189
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASllslLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 .
gi 489005730 190 T 190
Cdd:cd04795   81 T 81
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 82-202 9.32e-05

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 43.09  E-value: 9.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  82 ASEIMSF-FKSVNNDEFDEL--LEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFsNHI--DDPY-FPVTNDMA 155
Cdd:PTZ00295 290 LSRALNNgGRLSGYNNRVKLggLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCF-NTVqvIDASeLTLYRLPD 368

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489005730 156 RNALAIVLSVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLAD 202
Cdd:PTZ00295 369 EDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTD 415
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
98-230 3.59e-04

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 41.18  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  98 DELLEQAVDIILASERIIFVGAGTS---GALAKYgarFFSNVGKFSNHID--------DPYfpvtndMARNALAIVLSVS 166
Cdd:PRK00331 276 LGEGELADEDLKKIDRIYIVACGTSyhaGLVAKY---LIESLAGIPVEVEiasefryrDPV------LSPKTLVIAISQS 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489005730 167 GETE---EILRFASQfslHHCKVMSITSHEHSRLAKLADfnlswHVPQTRIG---GV-----YdiTTQIPVIYIL 230
Cdd:PRK00331 347 GETAdtlAALRLAKE---LGAKTLAICNVPGSTIARESD-----AVLYTHAGpeiGVastkaF--TAQLAVLYLL 411
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 99-230 1.24e-03

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 39.61  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  99 ELLEQAVDIILASERIIFVGAGTS---GALAKYgarFFSNVGKfsnhiddpyFPVTNDMA-----------RNALAIVLS 164
Cdd:COG0449  282 DELNLAAEDLRNIDRIYIVACGTSyhaGLVGKY---LIEELAR---------IPVEVEIAsefryrdpvvdPGTLVIAIS 349

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489005730 165 VSGETE---EILRFASQfslHHCKVMSITSHEHSRLAKLADFNLswhvpQTRIG---GV-----YdiTTQIPVIYIL 230
Cdd:COG0449  350 QSGETAdtlAALREAKE---KGAKVLAICNVVGSTIARESDAVL-----YTHAGpeiGVastkaF--TTQLAALYLL 416
G6PI_arch TIGR02128
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ...
 96-201 1.53e-03

bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea.


Pssm-ID: 273988 [Multi-domain]  Cd Length: 308  Bit Score: 38.96  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730   96 EFDELLEQAV--DIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHI--DDPYFPVTNDmaRNALAIVLSVSGETEE 171
Cdd:TIGR02128   4 EFLEALDIVNidEILKIYDEIVICGMGGSGIAGRIISILLLEKSFQGPVFvvKDYRLPRFVD--GKTLLIAVSYSGNTEE 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 489005730  172 ILRFASQFSLHHCKVMSITSheHSRLAKLA 201
Cdd:TIGR02128  82 TLSAVEEAKKKGAKVIAITS--GGRLEEMA 109
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 99-230 2.15e-03

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: 37.87  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  99 ELLEQAVDIILAS----ERIIFVGAGTSGALAKYGARFFsnVGKFsnHIDDPYFPV-------------TNDM------A 155
Cdd:cd05006   17 EAIEQAAQLLAEAllngGKILICGNGGSAADAQHFAAEL--VKRF--EKERPGLPAialttdtsiltaiANDYgyeevfS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 156 R--NALA------IVLSVSGETEEILRfASQFSLHH-CKVMSITSHEHSRLAKLADFNLswHVPQTRIGGVYDIttQIPV 226
Cdd:cd05006   93 RqvEALGqpgdvlIGISTSGNSPNVLK-ALEAAKERgMKTIALTGRDGGKLLELADIEI--HVPSDDTPRIQEV--HLLI 167


                 ....
gi 489005730 227 IYIL 230
Cdd:cd05006  168 GHIL 171
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 113-207 2.27e-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: 36.79  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730 113 RIIFVGAGTSGALAKYGARFFSNVGKFS---------NHIDDPYFpvtndmARNALAIVLSVSGETEEIL---RFASQfs 180
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESKLPvfvynaaefLHTGPKRL------TEKSVVILASHSGNTKETVaaaKFAKE-- 72

                         90       100
                 ....*....|....*....|....*..
gi 489005730 181 lHHCKVMSITSHEHSRLAKLADFNLSW 207
Cdd:cd05710   73 -KGATVIGLTDDEDSPLAKLADYVIVY 98
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
94-211 2.80e-03

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 38.17  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489005730  94 NDEFdellEQAVDIILASE-RIIFVGAGTSGALAKYGARFFSNVGKfsnhiddPYFPVTNDMARNA---------LAIVL 163
Cdd:PRK10892  33 NQDF----TLACEKMFWCKgKVVVMGMGKSGHIGRKMAATFASTGT-------PSFFVHPGEAAHGdlgmvtpqdVVIAI 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489005730 164 SVSGETEEILRFASQFSLHHCKVMSITSHEHSRLAKLADFNLSWHVPQ 211
Cdd:PRK10892 102 SNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADIHLCVKVPK 149
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
31-59 5.78e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 33.95  E-value: 5.78e-03
                          10        20
                  ....*....|....*....|....*....
gi 489005730   31 MTIRELAEAAGVSTTTVLRFCRKLQCEGY 59
Cdd:pfam13412  16 ISQRELAERLGLSPSTVNRRLKRLEEEGV 44
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 101-126 8.44e-03

N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 36.61  E-value: 8.44e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 489005730 101 LEQAVDII---LASE-RIIFVGAGTSGALA 126
Cdd:COG2103   49 IAAAVDAIaeaLRAGgRLIYVGAGTSGRLG 78
 
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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