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Conserved domains on  [gi|654546546|ref|WP_028014252|]
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MULTISPECIES: MurR/RpiR family transcriptional regulator [Enterobacter]

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 ...
1-256 8.39e-72

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


:

Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 222.11  E-value: 8.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546   1 MSDHENLLLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALALDIQQ 80
Cdd:COG1737    1 MMSAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  81 G----------QPARQAGDEIDSVVDESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLG 150
Cdd:COG1737   81 GlssyerlrrlSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 151 KSAQLFS-DMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPL 229
Cdd:COG1737  161 KNVVLLDgDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTL 240
                        250       260
                 ....*....|....*....|....*..
gi 654546546 230 SAGALNAKVGVMLLVELLTTSMIALDG 256
Cdd:COG1737  241 RSSAFSSRVAQLALIDALAAAVAQRDG 267
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
1-256 8.39e-72

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 222.11  E-value: 8.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546   1 MSDHENLLLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALALDIQQ 80
Cdd:COG1737    1 MMSAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  81 G----------QPARQAGDEIDSVVDESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLG 150
Cdd:COG1737   81 GlssyerlrrlSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 151 KSAQLFS-DMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPL 229
Cdd:COG1737  161 KNVVLLDgDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTL 240
                        250       260
                 ....*....|....*....|....*..
gi 654546546 230 SAGALNAKVGVMLLVELLTTSMIALDG 256
Cdd:COG1737  241 RSSAFSSRVAQLALIDALAAAVAQRDG 267
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
122-247 4.14e-35

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: 123.11  E-value: 4.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 122 HQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLFSDMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKV 201
Cdd:cd05013   11 AKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKV 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654546546 202 LALSNTPRSPLASLSDMLLVAAKPEGPLSAGALNAKVGVMLLVELL 247
Cdd:cd05013   91 IAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDAL 136
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
11-229 1.06e-32

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 121.41  E-value: 1.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  11 LRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMAL--------ALDIQQGQ 82
Cdd:PRK11337  19 IRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALedyfsqseQVLHSELS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  83 PARQAGDEIDSVVDESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLFSDMHRA 162
Cdd:PRK11337  99 FDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIM 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654546546 163 AMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPL 229
Cdd:PRK11337 179 LMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPL 245
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
6-81 1.36e-16

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: 72.75  E-value: 1.36e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654546546    6 NLLLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALALDIQQG 81
Cdd:pfam01418   2 GLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELANS 77
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
1-256 8.39e-72

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 222.11  E-value: 8.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546   1 MSDHENLLLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALALDIQQ 80
Cdd:COG1737    1 MMSAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  81 G----------QPARQAGDEIDSVVDESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLG 150
Cdd:COG1737   81 GlssyerlrrlSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 151 KSAQLFS-DMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPL 229
Cdd:COG1737  161 KNVVLLDgDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTL 240
                        250       260
                 ....*....|....*....|....*..
gi 654546546 230 SAGALNAKVGVMLLVELLTTSMIALDG 256
Cdd:COG1737  241 RSSAFSSRVAQLALIDALAAAVAQRDG 267
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
122-247 4.14e-35

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: 123.11  E-value: 4.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 122 HQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLFSDMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKV 201
Cdd:cd05013   11 AKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKV 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654546546 202 LALSNTPRSPLASLSDMLLVAAKPEGPLSAGALNAKVGVMLLVELL 247
Cdd:cd05013   91 IAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDAL 136
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
11-229 1.06e-32

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 121.41  E-value: 1.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  11 LRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMAL--------ALDIQQGQ 82
Cdd:PRK11337  19 IRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALedyfsqseQVLHSELS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  83 PARQAGDEIDSVVDESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLFSDMHRA 162
Cdd:PRK11337  99 FDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIM 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654546546 163 AMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPL 229
Cdd:PRK11337 179 LMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPL 245
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
5-251 2.22e-27

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 110.78  E-value: 2.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546   5 ENLLLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALALDIQQGQP- 83
Cdd:PRK14101 341 SAVFERIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPm 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  84 -------ARQAGDEIDSVVDESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLF 156
Cdd:PRK14101 421 shsqvhlGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAY 500
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 157 SDMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTpRSPLASLSDMLLVAAKPEGPLSAGALNA 236
Cdd:PRK14101 501 GDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSS-NTPLAKRATVALETDHIEMRESQLSMIS 579
                        250
                 ....*....|....*
gi 654546546 237 KVGVMLLVELLTTSM 251
Cdd:PRK14101 580 RILHLVMIDILAVGV 594
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
5-226 5.66e-27

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 105.85  E-value: 5.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546   5 ENLLLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALALDIQQGQP- 83
Cdd:PRK11302   1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANGTPy 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  84 ARQAGDEIDSV------VDESVQALQDTAR-LLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLF 156
Cdd:PRK11302  81 VNRNVEEDDSVeaytgkIFESAMASLDHARqSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQNKFFRFNVPVVYF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654546546 157 SD--MHR-AAMNATTlsaETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNtPRSPLASLSDMLLVAAKPE 226
Cdd:PRK11302 161 DDivMQRmSCMNSSD---GDVVVLISHTGRTKSLVELAQLARENGATVIAITS-AGSPLAREATLALTLDVPE 229
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
8-255 9.17e-24

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 97.46  E-value: 9.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546   8 LLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALaldIQQGQPARQ- 86
Cdd:PRK15482   4 LTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMAL---IGEYSASREk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  87 -------------AGDEIDSVVD----ESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRL 149
Cdd:PRK15482  81 tnatalhlhssitSDDSLEVIARklnrEKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 150 GKSAQLFSDMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPL 229
Cdd:PRK15482 161 GYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEW 240
                        250       260
                 ....*....|....*....|....*.
gi 654546546 230 SAGALNAKVGVMLLVELLTTSMIALD 255
Cdd:PRK15482 241 RSSSMSTRTAQNSVTDLLFVGLVQLN 266
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
9-259 3.16e-19

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 84.82  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546   9 LKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMAL--ALDIQQGQPARQ 86
Cdd:PRK11557   1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALseALASQPEPPSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  87 AGDEIDS----------VVDESVQALQDTARLLDRALLEKAALALHQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLF 156
Cdd:PRK11557  81 VHNQIRGddplrlvgekLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 157 SDMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPLSAGALNA 236
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240
                        250       260
                 ....*....|....*....|...
gi 654546546 237 KVGVMLLVELLTTSMIALDGHYA 259
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERA 263
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
6-81 1.36e-16

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: 72.75  E-value: 1.36e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654546546    6 NLLLKLRQEASGYSPTQQKLGEFVLSDPARVLYLTITELARESHTSEASVTRLCRTLGCKGYNEFKMALALDIQQG 81
Cdd:pfam01418   2 GLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELANS 77
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
122-250 3.05e-14

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: 67.71  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  122 HQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLFSDMHRAAMN-ATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVK 200
Cdd:pfam01380   3 AKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARGAK 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 654546546  201 VLALSNTPRSPLASLSDMLLVAAKPEGPLSAgALNAKVGVMLLVELLTTS 250
Cdd:pfam01380  83 IIAITDSPGSPLAREADHVLYINAGPETGVA-STKSITAQLAALDALAVA 131
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
169-226 2.75e-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: 2.75e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 654546546 169 LSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDM-LLVAAKPE 226
Cdd:cd05008   44 LDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYvLYLRAGPE 102
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
169-226 6.08e-09

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: 56.17  E-value: 6.08e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 654546546 169 LSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDM-LLVAAKPE 226
Cdd:COG0449  339 VDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAvLYTHAGPE 397
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
169-227 2.00e-08

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: 51.77  E-value: 2.00e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 169 LSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAA-KPEG 227
Cdd:cd05014   45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPvEEEA 104
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
169-226 2.65e-08

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 54.28  E-value: 2.65e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 654546546 169 LSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDM-LLVAAKPE 226
Cdd:PRK00331 334 LSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAvLYTHAGPE 392
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
173-221 3.47e-08

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: 53.75  E-value: 3.47e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 654546546 173 TLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLV 221
Cdd:COG2222   84 TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLP 132
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
89-221 9.28e-08

Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.


Pssm-ID: 240138 [Multi-domain]  Cd Length: 179  Bit Score: 50.65  E-value: 9.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546  89 DEIDSVVDESVQAlqDTARLLDRALlekaalalhQAQSVQIYGVAASAILGEYLHYKLLRLGKSAQLFSDMhraamnaTT 168
Cdd:cd05005    9 EEIENVADKIDEE--ELDKLISAIL---------NAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGET-------TT 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 654546546 169 --LSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLV 221
Cdd:cd05005   71 paIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
127-205 1.22e-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: 49.19  E-value: 1.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654546546 127 VQIYGVAASAILGEYLhYKLLRLGKSAQLFsdMHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALS 205
Cdd:cd05017    2 IVILGMGGSGIGGDLL-ESLLLDEAKIPVY--VVKDYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
169-226 8.36e-07

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: 49.20  E-value: 8.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 654546546 169 LSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPE 226
Cdd:COG0794   89 ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVER 146
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
161-257 2.58e-05

N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.


Pssm-ID: 240140 [Multi-domain]  Cd Length: 257  Bit Score: 44.44  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 161 RAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDM-LLVAAKPEgpLSAGALNAKVG 239
Cdd:cd05007  108 AADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIaIALITGPE--VVAGSTRLKAG 185
                         90       100
                 ....*....|....*....|.
gi 654546546 240 V---MLLVELLTTSMIALdGH 257
Cdd:cd05007  186 TaqkLALNMLSTAVMIRL-GK 205
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
169-221 3.61e-05

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: 42.18  E-value: 3.61e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 654546546 169 LSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLV 221
Cdd:cd05710   45 LTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIV 97
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
129-205 4.54e-05

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 44.20  E-value: 4.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654546546 129 IYGVAASAILGEYLHyKLLRLGKSAQLFSdmHRAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALS 205
Cdd:PRK08674  39 ISGMGGSGIGGDLLR-ILLFDELKVPVFV--NRDYTLPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAIT 112
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
161-217 4.59e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 40.92  E-value: 4.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 654546546 161 RAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSD 217
Cdd:PRK05441 121 AADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEAD 177
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
175-246 1.31e-03

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 40.00  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654546546 175 VVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSD--MLLVAAKPEGPLSAGALNAKVGVMLLVEL 246
Cdd:PTZ00295 373 VIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDcgVYLNAGREVAVASTKAFTSQVTVLSLIAL 446
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
174-229 1.98e-03

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 38.30  E-value: 1.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 654546546 174 LVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLVAAKPEGPL 229
Cdd:PRK13937 109 VLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIVPSDDTPR 164
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
174-221 2.15e-03

Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).


Pssm-ID: 240139 [Multi-domain]  Cd Length: 177  Bit Score: 37.87  E-value: 2.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 654546546 174 LVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDMLLV 221
Cdd:cd05006  104 VLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIH 151
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
161-254 3.46e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 38.13  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 161 RAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLALSNTPRSPLASLSDmllVAAKPE-GP-LSAGALNAKV 238
Cdd:PRK12570 117 AQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIAD---IAISPVvGPeVLTGSTRLKS 193
                         90
                 ....*....|....*....
gi 654546546 239 GV---MLLVELLTTSMIAL 254
Cdd:PRK12570 194 GTaqkMVLNMLSTASMIRL 212
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
127-205 5.28e-03

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: 35.43  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546546 127 VQIYGVAASAILGEYLHYKLLRL-GKSAQLFSDMH-RAAMNATTLSAETLVVAISSSGSTRDLLHVVKLARKRGVKVLAL 204
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATElEHASLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80

                 .
gi 654546546 205 S 205
Cdd:cd04795   81 T 81
 
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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