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Conserved domains on  [gi|1391744357|gb|AWM85818|]
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N-acetylmuramic acid 6-phosphate etherase [Microvirga sp. 17 mud 1-3]

Protein Classification

N-acetylmuramic acid 6-phosphate etherase( domain architecture ID 11450007)

N-acetylmuramic acid 6-phosphate etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate, a bacterial cell wall sugar.

PubMed:  24251551

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 1-291 2.70e-150

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


:

Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 422.96  E-value: 2.70e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   1 MPTENFSTRFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELP 80
Cdd:COG2103     7 LTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLDASECP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  81 PTFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:COG2103    87 PTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGALTVAIA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 161 NNPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQI 240
Cdd:COG2103   167 CNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIRIVMEA 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391744357 241 TGCDDATAIEALRRANGDMKLASL-IALGVDPSEAQGALTQSDGNLREALSH 291
Cdd:COG2103   247 TGCDEEEAEEALEAAGGHVKTAILmILTGLDAEEAEALLARAGGFLRKALAA 298
 
Name Accession Description Interval E-value
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 1-291 2.70e-150

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 422.96  E-value: 2.70e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   1 MPTENFSTRFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELP 80
Cdd:COG2103     7 LTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLDASECP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  81 PTFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:COG2103    87 PTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGALTVAIA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 161 NNPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQI 240
Cdd:COG2103   167 CNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIRIVMEA 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391744357 241 TGCDDATAIEALRRANGDMKLASL-IALGVDPSEAQGALTQSDGNLREALSH 291
Cdd:COG2103   247 TGCDEEEAEEALEAAGGHVKTAILmILTGLDAEEAEALLARAGGFLRKALAA 298
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 1-291 1.52e-139

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 395.69  E-value: 1.52e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   1 MPTENFSTRFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELP 80
Cdd:PRK05441    6 LTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDASECP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  81 PTFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:PRK05441   86 PTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTIGIS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 161 NNPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQI 240
Cdd:PRK05441  166 CNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRIVMEA 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391744357 241 TGCDDATAIEALRRANGDMKLASLIAL-GVDPSEAQGALTQSDGNLREALSH 291
Cdd:PRK05441  246 TGVSREEAEAALEAADGSVKLAIVMILtGLDAAEAKALLARHGGFLRKALAE 297
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 9-265 1.05e-120

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: 346.05  E-value: 1.05e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   9 RFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELPPTFNWPDD 88
Cdd:cd05007     1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  89 KLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPIL 168
Cdd:cd05007    81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 169 DACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQITGCDDATA 248
Cdd:cd05007   161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240

                         250
                  ....*....|....*..
gi 1391744357 249 IEALRRANGDMKLASLI 265
Cdd:cd05007   241 EAALEQAGGDVKTAILM 257
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
 1-290 3.72e-79

N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling components of the bacterial murein sacculus turned over during cell growth. The cell wall metabolite anhydro-N-acetylmuramic acid (anhMurNAc) is converted by a kinase, AnmK, to MurNAc-phosphate, then converted to N-acetylglucosamine-phosphate by this etherase, called MurQ. This family of proteins is similar to the C-terminal half of a number of vertebrate glucokinase regulator proteins and contains a Prosite pattern which is shared by this group of proteins in a region of local similarity. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 272991 [Multi-domain]  Cd Length: 291  Bit Score: 242.06  E-value: 3.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   1 MPTENFSTRFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELP 80
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  81 PTFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 161 NNPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQI 240
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391744357 241 TGCDDATAIEALRRANGDMKLASLIAL-GVDPSEAQGALTQSDGNLREALS 290
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILsTLSASEAKVLLDRHGGFLRQALD 291
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 54-203 1.98e-12

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 63.09  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  54 LRRGGRLVYVGAGTSGRIGVqdgtELPPTFNwpddKLVYLIAggegallkAVENAEDSVEQGIAGIRdsgvgPDDIVIGV 133
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIAL----ELALKFE----EIGYKVV--------EVELASELRHGVLALVD-----EDDLVIAI 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 134 AASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEVIAGSTrmKAGTAQKVILNLL 203
Cdd:pfam01380  61 SYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDAL 128
 
Name Accession Description Interval E-value
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 1-291 2.70e-150

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 422.96  E-value: 2.70e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   1 MPTENFSTRFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELP 80
Cdd:COG2103     7 LTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLDASECP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  81 PTFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:COG2103    87 PTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGALTVAIA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 161 NNPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQI 240
Cdd:COG2103   167 CNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIRIVMEA 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391744357 241 TGCDDATAIEALRRANGDMKLASL-IALGVDPSEAQGALTQSDGNLREALSH 291
Cdd:COG2103   247 TGCDEEEAEEALEAAGGHVKTAILmILTGLDAEEAEALLARAGGFLRKALAA 298
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 1-291 1.52e-139

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 395.69  E-value: 1.52e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   1 MPTENFSTRFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELP 80
Cdd:PRK05441    6 LTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDASECP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  81 PTFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:PRK05441   86 PTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTIGIS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 161 NNPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQI 240
Cdd:PRK05441  166 CNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRIVMEA 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391744357 241 TGCDDATAIEALRRANGDMKLASLIAL-GVDPSEAQGALTQSDGNLREALSH 291
Cdd:PRK05441  246 TGVSREEAEAALEAADGSVKLAIVMILtGLDAAEAKALLARHGGFLRKALAE 297
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 9-265 1.05e-120

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: 346.05  E-value: 1.05e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   9 RFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELPPTFNWPDD 88
Cdd:cd05007     1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  89 KLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPIL 168
Cdd:cd05007    81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 169 DACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQITGCDDATA 248
Cdd:cd05007   161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240

                         250
                  ....*....|....*..
gi 1391744357 249 IEALRRANGDMKLASLI 265
Cdd:cd05007   241 EAALEQAGGDVKTAILM 257
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 3-290 2.44e-94

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 280.81  E-value: 2.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   3 TENFSTRFQDLDAWPSSDILSAF-YEGQLAAVAaVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELPP 81
Cdd:PRK12570    4 SEGRNPATMDIDLLSSLDIVTLInQEDKKVPLA-VEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASECPP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  82 TFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISN 161
Cdd:PRK12570   83 TFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSC 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 162 NPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQIT 241
Cdd:PRK12570  163 NPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQAT 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1391744357 242 GCDDATAIEALRRANGDMKLASLIAL-GVDPSEAQGALTQSDGNLREALS 290
Cdd:PRK12570  243 GCSEDEAKELLKESDNDVKLAILMILtGMDVEQARAALSHADGFLRKAIE 292
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
 1-290 3.72e-79

N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling components of the bacterial murein sacculus turned over during cell growth. The cell wall metabolite anhydro-N-acetylmuramic acid (anhMurNAc) is converted by a kinase, AnmK, to MurNAc-phosphate, then converted to N-acetylglucosamine-phosphate by this etherase, called MurQ. This family of proteins is similar to the C-terminal half of a number of vertebrate glucokinase regulator proteins and contains a Prosite pattern which is shared by this group of proteins in a region of local similarity. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 272991 [Multi-domain]  Cd Length: 291  Bit Score: 242.06  E-value: 3.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357   1 MPTENFSTRFQDLDAWPSSDILSAFYEGQLAAVAAVRPALPAIAAAAEAAVERLRRGGRLVYVGAGTSGRIGVQDGTELP 80
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  81 PTFNWPDDKLVYLIAGGEGALLKAVENAEDSVEQGIAGIRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 161 NNPAAPILDACSHPILADTGEEVIAGSTRMKAGTAQKVILNLLSTLIMVRLGRVYRGLMVHMRATNAKLRRRSEIMVSQI 240
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391744357 241 TGCDDATAIEALRRANGDMKLASLIAL-GVDPSEAQGALTQSDGNLREALS 290
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILsTLSASEAKVLLDRHGGFLRQALD 291
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 59-204 5.21e-14

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: 67.52  E-value: 5.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  59 RLVYVGAGTSGRIGVQdgtelpptfnwpddkLVYLIaggEGALLKAVEnAEDSVEqgiAGIRDSGVGPDDIVIGVAASGR 138
Cdd:cd05008     1 RILIVGCGTSYHAALV---------------AKYLL---ERLAGIPVE-VEAASE---FRYRRPLLDEDTLVIAISQSGE 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391744357 139 TPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEViaGSTRMKAGTAQKVILNLLS 204
Cdd:cd05008    59 TADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEI--SVAATKAFTSQLLALLLLA 122
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 122-230 6.86e-13

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 67.26  E-value: 6.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 122 SGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTgEEVIAGSTRMKAGTAQKVILN 201
Cdd:COG1737   178 ALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPS-EEPTLRSSAFSSRVAQLALID 256

                          90       100
                  ....*....|....*....|....*....
gi 1391744357 202 LLSTLIMVRLGRVYRGLMVHMRATNAKLR 230
Cdd:COG1737   257 ALAAAVAQRDGDKARERLERTEALLSELR 285
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 54-203 1.98e-12

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 63.09  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  54 LRRGGRLVYVGAGTSGRIGVqdgtELPPTFNwpddKLVYLIAggegallkAVENAEDSVEQGIAGIRdsgvgPDDIVIGV 133
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIAL----ELALKFE----EIGYKVV--------EVELASELRHGVLALVD-----EDDLVIAI 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 134 AASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEVIAGSTrmKAGTAQKVILNLL 203
Cdd:pfam01380  61 SYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDAL 128
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 53-182 5.10e-10

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: 59.53  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  53 RLRRGGRLVYVGAGTSGRIGvqdgtelpptfnwpdDKLVYLIAGGEGALLKAVENAEDSVEQgiAGIRDSGvgpdDIVIG 132
Cdd:COG2222    30 RAKPPRRVVLVGAGSSDHAA---------------QAAAYLLERLLGIPVAALAPSELVVYP--AYLKLEG----TLVVA 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1391744357 133 VAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEE 182
Cdd:COG2222    89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPE 138
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 104-251 2.57e-09

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 57.97  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 104 AVENAEDSVEqgiagiRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEV 183
Cdd:PTZ00394  385 SVENASDFLD------RRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEV 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 184 IAGSTrmKAGTAQKVILNLLSTL-------IMVRLGRVYRGL------------MVH--MRATNAKLRRRSEIMVSQiTG 242
Cdd:PTZ00394  459 GVAST--KAYTSQVVVLTLVALLlssdsvrLQERRNEIIRGLaelpaaiseclkITHdpVKALAARLKESSSILVLG-RG 535


                  ....*....
gi 1391744357 243 CDDATAIEA 251
Cdd:PTZ00394  536 YDLATAMEA 544
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 51-206 1.47e-08

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: 52.62  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  51 VERLRRGGRLVYVGAGTSGRIGvQDGTelpptfnwpdDKLvyliaggeGALLKAVENAEDSVEQGIAGIRdsgVGPDDIV 130
Cdd:cd05013     7 VDLLAKARRIYIFGVGSSGLVA-EYLA----------YKL--------LRLGKPVVLLSDPHLQLMSAAN---LTPGDVV 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391744357 131 IGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEVIAGSTrMKAGTAQKVILNLLSTL 206
Cdd:cd05013    65 IAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSA-FSSRIAQLALIDALFLA 139
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 124-175 1.20e-07

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: 49.50  E-value: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391744357 124 VGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPI 175
Cdd:cd05710    45 LTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 120-219 2.15e-06

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: 48.86  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 120 RDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPIldacshPILADtgeEVI---AG------STrm 190
Cdd:COG0449   335 RDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTI------ARESD---AVLythAGpeigvaST-- 403

                          90       100
                  ....*....|....*....|....*....
gi 1391744357 191 KAGTAQKVILNLLStlimVRLGRVyRGLM 219
Cdd:COG0449   404 KAFTTQLAALYLLA----LYLARA-RGTL 427
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
125-182 6.61e-06

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 46.68  E-value: 6.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1391744357 125 GPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDaCSHPILADTGEE 182
Cdd:PRK11337  186 QEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAK-LADYVICSTAQG 242
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 126-178 1.24e-05

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 44.85  E-value: 1.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1391744357 126 PDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILAD 178
Cdd:PRK13937  106 PGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIVP 158
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 54-204 1.32e-05

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 46.28  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  54 LRRGGRLVYVGAGTS------GRIGVQDGTELPPTfnwpddklvyliaggegallkaVENAEDSVEqgiagiRDSGVGPD 127
Cdd:PLN02981  360 IRRSRRIVFIGCGTSynaalaARPILEELSGVPVT----------------------MELASDLLD------RQGPIYRE 411

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391744357 128 DIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEVIAGSTrmKAGTAQKVILNLLS 204
Cdd:PLN02981  412 DTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVAST--KAYTSQIVAMTMLA 486
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
120-219 3.28e-05

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 45.03  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 120 RDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEVIAGSTrmKAGTAQKVI 199
Cdd:PRK00331  330 RDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVAST--KAFTAQLAV 407

                          90       100
                  ....*....|....*....|
gi 1391744357 200 LNLLStlimVRLGRVyRGLM 219
Cdd:PRK00331  408 LYLLA----LALAKA-RGTL 422
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 121-212 5.24e-05

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: 42.14  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 121 DSG-VGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPILADTGEEVIagstrmkagtaqkvI 199
Cdd:cd05014    41 DLGmVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEAC--------------P 106

                          90
                  ....*....|....*.
gi 1391744357 200 LNLL---STLIMVRLG 212
Cdd:cd05014   107 LGLApttSTTAMLALG 122
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 126-175 5.60e-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: 5.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1391744357 126 PDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDACSHPI 175
Cdd:cd05006   101 PGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEI 150
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 124-232 5.03e-04

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: 40.25  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357 124 VGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISNNPAAPILDacshpiLADTgEEVIAGSTRMKAGTAQKVILnLL 203
Cdd:cd05005    73 IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAK------LADV-VVVIPAATKDDHGGEHKSIQ-PL 144

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1391744357 204 STL----IMVRLGRVYRGLMVHMRATNAKLRRR 232
Cdd:cd05005   145 GTLfeqsALVFLDAVIAKLMEELGVSEEEMKKR 177
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 120-160 1.18e-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: 433326 [Multi-domain]  Cd Length: 138  Bit Score: 38.35  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1391744357 120 RDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:pfam13580  97 ALYPGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALT 137
PRK02947 PRK02947
sugar isomerase domain-containing protein;
119-161 1.22e-03

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 39.47  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1391744357 119 IRDSGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGISN 161
Cdd:PRK02947   99 LDRYDIRPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVTS 141
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 88-160 2.50e-03

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 38.81  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  88 DKLVYLIAGGEGA---LLKAVENAEDSVEqgIAGIRD----SGVGPDDIVIGVAASGRTPFTIAALEEARARGAQTIGIS 160
Cdd:PRK08674   35 DNIVISGMGGSGIggdLLRILLFDELKVP--VFVNRDytlpAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAIT 112
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 60-160 3.19e-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: 36.20  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391744357  60 LVYVGAGTSGRIGVQDGTELPPTFNWPddklVYLIAGGEGALlkavenaedsveqgiaGIRDSGVGPDDIVIGVAASGRT 139
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLELTGIE----VVALIATELEH----------------ASLLSLLRKGDVVIALSYSGRT 60

                          90       100
                  ....*....|....*....|.
gi 1391744357 140 PFTIAALEEARARGAQTIGIS 160
Cdd:cd04795    61 EELLAALEIAKELGIPVIAIT 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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