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Conserved domains on  [gi|490521950|ref|WP_004387387|]
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MULTISPECIES: N-acetylmuramic acid 6-phosphate etherase [Cronobacter]

Protein Classification

N-acetylmuramic acid 6-phosphate etherase( domain architecture ID 11480961)

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.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
1-296 3.25e-180

N-acetylmuramic acid-6-phosphate etherase; Reviewed


:

Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 498.54  E-value: 3.25e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
1-296 3.25e-180

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 498.54  E-value: 3.25e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
1-296 1.40e-174

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 484.21  E-value: 1.40e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:COG2103    2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:COG2103   82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:COG2103  162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:COG2103  242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALA 297
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
14-270 1.34e-140

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: 396.51  E-value: 1.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  14 DTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECPPTFGVPHG 93
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  94 VVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIA 173
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 174 EAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEATGVTREEA 253
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
                        250
                 ....*....|....*..
gi 490521950 254 EAVLTQTEYEVKPAILM 270
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
6-295 4.69e-130

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: 371.10  E-value: 4.69e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950    6 LVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECP 85
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   86 PTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAIS 165
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  166 CNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 490521950  246 TGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAAL 295
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
59-207 8.27e-08

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: 50.38  E-value: 8.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   59 LTCGGRLIYMGAGTSGRLGVldasecpptFGVPHgvvVGLIAGgpgallKAVEGaEDNAQLGEDDLKAIglNARDMVVGL 138
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIAL---------ELALK---FEEIGY------KVVEV-ELASELRHGVLALV--DEDDLVIAI 60
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490521950  139 AASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEALTGSTrlKSGTAQKLVLNM 207
Cdd:pfam01380  61 SYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
1-296 3.25e-180

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 498.54  E-value: 3.25e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
1-296 1.40e-174

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 484.21  E-value: 1.40e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:COG2103    2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:COG2103   82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:COG2103  162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:COG2103  242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALA 297
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
6-296 1.40e-158

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 443.75  E-value: 1.40e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   6 LVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECP 85
Cdd:PRK12570   2 LVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASECP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  86 PTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAIS 165
Cdd:PRK12570  82 PTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 166 CNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEA 245
Cdd:PRK12570 162 CNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQA 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490521950 246 TGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:PRK12570 242 TGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIE 292
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
14-270 1.34e-140

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: 396.51  E-value: 1.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  14 DTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECPPTFGVPHG 93
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  94 VVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIA 173
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 174 EAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEATGVTREEA 253
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
                        250
                 ....*....|....*..
gi 490521950 254 EAVLTQTEYEVKPAILM 270
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
6-295 4.69e-130

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: 371.10  E-value: 4.69e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950    6 LVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECP 85
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   86 PTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAIS 165
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  166 CNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 490521950  246 TGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAAL 295
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
129-209 3.69e-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: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEALTGSTrlKSGTAQKLVLNMI 208
Cdd:cd05008   44 LDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEISVAAT--KAFTSQLLALLLL 121

                 .
gi 490521950 209 S 209
Cdd:cd05008  122 A 122
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
126-218 4.73e-08

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 53.01  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 126 AIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIsPVVGPEALTGSTRLKSGTAQKLVL 205
Cdd:COG1737  177 AALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVL-YVPSEEPTLRSSAFSSRVAQLALI 255
                         90
                 ....*....|...
gi 490521950 206 NMISTGAMVKCGK 218
Cdd:COG1737  256 DALAAAVAQRDGD 268
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
126-211 5.87e-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: 50.69  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 126 AIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIsPVVGPEALTGSTRLKSGTAQKLVL 205
Cdd:cd05013   55 AANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVL-LVSSEEGDFRSSAFSSRIAQLALI 133

                 ....*.
gi 490521950 206 NMISTG 211
Cdd:cd05013  134 DALFLA 139
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
59-207 8.27e-08

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: 50.38  E-value: 8.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950   59 LTCGGRLIYMGAGTSGRLGVldasecpptFGVPHgvvVGLIAGgpgallKAVEGaEDNAQLGEDDLKAIglNARDMVVGL 138
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIAL---------ELALK---FEEIGY------KVVEV-ELASELRHGVLALV--DEDDLVIAI 60
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490521950  139 AASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEALTGSTrlKSGTAQKLVLNM 207
Cdd:pfam01380  61 SYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
130-214 3.43e-07

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: 50.67  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 130 NARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIspvvgpeaLTGSTRLKSGTAQKLVLNMIS 209
Cdd:COG2222   81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL--------PLPAGPEKSVAATKSFTTMLL 152

                 ....*
gi 490521950 210 TGAMV 214
Cdd:COG2222  153 ALLAL 157
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
129-188 1.40e-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: 43.69  E-value: 1.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEA 188
Cdd:cd05014   45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEA 104
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
65-165 1.51e-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: 42.75  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950  65 LIYMGAGTSGRLGVLDASECPPTFGVPhgvVVGLIAGGpgallkavegaednaqlGEDDLKAIGLNARDMVVGLAASGRT 144
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIE---VVALIATE-----------------LEHASLLSLLRKGDVVIALSYSGRT 60
                         90       100
                 ....*....|....*....|.
gi 490521950 145 PYVIGGLKYARALGCATAAIS 165
Cdd:cd04795   61 EELLAALEIAKELGIPVIAIT 81
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
124-180 7.15e-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: 42.50  E-value: 7.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490521950 124 LKAIGlNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:cd05006   95 VEALG-QPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEI 150
frlB PRK11382
fructoselysine 6-phosphate deglycase;
129-181 1.41e-04

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 42.68  E-value: 1.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIS 181
Cdd:PRK11382  90 LDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSID 142
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
133-180 2.21e-04

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 41.38  E-value: 2.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 490521950 133 DMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:PRK13937 108 DVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLL 155
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
129-188 2.39e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 42.05  E-value: 2.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI------SPVVGPEA 188
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVIcstaqgSPLLGENA 250
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
115-180 1.30e-03

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: 37.94  E-value: 1.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 115 DNAQLGEDDLkaiglnardmVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:cd05710   41 GPKRLTEKSV----------VILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
133-180 2.61e-03

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: 37.94  E-value: 2.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 490521950 133 DMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:cd05005   77 DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
 
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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