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Conserved domains on  [gi|1737604106|emb|VAX66794|]
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DNA-binding transcriptional regulator HexR [Enterobacter kobei]

Protein Classification

MurR/RpiR family transcriptional regulator( domain architecture ID 11485311)

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

Gene Ontology:  GO:0006355|GO:0006351|GO:0003677|GO:0003700|GO:0097367

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 31-314 0e+00

DNA-binding transcriptional regulator HexR; Provisional


:

Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 592.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  31 MNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANGTPY 110
Cdd:PRK11302    1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANGTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 111 VNRNVDEDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPVIYS 190
Cdd:PRK11302   81 VNRNVEEDDSVEAYTGKIFESAMASLDHARQSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQNKFFRFNVPVVYF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 191 DDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTTAGTPLAREATLAITLDVPEDTDMYMPMVSR 270
Cdd:PRK11302  161 DDIVMQRMSCMNSSDGDVVVLISHTGRTKSLVELAQLARENGATVIAITSAGSPLAREATLALTLDVPEDTDIYMPMVSR 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1737604106 271 LAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDKELLI 314
Cdd:PRK11302  241 IAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDKDLLN 284
 
Name Accession Description Interval E-value
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 31-314 0e+00

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 592.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  31 MNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANGTPY 110
Cdd:PRK11302    1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANGTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 111 VNRNVDEDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPVIYS 190
Cdd:PRK11302   81 VNRNVEEDDSVEAYTGKIFESAMASLDHARQSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQNKFFRFNVPVVYF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 191 DDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTTAGTPLAREATLAITLDVPEDTDMYMPMVSR 270
Cdd:PRK11302  161 DDIVMQRMSCMNSSDGDVVVLISHTGRTKSLVELAQLARENGATVIAITSAGSPLAREATLALTLDVPEDTDIYMPMVSR 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1737604106 271 LAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDKELLI 314
Cdd:PRK11302  241 IAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDKDLLN 284
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 30-308 2.05e-92

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 276.42  E-value: 2.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  30 TMNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANGTP 109
Cdd:COG1737     4 AMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 110 YVNR--NVDEDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPV 187
Cdd:COG1737    84 SYERlrRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 188 I-YSDDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALT-TAGTPLAREATLAITLDVPEDTDMYM 265
Cdd:COG1737   164 VlLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITdSPLSPLAKLADVVLYVPSEEPTLRSS 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1737604106 266 PMVSRLAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRF 308
Cdd:COG1737   244 AFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELRE 286
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 146-283 9.79e-41

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: 138.90  E-value: 9.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 146 SSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPVIYSDDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELA 225
Cdd:cd05013     1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737604106 226 QLARENDAMVIALTTAGT-PLAREATLAITLDVPEDTDMYMPMVSRLAQLTVIDVLATG 283
Cdd:cd05013    81 EIAKERGAKVIAITDSANsPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 31-107 4.93e-33

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: 117.05  E-value: 4.93e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737604106  31 MNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANG 107
Cdd:pfam01418   1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELANS 77
 
Name Accession Description Interval E-value
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 31-314 0e+00

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 592.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  31 MNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANGTPY 110
Cdd:PRK11302    1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANGTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 111 VNRNVDEDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPVIYS 190
Cdd:PRK11302   81 VNRNVEEDDSVEAYTGKIFESAMASLDHARQSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQNKFFRFNVPVVYF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 191 DDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTTAGTPLAREATLAITLDVPEDTDMYMPMVSR 270
Cdd:PRK11302  161 DDIVMQRMSCMNSSDGDVVVLISHTGRTKSLVELAQLARENGATVIAITSAGSPLAREATLALTLDVPEDTDIYMPMVSR 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1737604106 271 LAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDKELLI 314
Cdd:PRK11302  241 IAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDKDLLN 284
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 30-308 2.05e-92

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 276.42  E-value: 2.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  30 TMNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANGTP 109
Cdd:COG1737     4 AMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 110 YVNR--NVDEDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPV 187
Cdd:COG1737    84 SYERlrRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 188 I-YSDDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALT-TAGTPLAREATLAITLDVPEDTDMYM 265
Cdd:COG1737   164 VlLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITdSPLSPLAKLADVVLYVPSEEPTLRSS 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1737604106 266 PMVSRLAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRF 308
Cdd:COG1737   244 AFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELRE 286
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
4-290 1.23e-64

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 214.78  E-value: 1.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106   4 TGVISANR---MKISSIYEIVSTPTSALLTMNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPT 80
Cdd:PRK14101  311 TYLITAEYpafLGVSAILAEQLSNRTGGASSAVFERIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPT 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  81 VNRFCRSLETRGFPDFKLHLAQSLANGTPYVNRNVDEDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKR 160
Cdd:PRK14101  391 VIRFCRSLGCQGLSDFKLKLATGLTGTIPMSHSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARR 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 161 IAFFGLGSSAAVAHDAMNKFFRFNVPVIYSDDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTT 240
Cdd:PRK14101  471 IEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITS 550

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737604106 241 AGTPLAREATLAITLDVPEDTDMYMPMVSRLAQLTVIDVLATGFTLRRGA 290
Cdd:PRK14101  551 SNTPLAKRATVALETDHIEMRESQLSMISRILHLVMIDILAVGVAIRRAA 600
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
37-307 4.85e-42

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 147.21  E-value: 4.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  37 IQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANGTPYVNRNVD 116
Cdd:PRK11337   19 IRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEQVLHSELS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 117 EDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPVIYSDDIVLQ 196
Cdd:PRK11337   99 FDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHIM 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 197 RMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALT-TAGTPLAREATLAITLDVPEDTDMYMPMVSRLAQLT 275
Cdd:PRK11337  179 LMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITnSYHSPIAKLADYVICSTAQGSPLLGENAAARIAQLN 258

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1737604106 276 VIDVLATGFTLRRGAKFRDNLKRVKEALKESR 307
Cdd:PRK11337  259 ILDAFFVSVAQLNIEQAEINLQKTGAAVDFFR 290
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 146-283 9.79e-41

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: 138.90  E-value: 9.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 146 SSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPVIYSDDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELA 225
Cdd:cd05013     1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737604106 226 QLARENDAMVIALTTAGT-PLAREATLAITLDVPEDTDMYMPMVSRLAQLTVIDVLATG 283
Cdd:cd05013    81 EIAKERGAKVIAITDSANsPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 31-107 4.93e-33

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: 117.05  E-value: 4.93e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737604106  31 MNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLANG 107
Cdd:pfam01418   1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELANS 77
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 154-282 1.08e-26

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: 101.99  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 154 LLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNV-PVIYSDDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLAREND 232
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYkVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1737604106 233 AMVIALT-TAGTPLAREATLAITLDVPEDTdMYMPMVSRLAQLTVIDVLAT 282
Cdd:pfam01380  81 AKIIAITdSPGSPLAREADHVLYINAGPET-GVASTKSITAQLAALDALAV 130
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
44-280 9.82e-25

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 101.00  E-value: 9.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  44 LSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLA-NGTPY---VNRNVDEDD 119
Cdd:PRK11557   10 LAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALAsQPEPPsvpVHNQIRGDD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 120 SVDAYTAKIFESAMATLdhvRQSLDMSS---VNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRFNVPVIYSDDIVLQ 196
Cdd:PRK11557   90 PLRLVGEKLIKENTAAM---RATLDVNSeekLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAERDMHAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 197 RMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTT-AGTPLAREATLAITLDVPEDTDMYMPMVSRLAQLT 275
Cdd:PRK11557  167 LATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGfTPNALQQRASHCLYTIAEEQATRSAAISSTHAQGM 246


                  ....*
gi 1737604106 276 VIDVL 280
Cdd:PRK11557  247 LTDLL 251
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
31-284 9.33e-21

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 90.14  E-value: 9.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106  31 MNMLEKIQYQLEHLSKSERKVAEVILASPAQAIHSSIAALAQEAGVSEPTVNRFCRSLETRGFPDFKLHLAQSLA----- 105
Cdd:PRK15482    1 MLYLTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSasrek 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 106 -NGTP-YVNRNVDEDDSVDAYTAKIFESAMATLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAHDAMNKFFRF 183
Cdd:PRK15482   81 tNATAlHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 184 NVPVIYSDDIVLQRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTT-AGTPLAREATLaiTLD-VPEDT 261
Cdd:PRK15482  161 GYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSlADSPLRRLAHF--TLDtVSGET 238

                         250       260
                  ....*....|....*....|....
gi 1737604106 262 D-MYMPMVSRLAQLTVIDVLATGF 284
Cdd:PRK15482  239 EwRSSSMSTRTAQNSVTDLLFVGL 262
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 124-262 1.83e-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: 59.13  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 124 YTAKIFEsamaTLDHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAhdamnKFF--R-----FNVPVIysDDIVlq 196
Cdd:cd05005     3 YLSLILE----EIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVA-----KAFamRlmhlgLNVYVV--GETT-- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737604106 197 rmsCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTT-AGTPLAREATLAITLDVPEDTD 262
Cdd:cd05005    70 ---TPAIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSnPDSPLAKLADVVVVIPAATKDD 133
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 160-259 4.05e-10

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


Pssm-ID: 240141 [Multi-domain]  Cd Length: 126  Bit Score: 56.74  E-value: 4.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 160 RIAFFGLGSS---AAVAHDAMNKFFRFNVPVIYSDDIvlqRMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVI 236
Cdd:cd05008     1 RILIVGCGTSyhaALVAKYLLERLAGIPVEVEAASEF---RYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTV 77

                          90       100
                  ....*....|....*....|....*
gi 1737604106 237 ALT-TAGTPLAREATLAITLDV-PE 259
Cdd:cd05008    78 AITnVVGSTLAREADYVLYLRAgPE 102
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 203-281 8.10e-09

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: 52.93  E-value: 8.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 203 CSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALT-TAGTPLAREATLAITLDVPEDTDMY--MPMVSRLAQLTVIDV 279
Cdd:cd05014    45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITgNPNSTLAKLSDVVLDLPVEEEACPLglAPTTSTTAMLALGDA 124


                  ..
gi 1737604106 280 LA 281
Cdd:cd05014   125 LA 126
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 204-254 7.87e-08

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: 50.27  E-value: 7.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737604106 204 SEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTT-AGTPLAREATLAIT 254
Cdd:cd05710    46 TEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDdEDSPLAKLADYVIV 97
PRK02947 PRK02947
sugar isomerase domain-containing protein;
123-239 2.27e-06

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 47.94  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 123 AYTAKIFESAMATLDHVRQSlDMSSVNRAVDLLTQA----KRIAFFGLGSSAAVAHDAmnkFFRFN--VPV--IYSDDIV 194
Cdd:PRK02947    2 DMIDEYFDAVIELLERVRET-QAEAIEKAADLIADSirngGLIYVFGTGHSHILAEEV---FYRAGglAPVnpILEPSLM 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737604106 195 LQRMscMNCS--------------------EDDVVVLISHTGRTKSQVELAQLARENDAMVIALT 239
Cdd:PRK02947   78 LHEG--AVASsylervegyakaildrydirPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVT 140
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 159-260 2.78e-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: 48.36  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 159 KRIAFFGLGSSAAVAH---DAMNKFFRFNVPVIYSDDIVLQRMSCMNcsEDDVVVLISHTGRTKSQVELAQLARENDAMV 235
Cdd:COG2222    35 RRVVLVGAGSSDHAAQaaaYLLERLLGIPVAALAPSELVVYPAYLKL--EGTLVVAISRSGNSPEVVAALELAKARGART 112

                          90       100
                  ....*....|....*....|....*.
gi 1737604106 236 IALT-TAGTPLAREATLAITLDVPED 260
Cdd:COG2222   113 LAITnNPDSPLAEAADRVLPLPAGPE 138
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 129-239 7.70e-06

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: 433326 [Multi-domain]  Cd Length: 138  Bit Score: 44.89  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 129 FESAMATLDHVRQSLdMSSVNRAVDLLTQA----KRIAFFGLGSSAAVAHDAmnkFFRFN--VPV--IYSDDIVLQRMSC 200
Cdd:pfam13580   3 LDEVRALLERVVETQ-ADAIEKAADLIAASlangGKVYAFGTGHSAAPAEEL---FARAGglAGFepILLPALALHTDAS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737604106 201 MNCSED--------------------DVVVLISHTGRTKSQVELAQLARENDAMVIALT 239
Cdd:pfam13580  79 ATISTAlerdegyarqilalypgrpgDVLIVISNSGINAVPVEAALEAKERGMKVIALT 137
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 161-239 1.97e-05

SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 42.36  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 161 IAFFGLGSSAAVAHDAMNKFFRFN-VPVIYSDDIVLQRMS-CMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIAL 238
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLELTgIEVVALIATELEHASlLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                  .
gi 1737604106 239 T 239
Cdd:cd04795    81 T 81
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 137-305 4.19e-05

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 44.59  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 137 DHVRQSLDMSSVNRAVDLLTQAKRIAFFGLGSSAAVAhDAMNKFFR--FNVPVIYSDDIVLQRMscmnCSEDDVVVLISH 214
Cdd:PRK08674   13 EQFEEALEIAISLDLEEDLEKIDNIVISGMGGSGIGG-DLLRILLFdeLKVPVFVNRDYTLPAF----VDEKTLVIAVSY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 215 TGRTKSQVELAQLARENDAMVIALTTAG--TPLAREATLAiTLDVPEDTD-------MYMPMVSRLAQLTVIDVLATGF- 284
Cdd:PRK08674   88 SGNTEETLSAVEQALKRGAKIIAITSGGklKEMAKEHGLP-VIIVPGGYQpraalgyLFTPLLKILEKLGLIPDKSAEVl 166

                         170       180
                  ....*....|....*....|..
gi 1737604106 285 -TLRRGAKFRDNLKRVKEALKE 305
Cdd:PRK08674  167 eTKIVLSELAEGLKEKVPTLKN 188
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 204-285 5.32e-05

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: 44.20  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 204 SEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTT-AGTPLAREATLAITLDVPEDTDMY--MPMVSRLAQLTVIDVL 280
Cdd:COG0794    90 TPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGnPDSTLARAADVVLDLPVEREACPLnlAPTTSTTATLALGDAL 169

                          90
                  ....*....|.
gi 1737604106 281 A------TGFT 285
Cdd:COG0794   170 AvalleaRGFT 180
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 142-260 5.83e-05

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: 42.88  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 142 SLDMSSVNRAVDLLTQA----KRIAFFGLGSSAAVA-HDA--MNKFFRFN---VPVI---------------YSDDIVLQ 196
Cdd:cd05006    13 ELLAEAIEQAAQLLAEAllngGKILICGNGGSAADAqHFAaeLVKRFEKErpgLPAIalttdtsiltaiandYGYEEVFS 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737604106 197 RMSCMNCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTTA-GTPLAREATLAITldVPED 260
Cdd:cd05006    93 RQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRdGGKLLELADIEIH--VPSD 155
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 160-242 8.09e-05

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: 41.48  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 160 RIAFFGLGSSAAVAhDAMNKFF--RFNVPVIYSDDIVLQRMScmncSEDDVVVLISHTGRTKSQVELAQLARENDAMVIA 237
Cdd:cd05017     1 NIVILGMGGSGIGG-DLLESLLldEAKIPVYVVKDYTLPAFV----DRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVA 75


                  ....*
gi 1737604106 238 LTTAG 242
Cdd:cd05017    76 ITSGG 80
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 202-259 2.45e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 42.08  E-value: 2.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 202 NCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALT-TAGTPLAREATLAITLDV-PE 259
Cdd:PRK05441  128 NLTAKDVVVGIAASGRTPYVIGALEYARERGALTIGIScNPGSPLSKEADIAIEVVVgPE 187
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 202-258 3.37e-04

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: 41.35  E-value: 3.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1737604106 202 NCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALT-TAGTPLAREATLAITLDVP 258
Cdd:cd05007   115 NLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIAcNPGSPLLQLADIAIALITG 172
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 202-259 1.96e-03

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 39.31  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737604106 202 NCSEDDVVVLISHTGRTKSQVELAQLARENDAMVIALTT-AGTPLAREATLAITLDV-PE 259
Cdd:COG2103   129 GLGPGDVVVGIAASGRTPYVIGALEYARARGALTVAIACnPGSPLSAAADIAIELVTgPE 188
 
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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