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Conserved domains on  [gi|1033036283|ref|WP_064352017|]
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MurR/RpiR family transcriptional regulator [Klebsiella oxytoca]

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 ...
 4-241 4.49e-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: 4.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283   4 HAAIASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEPQ------- 76
Cdd:COG1737    12 RARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSyerlrrl 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  77 QANIGASEIMSFFKSINNDEFDQL--------LEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPY 147
Cdd:COG1737    92 SPDDSLEDILAKVLEAEIANLEETlelldeeaLERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGH 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 148 FPVT--NDMARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIP 225
Cdd:COG1737   172 LQAEsaALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVA 250

                         250
                  ....*....|....*.
gi 1033036283 226 VIYILETLGRKLARKL 241
Cdd:COG1737   251 QLALIDALAAAVAQRD 266
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 4-241 4.49e-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: 4.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283   4 HAAIASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEPQ------- 76
Cdd:COG1737    12 RARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSyerlrrl 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  77 QANIGASEIMSFFKSINNDEFDQL--------LEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPY 147
Cdd:COG1737    92 SPDDSLEDILAKVLEAEIANLEETlelldeeaLERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGH 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 148 FPVT--NDMARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIP 225
Cdd:COG1737   172 LQAEsaALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVA 250

                         250
                  ....*....|....*.
gi 1033036283 226 VIYILETLGRKLARKL 241
Cdd:COG1737   251 QLALIDALAAAVAQRD 266
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 101-233 9.78e-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: 110.78  E-value: 9.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 101 LEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVT--NDMARNALAIVLSVSGETEEILRFASQ 178
Cdd:cd05013     3 LEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMsaANLTPGDVVIAISFSGETKETVEAAEI 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1033036283 179 FSLHRCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIPVIYILETL 233
Cdd:cd05013    83 AKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRS-SAFSSRIAQLALIDAL 136
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
7-205 2.23e-14

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 70.94  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283   7 IASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNE------------ 74
Cdd:PRK11337   23 QEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEqvlhselsfdda 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  75 PQQA-----NIGASEIMSFFKSINNDEFDqlleQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFP 149
Cdd:PRK11337  103 PQDVvnkvfNTSLQAIEETQSILDVDEFH----RAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIM 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1033036283 150 VTND--MARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADFNL 205
Cdd:PRK11337  179 LMSAalLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 9-72 1.53e-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: 1.53e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033036283   9 SLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQ 72
Cdd:pfam01418  13 KLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
G6PI_arch TIGR02128
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ...
 96-201 7.84e-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: 37.03  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  96 EFDQLLEQAV--DIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHI--DDPYFPVTNDmaRNALAIVLSVSGETEE 171
Cdd:TIGR02128   4 EFLEALDIVNidEILKIYDEIVICGMGGSGIAGRIISILLLEKSFQGPVFvvKDYRLPRFVD--GKTLLIAVSYSGNTEE 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1033036283 172 ILRFASQFSLHRCKVMSITSheHSRLAKLA 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 ...
 4-241 4.49e-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: 4.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283   4 HAAIASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEPQ------- 76
Cdd:COG1737    12 RARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSyerlrrl 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  77 QANIGASEIMSFFKSINNDEFDQL--------LEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPY 147
Cdd:COG1737    92 SPDDSLEDILAKVLEAEIANLEETlelldeeaLERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGH 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 148 FPVT--NDMARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIP 225
Cdd:COG1737   172 LQAEsaALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVA 250

                         250
                  ....*....|....*.
gi 1033036283 226 VIYILETLGRKLARKL 241
Cdd:COG1737   251 QLALIDALAAAVAQRD 266
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 101-233 9.78e-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: 110.78  E-value: 9.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 101 LEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVT--NDMARNALAIVLSVSGETEEILRFASQ 178
Cdd:cd05013     3 LEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMsaANLTPGDVVIAISFSGETKETVEAAEI 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1033036283 179 FSLHRCKVMSITSHEHSRLAKLADFNLSWHVPQTRIGGvYDITTQIPVIYILETL 233
Cdd:cd05013    83 AKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRS-SAFSSRIAQLALIDAL 136
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
7-205 2.23e-14

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 70.94  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283   7 IASLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNE------------ 74
Cdd:PRK11337   23 QEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEqvlhselsfdda 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  75 PQQA-----NIGASEIMSFFKSINNDEFDqlleQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFP 149
Cdd:PRK11337  103 PQDVvnkvfNTSLQAIEETQSILDVDEFH----RAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIM 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1033036283 150 VTND--MARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADFNL 205
Cdd:PRK11337  179 LMSAalLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
33-213 6.21e-13

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 67.63  E-value: 6.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  33 IRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQNEP---QQANIG--ASEIMSffKSINN---------DEFD 98
Cdd:PRK14101  377 IVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPmshSQVHLGdtATDFGA--KVLDNtvsailqlrEHLN 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  99 -QLLEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVTND--MARNALAIVLSVSGETEEILRF 175
Cdd:PRK14101  455 fEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLYMQAASAalLGKGDVIVAVSKSGRAPELLRV 534

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1033036283 176 ASQFSLHRCKVMSITShEHSRLAKLADFNLSWHVPQTR 213
Cdd:PRK14101  535 LDVAMQAGAKVIAITS-SNTPLAKRATVALETDHIEMR 571
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 82-211 1.55e-12

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: 65.77  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  82 ASEIMSFFKSINnDEFdqllEQAVDIILASE-RIIFVGAGTSGALAKYGARFFSNVGKfsnhiddPYFPV-TND------ 153
Cdd:COG0794    19 AEALAALAERLD-ESF----EKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGT-------PAFFLhPAEashgdl 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 154 --MARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADFNLSWHVPQ 211
Cdd:COG0794    87 gmITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVER 146
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 82-205 1.93e-11

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: 62.61  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  82 ASEIMSFFKSINN--DEFDQLLEQAVDIILAS--ERIIFVGAGTSGALAKYGARFFSNVGKF-------SNHIDDPYFPV 150
Cdd:COG2222     1 AREIAQQPEAWRRalAALAAAIAALLARLRAKppRRVVLVGAGSSDHAAQAAAYLLERLLGIpvaalapSELVVYPAYLK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1033036283 151 TndmaRNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADFNL 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 5.26e-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: 58.32  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 113 RIIFVGAGTSGALAKYGARFFSNVGKFSnhiddpYF--PVT---NDM---ARNALAIVLSVSGETEEILRFASQFSLHRC 184
Cdd:cd05014     2 KVVVTGVGKSGHIARKIAATLSSTGTPA------FFlhPTEalhGDLgmvTPGDVVIAISNSGETDELLNLLPHLKRRGA 75

                          90       100
                  ....*....|....*....|....*..
gi 1033036283 185 KVMSITSHEHSRLAKLADFNLSWHVPQ 211
Cdd:cd05014    76 PIIAITGNPNSTLAKLSDVVLDLPVEE 102
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 113-205 7.89e-11

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: 57.89  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 113 RIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDP----YFPVTNDmaRNALAIVLSVSGETEEILRFASQFSLHRCKVMS 188
Cdd:cd05008     1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAAsefrYRRPLLD--EDTLVIAISQSGETADTLAALRLAKEKGAKTVA 78

                          90
                  ....*....|....*..
gi 1033036283 189 ITSHEHSRLAKLADFNL 205
Cdd:cd05008    79 ITNVVGSTLAREADYVL 95
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 9-72 1.53e-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: 1.53e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033036283   9 SLNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRFKLYLEQ 72
Cdd:pfam01418  13 KLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 107-230 7.34e-10

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: 55.38  E-value: 7.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 107 IILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHI-------DDPYFPVTNDMarnaLAIVLSVSGETEEILRFASQF 179
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVelaselrHGVLALVDEDD----LVIAISYSGETKDLLAAAELA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1033036283 180 SLHRCKVMSITSHEHSRLAKLADFNLSWHV-PQTRIGGVYDITTQIPVIYIL 230
Cdd:pfam01380  77 KARGAKIIAITDSPGSPLAREADHVLYINAgPETGVASTKSITAQLAALDAL 128
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 82-203 4.06e-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: 54.50  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  82 ASEIMSFFKSINNDEFDQLleqaVDIILASERIIFVGAGTSGalakYGARFFSN----VGKFSNHIDDPyfpVTNDMARN 157
Cdd:cd05005     8 LEEIENVADKIDEEELDKL----ISAILNAKRIFVYGAGRSG----LVAKAFAMrlmhLGLNVYVVGET---TTPAIGPG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1033036283 158 ALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLADF 203
Cdd:cd05005    77 DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADV 122
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 10-127 1.16e-08

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 54.23  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  10 LNNLEMMVYHYVIKNRDKVMYMTIRELAEAAGVSTTTVLRFCRKLQCEGYSEFRVRF-------KLYLEQN-------EP 75
Cdd:PRK11302   14 LSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLaqslangTPYVNRNveeddsvEA 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1033036283  76 QQANIGASEIMSFFKSINN-DEfdQLLEQAVDIILASERIIFVGAGTSGALAK 127
Cdd:PRK11302   94 YTGKIFESAMASLDHARQSlDP--SAINRAVDLLTQAKKISFFGLGASAAVAH 144
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 113-191 9.95e-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: 43.41  E-value: 9.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033036283 113 RIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFpVTNDMARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITS 191
Cdd:cd05017     1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYVVKDYT-LPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAITS 78
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 1033036283 114 IIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVTND----MARNALAIVLSVSGETEEILRFASQFSLHRCKVMSI 189
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASllslLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                  .
gi 1033036283 190 T 190
Cdd:cd04795    81 T 81
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 80-202 1.04e-04

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 43.09  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  80 IGASEIMSF-FKSINNDEFDQL--LEQAVDIILASERIIFVGAGTSGALAKYGARFFSNVGKFsNHI--DDPY-FPVTND 153
Cdd:PTZ00295  288 IALSRALNNgGRLSGYNNRVKLggLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCF-NTVqvIDASeLTLYRL 366

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1033036283 154 MARNALAIVLSVSGETEEILRFASQFSLHRCKVMSITSHEHSRLAKLAD 202
Cdd:PTZ00295  367 PDEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTD 415
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
101-230 6.82e-04

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 40.41  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 101 LEQAVDIILASERIIFVGAGTS---GALAKYgarFFSNVGKFSNHID--------DPYfpvtndMARNALAIVLSVSGET 169
Cdd:PRK00331  279 GELADEDLKKIDRIYIVACGTSyhaGLVAKY---LIESLAGIPVEVEiasefryrDPV------LSPKTLVIAISQSGET 349

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033036283 170 E---EILRFASQfslHRCKVMSITSHEHSRLAKLADfnlswHVPQTRIG---GV-----YdiTTQIPVIYIL 230
Cdd:PRK00331  350 AdtlAALRLAKE---LGAKTLAICNVPGSTIARESD-----AVLYTHAGpeiGVastkaF--TAQLAVLYLL 411
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 95-230 7.06e-04

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: 39.42  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  95 DEFDQLLEQAVDIILASERIIFVGAGTSGALAKYGARFFsnVGKFsnHIDDPYFPV-------------TNDM------A 155
Cdd:cd05006    17 EAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAEL--VKRF--EKERPGLPAialttdtsiltaiANDYgyeevfS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 156 R--NALA------IVLSVSGETEEILRfASQFSLHR-CKVMSITSHEHSRLAKLADFNLswHVPQTRIGGVYDIttQIPV 226
Cdd:cd05006    93 RqvEALGqpgdvlIGISTSGNSPNVLK-ALEAAKERgMKTIALTGRDGGKLLELADIEI--HVPSDDTPRIQEV--HLLI 167


                  ....
gi 1033036283 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 2.14e-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: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 113 RIIFVGAGTSGALAKYGARFFSNVGKFS---------NHIDDPYFpvtndmARNALAIVLSVSGETEEIL---RFASQfs 180
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKESKLPvfvynaaefLHTGPKRL------TEKSVVILASHSGNTKETVaaaKFAKE-- 72

                          90       100
                  ....*....|....*....|....*..
gi 1033036283 181 lHRCKVMSITSHEHSRLAKLADFNLSW 207
Cdd:cd05710    73 -KGATVIGLTDDEDSPLAKLADYVIVY 98
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 101-230 2.25e-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: 38.84  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283 101 LEQAVDIILASERIIFVGAGTS---GALAKYgarFFSNVGKfsnhiddpyFPVTNDMA-----------RNALAIVLSVS 166
Cdd:COG0449   284 LNLAAEDLRNIDRIYIVACGTSyhaGLVGKY---LIEELAR---------IPVEVEIAsefryrdpvvdPGTLVIAISQS 351

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033036283 167 GETE---EILRFASQfslHRCKVMSITSHEHSRLAKLADFNLswhvpQTRIG---GV-----YdiTTQIPVIYIL 230
Cdd:COG0449   352 GETAdtlAALREAKE---KGAKVLAICNVVGSTIARESDAVL-----YTHAGpeiGVastkaF--TTQLAALYLL 416
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
31-59 7.62e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 33.56  E-value: 7.62e-03
                          10        20
                  ....*....|....*....|....*....
gi 1033036283  31 MTIRELAEAAGVSTTTVLRFCRKLQCEGY 59
Cdd:pfam13412  16 ISQRELAERLGLSPSTVNRRLKRLEEEGV 44
G6PI_arch TIGR02128
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ...
 96-201 7.84e-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: 37.03  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033036283  96 EFDQLLEQAV--DIILASERIIFVGAGTSGALAKYGARFFSNVGKFSNHI--DDPYFPVTNDmaRNALAIVLSVSGETEE 171
Cdd:TIGR02128   4 EFLEALDIVNidEILKIYDEIVICGMGGSGIAGRIISILLLEKSFQGPVFvvKDYRLPRFVD--GKTLLIAVSYSGNTEE 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1033036283 172 ILRFASQFSLHRCKVMSITSheHSRLAKLA 201
Cdd:TIGR02128  82 TLSAVEEAKKKGAKVIAITS--GGRLEEMA 109
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 101-126 9.15e-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: 9.15e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1033036283 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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