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Conserved domains on  [gi|549579165|gb|ERN83913|]
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transcriptional regulator [Salmonella enterica subsp. enterica serovar Kentucky str. 20793]

Protein Classification

MurR/RpiR family transcriptional regulator( domain architecture ID 11485394)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
5-282 0e+00

MurR/RpiR family transcriptional regulator;


:

Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 531.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   5 IRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASNPNPHSVP 84
Cdd:PRK11557   1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  85 VHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVE 164
Cdd:PRK11557  81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 165 RDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISS 244
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 549579165 245 THAQMMLTDLLFMALVQQDLERAPERIRHSEALVKKLV 282
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
 
Name Accession Description Interval E-value
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
5-282 0e+00

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 531.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   5 IRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASNPNPHSVP 84
Cdd:PRK11557   1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  85 VHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVE 164
Cdd:PRK11557  81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 165 RDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISS 244
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 549579165 245 THAQMMLTDLLFMALVQQDLERAPERIRHSEALVKKLV 282
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 1-281 4.41e-82

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 248.69  E-value: 4.41e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   1 MNCLIRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASNPNP 80
Cdd:COG1737    5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  81 HSvpVHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGIN 160
Cdd:COG1737   85 YE--RLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 161 AV-VERDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRS 239
Cdd:COG1737  163 VVlLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 549579165 240 AAISSTHAQMMLTDLLFMALVQQDLERAPERIRHSEALVKKL 281
Cdd:COG1737  243 SAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 120-258 1.17e-32

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: 116.94  E-value: 1.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 120 EKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVERDMHALLATVQALAPEDLLLAISYSGERRELNLAA 199
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 549579165 200 DETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISSTHAQMMLTDLLFMA 258
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 1-76 1.01e-28

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: 104.72  E-value: 1.01e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549579165    1 MNCLIRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALAS 76
Cdd:pfam01418   1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
G6PI_arch TIGR02128
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ...
 134-240 4.29e-05

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: 44.35  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  134 RIVITGIGASGLVAQNF-AWKLLKIGINAVVERDMHALLATVQAlapEDLLLAISYSGERRELNLAADETLRAGAKILAI 212
Cdd:TIGR02128  23 EIVICGMGGSGIAGRIIsILLLEKSFQGPVFVVKDYRLPRFVDG---KTLLIAVSYSGNTEETLSAVEEAKKKGAKVIAI 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 549579165  213 TgfSPNALQQRATRC---LYTIAEEQATRSA 240
Cdd:TIGR02128 100 T--SGGRLEEMAKERgldVIKIPKGLQPRAA 128
 
Name Accession Description Interval E-value
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
5-282 0e+00

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 531.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   5 IRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASNPNPHSVP 84
Cdd:PRK11557   1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  85 VHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVE 164
Cdd:PRK11557  81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 165 RDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISS 244
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 549579165 245 THAQMMLTDLLFMALVQQDLERAPERIRHSEALVKKLV 282
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 1-281 4.41e-82

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 248.69  E-value: 4.41e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   1 MNCLIRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASNPNP 80
Cdd:COG1737    5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  81 HSvpVHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGIN 160
Cdd:COG1737   85 YE--RLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 161 AV-VERDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRS 239
Cdd:COG1737  163 VVlLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 549579165 240 AAISSTHAQMMLTDLLFMALVQQDLERAPERIRHSEALVKKL 281
Cdd:COG1737  243 SAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
1-281 1.28e-56

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 183.36  E-value: 1.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   1 MNCLIRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASN--- 77
Cdd:PRK15482   1 MLYLTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSASrek 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  78 PNPHSVPVHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKI 157
Cdd:PRK15482  81 TNATALHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 158 GINAVVERDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQAT 237
Cdd:PRK15482 161 GYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEW 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 549579165 238 RSAAISSTHAQMMLTDLLFMALVQQDLERAPERIRHSEALVKKL 281
Cdd:PRK15482 241 RSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSELTQRL 284
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
6-281 4.70e-38

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 135.66  E-value: 4.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   6 RIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASNpnphSVPV 85
Cdd:PRK11337  18 YIRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQS----EQVL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  86 HNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVER 165
Cdd:PRK11337  94 HSELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYD 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 166 DMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISST 245
Cdd:PRK11337 174 DAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGENAAAR 253

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 549579165 246 HAQMMLTDLLFMALVQQDLERAPERIRHSEALVKKL 281
Cdd:PRK11337 254 IAQLNILDAFFVSVAQLNIEQAEINLQKTGAAVDFF 289
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 120-258 1.17e-32

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: 116.94  E-value: 1.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 120 EKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVERDMHALLATVQALAPEDLLLAISYSGERRELNLAA 199
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 549579165 200 DETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISSTHAQMMLTDLLFMA 258
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
6-279 5.23e-32

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 124.26  E-value: 5.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   6 RIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASnpnphSVPV 85
Cdd:PRK14101 346 RIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTG-----TIPM 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  86 -HNQIRGDDPMRLVGEKLIKENVAAMHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVE 164
Cdd:PRK14101 421 sHSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAY 500

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 165 RDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGfSPNALQQRATRCLYTIAEEQATRSAAISS 244
Cdd:PRK14101 501 GDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITS-SNTPLAKRATVALETDHIEMRESQLSMIS 579

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 549579165 245 THAQMMLTDLLFMALVqqdLERAPERIRHSEALVK 279
Cdd:PRK14101 580 RILHLVMIDILAVGVA---IRRAAPNAELAEAVAR 611
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 1-76 1.01e-28

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: 104.72  E-value: 1.01e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549579165    1 MNCLIRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALAS 76
Cdd:pfam01418   1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 128-258 4.45e-28

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: 104.69  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  128 MLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVERDMHALLATVQALA-PEDLLLAISYSGERRELNLAADETLRAG 206
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVdEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 549579165  207 AKILAITGFSPNALQQRATRCLYTIAEEQaTRSAAISSTHAQMMLTDLLFMA 258
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPE-TGVASTKSITAQLAALDALAVA 131
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 1-255 1.90e-23

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 96.60  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165   1 MNCLIRIRQRYPDLAQSDRKLADYLLAQPDTARHLSSQQLAAEAGVSQSSVVKFAQKLGFKGFPALKLAISEALASNPnP 80
Cdd:PRK11302   1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANGT-P 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  81 HsvpVHNQIRGDDPMRLVGEKLIKENVAAM---HATLDVNSEEKlleSVTMLRHARRIVITGIGASGLVAQNFAWKLLKI 157
Cdd:PRK11302  80 Y---VNRNVEEDDSVEAYTGKIFESAMASLdhaRQSLDPSAINR---AVDLLTQAKKISFFGLGASAAVAHDAQNKFFRF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 158 GINAVVERD--MHALLATVQALApeDLLLAISYSGERRELNLAADETLRAGAKILAITgfSPNA-LQQRATRCLYTIAEE 234
Cdd:PRK11302 154 NVPVVYFDDivMQRMSCMNSSDG--DVVVLISHTGRTKSLVELAQLARENGATVIAIT--SAGSpLAREATLALTLDVPE 229

                        250       260
                 ....*....|....*....|.
gi 549579165 235 QATRSAAISSTHAQMMLTDLL 255
Cdd:PRK11302 230 DTDIYMPMVSRIAQLTVIDVL 250
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 110-224 1.48e-16

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: 75.69  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 110 MHATLDVNSEEKLLESVTMLRHARRIVITGIGASGLVAQNFAWKLLKIGINAVVERDMhallaTVQALAPEDLLLAISYS 189
Cdd:cd05005   11 IENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGET-----TTPAIGPGDLLIAISGS 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 549579165 190 GERRELNLAADETLRAGAKILAITGFSPNALQQRA 224
Cdd:cd05005   86 GETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLA 120
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 133-258 2.11e-14

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: 68.34  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 133 RRIVITGIGASGLVAQNFAWKLLKIGINAVVERDMHALLATVQALAPEDLLLAISYSGERRELnLAADETLRA-GAKILA 211
Cdd:cd05014    1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDEL-LNLLPHLKRrGAPIIA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 549579165 212 ITGFSPNALQQRATRCL-YTIAEEQATRS-AAISSTHAQMMLTDLLFMA 258
Cdd:cd05014   80 ITGNPNSTLAKLSDVVLdLPVEEEACPLGlAPTTSTTAMLALGDALAVA 128
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 105-259 1.86e-11

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: 63.46  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 105 ENVAAMHATLDvnseEKLLESVTMLRHAR-RIVITGIGASGLVAQNFAWKLLKIGINAVVerdMHAllatVQA------- 176
Cdd:COG0794   20 EALAALAERLD----ESFEKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGTPAFF---LHP----AEAshgdlgm 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 177 LAPEDLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYTIAEEQATRS--AAISSTHAQMMLTDL 254
Cdd:COG0794   89 ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREACPLnlAPTTSTTATLALGDA 168


                 ....*
gi 549579165 255 LFMAL 259
Cdd:COG0794  169 LAVAL 173
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 135-213 4.02e-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.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 55.46  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 135 IVITGIGASGLVAQNFAWKLLKI-GINAVVERDMHALLA-TVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAI 212
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATELEHAsLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 .
gi 549579165 213 T 213
Cdd:cd04795   81 T 81
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
134-262 5.81e-08

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 52.85  E-value: 5.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 134 RIVITGIGASGLVAQNFAWKLLKIGINAVVERDMHALLATVQALAPEDLLLAISYSGERRELNLAADETLRAGAKILAIT 213
Cdd:PRK11543  44 KVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMT 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 549579165 214 GFSPNALQQRATRCLYTIAEEQA--TRSAAISSTHAQMMLTDLLFMALVQQ 262
Cdd:PRK11543 124 GKPTSPLGLAAKAVLDISVEREAcpMHLAPTSSTVNTLMMGDALAMAVMQA 174
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 134-226 7.78e-08

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: 49.96  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 134 RIVITGIGASGLVAQNF-AWKLLKIGINAVVERDMHaLLATVqalAPEDLLLAISYSGERRELNLAADETLRAGAKILAI 212
Cdd:cd05017    1 NIVILGMGGSGIGGDLLeSLLLDEAKIPVYVVKDYT-LPAFV---DRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAI 76

                         90
                 ....*....|....
gi 549579165 213 TgfSPNALQQRATR 226
Cdd:cd05017   77 T--SGGKLLEMARE 88
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 108-273 1.39e-06

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: 48.74  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 108 AAMHATLDVNSE--EKLLESVTMlRHARRIVITGIGASGLVAQnfawkLLKIGINAVVERDMHALLATVQALAPE----- 180
Cdd:COG2222    9 EAWRRALAALAAaiAALLARLRA-KPPRRVVLVGAGSSDHAAQ-----AAAYLLERLLGIPVAALAPSELVVYPAylkle 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 181 -DLLLAISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLYT-IAEEQ---ATRSAaissthAQMMLTDLL 255
Cdd:COG2222   83 gTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLpAGPEKsvaATKSF------TTMLLALLA 156

                        170       180
                 ....*....|....*....|....
gi 549579165 256 FMALVQQD------LERAPERIRH 273
Cdd:COG2222  157 LLAAWGGDdallaaLDALPAALEA 180
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 128-213 4.31e-06

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 47.28  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 128 MLRHARRIVITGIGASGLV---AQNFAWKLLKIGInaVVERDMHaLLATVqalAPEDLLLAISYSGERRELNLAADETLR 204
Cdd:PRK08674  30 DLEKIDNIVISGMGGSGIGgdlLRILLFDELKVPV--FVNRDYT-LPAFV---DEKTLVIAVSYSGNTEETLSAVEQALK 103


                 ....*....
gi 549579165 205 AGAKILAIT 213
Cdd:PRK08674 104 RGAKIIAIT 112
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 134-259 1.54e-05

SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.


Pssm-ID: 240141 [Multi-domain]  Cd Length: 126  Bit Score: 43.64  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 134 RIVITGIGAS---GLVAQNFAWKLLKIGINAV--VERDMHALLatvqaLAPEDLLLAISYSGERRELNLAADETLRAGAK 208
Cdd:cd05008    1 RILIVGCGTSyhaALVAKYLLERLAGIPVEVEaaSEFRYRRPL-----LDEDTLVIAISQSGETADTLAALRLAKEKGAK 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 549579165 209 ILAITGFSPNALQQRATRCLYTIA-EEQAtrSAAISSTHAQMMLtdLLFMAL 259
Cdd:cd05008   76 TVAITNVVGSTLAREADYVLYLRAgPEIS--VAATKAFTSQLLA--LLLLAL 123
G6PI_arch TIGR02128
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ...
 134-240 4.29e-05

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: 44.35  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165  134 RIVITGIGASGLVAQNF-AWKLLKIGINAVVERDMHALLATVQAlapEDLLLAISYSGERRELNLAADETLRAGAKILAI 212
Cdd:TIGR02128  23 EIVICGMGGSGIAGRIIsILLLEKSFQGPVFVVKDYRLPRFVDG---KTLLIAVSYSGNTEETLSAVEEAKKKGAKVIAI 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 549579165  213 TgfSPNALQQRATRC---LYTIAEEQATRSA 240
Cdd:TIGR02128 100 T--SGGRLEEMAKERgldVIKIPKGLQPRAA 128
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 129-229 1.56e-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: 41.34  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 129 LRHARRIVITGIGASGLVAQNFAWKLLKigiNAVVER----------DMHALLAT-------------VQALA-PEDLLL 184
Cdd:cd05006   30 LLNGGKILICGNGGSAADAQHFAAELVK---RFEKERpglpaialttDTSILTAIandygyeevfsrqVEALGqPGDVLI 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 549579165 185 AISYSGERRELNLAADETLRAGAKILAITGFSPNALQQRATRCLY 229
Cdd:cd05006  107 GISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIH 151
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 129-213 5.82e-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: 38.07  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549579165 129 LRHARRIVITGIGAS---GLVAQNFAWKLLKIGINAVV--E---RDMhallatvqALAPEDLLLAISYSGErrelnlAAD 200
Cdd:COG0449  291 LRNIDRIYIVACGTSyhaGLVGKYLIEELARIPVEVEIasEfryRDP--------VVDPGTLVIAISQSGE------TAD 356

                         90       100
                 ....*....|....*....|
gi 549579165 201 eTLRA-------GAKILAIT 213
Cdd:COG0449  357 -TLAAlreakekGAKVLAIC 375
 
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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