NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489117107|ref|WP_003026952|]
View 

MULTISPECIES: MurR/RpiR family transcriptional regulator [Citrobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 4-240 3.00e-55

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


:

Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 178.58  E-value: 3.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107   4 HAAIASLNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEFRVRFKLYLEQNEPQ------- 76
Cdd:COG1737   12 RARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSyerlrrl 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  77 QANFGASEIISFFKGVNNDEFDKL--------LDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPY 147
Cdd:COG1737   92 SPDDSLEDILAKVLEAEIANLEETlelldeeaLERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGH 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 148 FPVT--NDMARNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADFNLSWHVPQTRIAGvYDITTQIP 225
Cdd:COG1737  172 LQAEsaALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVA 250

                        250
                 ....*....|....*
gi 489117107 226 VIYILESLGRKLAKR 240
Cdd:COG1737  251 QLALIDALAAAVAQR 265
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 4-240 3.00e-55

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 178.58  E-value: 3.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107   4 HAAIASLNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEFRVRFKLYLEQNEPQ------- 76
Cdd:COG1737   12 RARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSyerlrrl 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  77 QANFGASEIISFFKGVNNDEFDKL--------LDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPY 147
Cdd:COG1737   92 SPDDSLEDILAKVLEAEIANLEETlelldeeaLERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGH 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 148 FPVT--NDMARNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADFNLSWHVPQTRIAGvYDITTQIP 225
Cdd:COG1737  172 LQAEsaALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVA 250

                        250
                 ....*....|....*
gi 489117107 226 VIYILESLGRKLAKR 240
Cdd:COG1737  251 QLALIDALAAAVAQR 265
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 101-233 7.72e-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: 7.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 101 LDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVT--NDMARNALAIVLSVSGETEEILRFASQ 178
Cdd:cd05013    3 LEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMsaANLTPGDVVIAISFSGETKETVEAAEI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489117107 179 FSLHNCKVLSVTSHENSRLAKLADFNLSWHVPQTRIaGVYDITTQIPVIYILESL 233
Cdd:cd05013   83 AKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDF-RSSAFSSRIAQLALIDAL 136
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
5-213 7.80e-14

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 70.33  E-value: 7.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107   5 AAIASLNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEFRVRFKLYLEQNEP--------- 75
Cdd:PRK14101 349 QMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPmshsqvhlg 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  76 -QQANFGA-------SEIISFFKGVNNDEFdkllDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPY 147
Cdd:PRK14101 429 dTATDFGAkvldntvSAILQLREHLNFEHV----EQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLY 504

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489117107 148 FPVTND--MARNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTShENSRLAKLADFNLSWHVPQTR 213
Cdd:PRK14101 505 MQAASAalLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITS-SNTPLAKRATVALETDHIEMR 571
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 107-230 5.83e-12

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: 61.16  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  107 IILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHI-------DDPYFPVTNDMarnaLAIVLSVSGETEEILRFASQF 179
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVelaselrHGVLALVDEDD----LVIAISYSGETKDLLAAAELA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489117107  180 SLHNCKVLSVTSHENSRLAKLADFNLSWHV-PQTRIAGVYDITTQIPVIYIL 230
Cdd:pfam01380  77 KARGAKIIAITDSPGSPLAREADHVLYINAgPETGVASTKSITAQLAALDAL 128
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 4-240 3.00e-55

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 178.58  E-value: 3.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107   4 HAAIASLNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEFRVRFKLYLEQNEPQ------- 76
Cdd:COG1737   12 RARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSyerlrrl 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  77 QANFGASEIISFFKGVNNDEFDKL--------LDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHID-DPY 147
Cdd:COG1737   92 SPDDSLEDILAKVLEAEIANLEETlelldeeaLERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDgDGH 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 148 FPVT--NDMARNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADFNLSWHVPQTRIAGvYDITTQIP 225
Cdd:COG1737  172 LQAEsaALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS-SAFSSRVA 250

                        250
                 ....*....|....*
gi 489117107 226 VIYILESLGRKLAKR 240
Cdd:COG1737  251 QLALIDALAAAVAQR 265
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 101-233 7.72e-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: 7.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 101 LDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVT--NDMARNALAIVLSVSGETEEILRFASQ 178
Cdd:cd05013    3 LEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMsaANLTPGDVVIAISFSGETKETVEAAEI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489117107 179 FSLHNCKVLSVTSHENSRLAKLADFNLSWHVPQTRIaGVYDITTQIPVIYILESL 233
Cdd:cd05013   83 AKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDF-RSSAFSSRIAQLALIDAL 136
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
5-213 7.80e-14

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 70.33  E-value: 7.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107   5 AAIASLNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEFRVRFKLYLEQNEP--------- 75
Cdd:PRK14101 349 QMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPmshsqvhlg 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  76 -QQANFGA-------SEIISFFKGVNNDEFdkllDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPY 147
Cdd:PRK14101 429 dTATDFGAkvldntvSAILQLREHLNFEHV----EQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLY 504

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489117107 148 FPVTND--MARNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTShENSRLAKLADFNLSWHVPQTR 213
Cdd:PRK14101 505 MQAASAalLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITS-SNTPLAKRATVALETDHIEMR 571
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 93-205 3.13e-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: 64.92  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  93 NNDEFDKLLDQAVDiiLSSERIIFVGAGTSGALAKYGARFFSNVGKF-------SNHIDDPYFPVTndmaRNALAIVLSV 165
Cdd:COG2222   18 LAAAIAALLARLRA--KPPRRVVLVGAGSSDHAAQAAAYLLERLLGIpvaalapSELVVYPAYLKL----EGTLVVAISR 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489117107 166 SGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADFNL 205
Cdd:COG2222   92 SGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL 131
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 94-211 3.32e-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: 64.61  E-value: 3.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  94 NDEFDklldQAVDIILSSE-RIIFVGAGTSGALAKYGARFFSNVGKfsnhiddPYFPV-TND--------MARNALAIVL 163
Cdd:COG0794   30 DESFE----KAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGT-------PAFFLhPAEashgdlgmITPGDVVIAI 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489117107 164 SVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADFNLSWHVPQ 211
Cdd:COG0794   99 SNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVER 146
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 107-230 5.83e-12

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: 61.16  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  107 IILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHI-------DDPYFPVTNDMarnaLAIVLSVSGETEEILRFASQF 179
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVelaselrHGVLALVDEDD----LVIAISYSGETKDLLAAAELA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489117107  180 SLHNCKVLSVTSHENSRLAKLADFNLSWHV-PQTRIAGVYDITTQIPVIYIL 230
Cdd:pfam01380  77 KARGAKIIAITDSPGSPLAREADHVLYINAgPETGVASTKSITAQLAALDAL 128
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 113-205 2.38e-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: 59.43  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 113 RIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDP----YFPVTNDmaRNALAIVLSVSGETEEILRFASQFSLHNCKVLS 188
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAAsefrYRRPLLD--EDTLVIAISQSGETADTLAALRLAKEKGAKTVA 78

                         90
                 ....*....|....*..
gi 489117107 189 VTSHENSRLAKLADFNL 205
Cdd:cd05008   79 ITNVVGSTLAREADYVL 95
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 113-211 4.85e-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: 58.71  E-value: 4.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 113 RIIFVGAGTSGALAKYGARFFSNVGKFSnhiddpYF--PVT---NDM---ARNALAIVLSVSGETEEILRFASQFSLHNC 184
Cdd:cd05014    2 KVVVTGVGKSGHIARKIAATLSSTGTPA------FFlhPTEalhGDLgmvTPGDVVIAISNSGETDELLNLLPHLKRRGA 75

                         90       100
                 ....*....|....*....|....*..
gi 489117107 185 KVLSVTSHENSRLAKLADFNLSWHVPQ 211
Cdd:cd05014   76 PIIAITGNPNSTLAKLSDVVLDLPVEE 102
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
7-205 1.38e-10

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 59.77  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107   7 IASLNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEFRVRFKLYLEQN--------EPQQA 78
Cdd:PRK11337  23 QEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSeqvlhselSFDDA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  79 N-------FGAS-----EIISFfkgVNNDEFDKlldqAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDP 146
Cdd:PRK11337 103 PqdvvnkvFNTSlqaieETQSI---LDVDEFHR----AARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489117107 147 YFPVTND--MARNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADFNL 205
Cdd:PRK11337 176 HIMLMSAalLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 82-203 1.57e-10

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: 58.36  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  82 ASEIISFFKGVNNDEfdklLDQAVDIILSSERIIFVGAGTSGalakYGARFFSN----VGKFSNHIDDPyfpVTNDMARN 157
Cdd:cd05005    8 LEEIENVADKIDEEE----LDKLISAILNAKRIFVYGAGRSG----LVAKAFAMrlmhLGLNVYVVGET---TTPAIGPG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489117107 158 ALAIVLSVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADF 203
Cdd:cd05005   77 DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADV 122
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 9-72 2.21e-09

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: 52.72  E-value: 2.21e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489117107    9 SLNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEFRVRFKLYLEQ 72
Cdd:pfam01418  13 KLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 113-232 6.81e-07

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: 46.87  E-value: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 113 RIIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFpVTNDMARNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTSh 192
Cdd:cd05017    1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYVVKDYT-LPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAITS- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489117107 193 eNSRLAKLADFN--LSWHVP---QTRIAGVYDITtqiPVIYILES 232
Cdd:cd05017   79 -GGKLLEMAREHgvPVIIIPkglQPRAAFPYLFT---ALLNILNK 119
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 82-202 9.64e-07

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 49.25  E-value: 9.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  82 ASEIISF-FKGVNNDEFDKL--LDQAVDIILSSERIIFVGAGTSGALAKYGARFFSNVGKFsNHI--DDPY-FPVTNDMA 155
Cdd:PTZ00295 290 LSRALNNgGRLSGYNNRVKLggLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCF-NTVqvIDASeLTLYRLPD 368

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489117107 156 RNALAIVLSVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLAD 202
Cdd:PTZ00295 369 EDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTD 415
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 10-211 5.19e-06

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 46.53  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  10 LNNLEMLVYNYVIKNRDKVMYMTIRELADAVGVSTTTVLRFCRKLKCEGYSEfrvrFKLYLEQ---------NEPQQANF 80
Cdd:PRK11302  14 LSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPD----FKLHLAQslangtpyvNRNVEEDD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  81 GASE--------IISFFKGVNNDEFDKLLDQAVDIILSSERIIFVGAGTSGALAKYGA-RFFS-NVgkfsnhiddpyfPV 150
Cdd:PRK11302  90 SVEAytgkifesAMASLDHARQSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQnKFFRfNV------------PV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489117107 151 T--ND--MAR----NA----LAIVLSVSGETEEILRFASQFSLHNCKVLSVTShENSRLAKLADFNLSWHVPQ 211
Cdd:PRK11302 158 VyfDDivMQRmscmNSsdgdVVVLISHTGRTKSLVELAQLARENGATVIAITS-AGSPLAREATLALTLDVPE 229
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
101-230 2.55e-04

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 41.57  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 101 LDQAVDIILSSERIIFVGAGTS---GALAKYgarFFSNVGKFSNHID--------DPYfpvtndMARNALAIVLSVSGET 169
Cdd:PRK00331 279 GELADEDLKKIDRIYIVACGTSyhaGLVAKY---LIESLAGIPVEVEiasefryrDPV------LSPKTLVIAISQSGET 349

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489117107 170 E---EILRFASQfslHNCKVLSVTSHENSRLAKLADfnlswHVPQTRiAGVyDI--------TTQIPVIYIL 230
Cdd:PRK00331 350 AdtlAALRLAKE---LGAKTLAICNVPGSTIARESD-----AVLYTH-AGP-EIgvastkafTAQLAVLYLL 411
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 113-207 3.14e-04

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: 39.48  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 113 RIIFVGAGTSGALAKYGARFFSNVGKFS---------NHIDDPYFpvtndmARNALAIVLSVSGETEEIL---RFASQfs 180
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESKLPvfvynaaefLHTGPKRL------TEKSVVILASHSGNTKETVaaaKFAKE-- 72

                         90       100
                 ....*....|....*....|....*..
gi 489117107 181 lHNCKVLSVTSHENSRLAKLADFNLSW 207
Cdd:cd05710   73 -KGATVIGLTDDEDSPLAKLADYVIVY 98
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 114-190 6.51e-04

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: 37.74  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 114 IIFVGAGTSGALAKYGARFFSNVGKFSNHIDDPYFPVTND----MARNALAIVLSVSGETEEILRFASQFSLHNCKVLSV 189
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASllslLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 .
gi 489117107 190 T 190
Cdd:cd04795   81 T 81
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 95-230 8.69e-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: 39.03  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  95 DEFDKLLDQAVDIILSSERIIFVGAGTSGALAKYgarfFSN--VGKFsnHIDDPYFPV-------------TNDM----- 154
Cdd:cd05006   17 EAIEQAAQLLAEALLNGGKILICGNGGSAADAQH----FAAelVKRF--EKERPGLPAialttdtsiltaiANDYgyeev 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 155 -AR--NALA------IVLSVSGETEEILRfASQFSL-HNCKVLSVTSHENSRLAKLADFNLswHVPQTRIAGVYDIttQI 224
Cdd:cd05006   91 fSRqvEALGqpgdvlIGISTSGNSPNVLK-ALEAAKeRGMKTIALTGRDGGKLLELADIEI--HVPSDDTPRIQEV--HL 165


                 ....*.
gi 489117107 225 PVIYIL 230
Cdd:cd05006  166 LIGHIL 171
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 101-205 1.12e-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: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107 101 LDQAVDIILSSERIIFVGAGTS---GALAKYgarFFSNVGKfsnhiddpyFPVTNDMA-----------RNALAIVLSVS 166
Cdd:COG0449  284 LNLAAEDLRNIDRIYIVACGTSyhaGLVGKY---LIEELAR---------IPVEVEIAsefryrdpvvdPGTLVIAISQS 351

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489117107 167 GETE---EILRFASQfslHNCKVLSVTSHENSRLAKLADFNL 205
Cdd:COG0449  352 GETAdtlAALREAKE---KGAKVLAICNVVGSTIARESDAVL 390
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
31-59 2.09e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 35.10  E-value: 2.09e-03
                          10        20
                  ....*....|....*....|....*....
gi 489117107   31 MTIRELADAVGVSTTTVLRFCRKLKCEGY 59
Cdd:pfam13412  16 ISQRELAERLGLSPSTVNRRLKRLEEEGV 44
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
94-211 2.75e-03

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 38.17  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  94 NDEFDklldQAVDIILSSE-RIIFVGAGTSGALAKYGARFFSNVGKfsnhiddPYFPVTNDMARNA---------LAIVL 163
Cdd:PRK10892  33 NQDFT----LACEKMFWCKgKVVVMGMGKSGHIGRKMAATFASTGT-------PSFFVHPGEAAHGdlgmvtpqdVVIAI 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489117107 164 SVSGETEEILRFASQFSLHNCKVLSVTSHENSRLAKLADFNLSWHVPQ 211
Cdd:PRK10892 102 SNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADIHLCVKVPK 149
HTH_AsnC-type pfam13404
AsnC-type helix-turn-helix domain;
31-55 6.89e-03

AsnC-type helix-turn-helix domain;


Pssm-ID: 433180 [Multi-domain]  Cd Length: 41  Bit Score: 33.50  E-value: 6.89e-03
                          10        20
                  ....*....|....*....|....*
gi 489117107   31 MTIRELADAVGVSTTTVLRFCRKLK 55
Cdd:pfam13404  17 ISFAELAERVGLSESTVLRRIRRLE 41
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 97-234 7.34e-03

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 36.88  E-value: 7.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117107  97 FDKLLDQAVDIILSS---------ERIIFVGAGTSGAlakyGARFFSNVGKFSNHIddPYFPVTNDM-----ARNALAIV 162
Cdd:PRK08674  11 WPEQFEEALEIAISLdleedlekiDNIVISGMGGSGI----GGDLLRILLFDELKV--PVFVNRDYTlpafvDEKTLVIA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489117107 163 LSVSGETEEILRFASQFSLHNCKVLSVTSheNSRLAKLADFNLSWH--VP---QTRIAGVYDITtqiPVIYILESLG 234
Cdd:PRK08674  85 VSYSGNTEETLSAVEQALKRGAKIIAITS--GGKLKEMAKEHGLPViiVPggyQPRAALGYLFT---PLLKILEKLG 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH