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Conserved domains on  [gi|658548680|ref|WP_029741136|]
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MULTISPECIES: N-acetylmuramic acid 6-phosphate etherase [Enterobacter]

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
1-297 2.64e-180

N-acetylmuramic acid-6-phosphate etherase; Reviewed


:

Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 498.54  E-value: 2.64e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   1 MNLGSLVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  81 ASECPPTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCT 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 161 TVAISCNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548680 241 MVMEATGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALEN 297
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
1-297 2.64e-180

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 498.54  E-value: 2.64e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   1 MNLGSLVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  81 ASECPPTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCT 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 161 TVAISCNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548680 241 MVMEATGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALEN 297
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
1-297 2.88e-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: 483.44  E-value: 2.88e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   1 MNLGSLVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLD 80
Cdd:COG2103    2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  81 ASECPPTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCT 160
Cdd:COG2103   82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 161 TVAISCNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACR 240
Cdd:COG2103  162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548680 241 MVMEATGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALEN 297
Cdd:COG2103  242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALAA 298
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
14-270 5.51e-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: 394.97  E-value: 5.51e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  14 QTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLDASECPPTFGVPHG 93
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  94 LVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIA 173
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 174 QVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACRMVMEATGAGREEA 253
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
                        250
                 ....*....|....*..
gi 658548680 254 EAVLKQTDHDVKPAILM 270
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
6-296 3.63e-133

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: 379.19  E-value: 3.63e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680    6 LVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLDASECP 85
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   86 PTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAIS 165
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  166 CNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACRMVMEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 658548680  246 TGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALE 296
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
63-207 8.74e-09

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: 53.07  E-value: 8.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   63 GRIIYMGAGTSGRLGVldasecpptFGVPHglvVGLIAGgpgallKAVEGaEDNAQLGEDDLkdLNLTAKDLVVGLAASG 142
Cdd:pfam01380   6 KRIFVIGRGTSYAIAL---------ELALK---FEEIGY------KVVEV-ELASELRHGVL--ALVDEDDLVIAISYSG 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548680  143 RTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAISPVVGPEALTGSTrlKSGTAQKLVLNM 207
Cdd:pfam01380  65 ETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
1-297 2.64e-180

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 498.54  E-value: 2.64e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   1 MNLGSLVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  81 ASECPPTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCT 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 161 TVAISCNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548680 241 MVMEATGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALEN 297
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
1-297 2.88e-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: 483.44  E-value: 2.88e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   1 MNLGSLVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLD 80
Cdd:COG2103    2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  81 ASECPPTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCT 160
Cdd:COG2103   82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 161 TVAISCNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACR 240
Cdd:COG2103  162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548680 241 MVMEATGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALEN 297
Cdd:COG2103  242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALAA 298
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
6-297 6.43e-162

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 452.22  E-value: 6.43e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   6 LVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLDASECP 85
Cdd:PRK12570   2 LVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASECP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  86 PTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAIS 165
Cdd:PRK12570  82 PTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 166 CNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACRMVMEA 245
Cdd:PRK12570 162 CNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQA 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 658548680 246 TGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALEN 297
Cdd:PRK12570 242 TGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIEA 293
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
14-270 5.51e-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: 394.97  E-value: 5.51e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  14 QTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLDASECPPTFGVPHG 93
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  94 LVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIA 173
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 174 QVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACRMVMEATGAGREEA 253
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
                        250
                 ....*....|....*..
gi 658548680 254 EAVLKQTDHDVKPAILM 270
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
6-296 3.63e-133

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: 379.19  E-value: 3.63e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680    6 LVSETRNPQTMDLDALSTLELVNRFNQQDTLVAQAVKETLPEVAKAVDAAAEALKAGGRIIYMGAGTSGRLGVLDASECP 85
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   86 PTFGVPHGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAIS 165
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  166 CNPGSPIAQVAAIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKFGKVYQNLMVDMQATNVKLVDRACRMVMEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 658548680  246 TGAGREEAEAVLKQTDHDVKPAILMILSGLDAAAARAKLAAHNGFLRAALE 296
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
126-209 1.98e-11

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


Pssm-ID: 240141 [Multi-domain]  Cd Length: 126  Bit Score: 60.20  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 126 DLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAISPVVGPEALTGSTrlKSGTAQKLVL 205
Cdd:cd05008   41 RPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEISVAAT--KAFTSQLLAL 118

                 ....
gi 658548680 206 NMIS 209
Cdd:cd05008  119 LLLA 122
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
128-211 4.10e-09

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 56.47  E-value: 4.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 128 NLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAIsPVVGPEALTGSTRLKSGTAQKLVLNM 207
Cdd:COG1737  179 LLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVL-YVPSEEPTLRSSAFSSRVAQLALIDA 257

                 ....
gi 658548680 208 ISTG 211
Cdd:COG1737  258 LAAA 261
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
63-207 8.74e-09

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: 53.07  E-value: 8.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   63 GRIIYMGAGTSGRLGVldasecpptFGVPHglvVGLIAGgpgallKAVEGaEDNAQLGEDDLkdLNLTAKDLVVGLAASG 142
Cdd:pfam01380   6 KRIFVIGRGTSYAIAL---------ELALK---FEEIGY------KVVEV-ELASELRHGVL--ALVDEDDLVIAISYSG 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548680  143 RTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAISPVVGPEALTGSTrlKSGTAQKLVLNM 207
Cdd:pfam01380  65 ETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
60-214 1.82e-08

Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 54.52  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  60 KAGGRIIYMGAGTSGRLGVLdasecpptfgvphglVVGLIAGGPGALLKAVEGAEdnAQLGEDDLKDlnltAKDLVVGLA 139
Cdd:COG2222   32 KPPRRVVLVGAGSSDHAAQA---------------AAYLLERLLGIPVAALAPSE--LVVYPAYLKL----EGTLVVAIS 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548680 140 ASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAIspvvgpeaLTGSTRLKSGTAQKLVLNMISTGAMV 214
Cdd:COG2222   91 RSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL--------PLPAGPEKSVAATKSFTTMLLALLAL 157
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
129-188 3.27e-07

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: 48.31  E-value: 3.27e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 129 LTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAISPVVGPEA 188
Cdd:cd05014   45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEA 104
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
59-211 4.42e-07

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: 48.38  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  59 LKAGGRIIYMGAGTSGRLGvLDASecppTFGVPHGLVVGLIAGGPGALLKAvegaednaqlgeddlkdLNLTAKDLVVGL 138
Cdd:cd05013   10 LAKARRIYIFGVGSSGLVA-EYLA----YKLLRLGKPVVLLSDPHLQLMSA-----------------ANLTPGDVVIAI 67
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548680 139 AASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAIsPVVGPEALTGSTRLKSGTAQKLVLNMISTG 211
Cdd:cd05013   68 SFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVL-LVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
65-165 1.69e-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: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 45.44  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680  65 IIYMGAGTSGRLGVLDASECPPTFGVPhglVVGLIAGGpgallkavegaednaqlGEDDLKDLNLTAKDLVVGLAASGRT 144
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIE---VVALIATE-----------------LEHASLLSLLRKGDVVIALSYSGRT 60
                         90       100
                 ....*....|....*....|.
gi 658548680 145 PYVIGGLEYANRTGCTTVAIS 165
Cdd:cd04795   61 EELLAALEIAKELGIPVIAIT 81
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
129-188 6.28e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 43.60  E-value: 6.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548680 129 LTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAI------SPVVGPEA 188
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVIcstaqgSPLLGENA 250
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
128-180 1.43e-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: 41.79  E-value: 1.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 658548680 128 NLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAI 180
Cdd:cd05005   72 AIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
129-176 1.88e-04

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: 40.25  E-value: 1.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 658548680 129 LTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVA 176
Cdd:cd05710   45 LTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLA 92
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
129-188 5.02e-04

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: 41.12  E-value: 5.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 129 LTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAISPVVGPEA 188
Cdd:COG0794   89 ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREA 148
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
129-180 6.53e-04

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


Pssm-ID: 240139 [Multi-domain]  Cd Length: 177  Bit Score: 39.80  E-value: 6.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 658548680 129 LTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAI 180
Cdd:cd05006   99 GQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEI 150
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
133-180 9.42e-04

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 39.45  E-value: 9.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 658548680 133 DLVVGLAASGRTPYVIGGLEYANRTGCTTVAISCNPGSPIAQVAAIAI 180
Cdd:PRK13937 108 DVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLL 155
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
59-165 1.29e-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: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680   59 LKAGGRIIYMGAGTSGrlgvLDASECPPTFG--VP-HGLVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKDLNLTAKDLV 135
Cdd:pfam13580  32 LANGGKVYAFGTGHSA----APAEELFARAGglAGfEPILLPALALHTDASATISTALERDEGYARQILALYPGRPGDVL 107
                          90       100       110
                  ....*....|....*....|....*....|
gi 658548680  136 VGLAASGRTPYVIGGLEYANRTGCTTVAIS 165
Cdd:pfam13580 108 IVISNSGINAVPVEAALEAKERGMKVIALT 137
UBA_AeNAC cd14359
UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from ...
240-271 1.94e-03

UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from Methanothermobacter marburgensis (AeNAC) and similar proteins; AeNAC is a functional archaeal homolog of eukaryotic nascent polypeptide-associated complex (NAC). Both AeNAC and eukaryotic NAC function as the cytosolic chaperone that can bind to ribosomal RNA, interact with the nascent polypeptide chains as they emerge from the ribosome, and assist in post-translational processes. They all contain a NAC domain and an ubiquitin-associated (UBA) domain in the C-terminus. However, unlike eukaryotic NAC, AeNAC forms a ribosome associated homodimer, but not heterodimer. The NAC domain of AeNAC is responsible for the homodimer formation.


Pssm-ID: 270542 [Multi-domain]  Cd Length: 40  Bit Score: 35.28  E-value: 1.94e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 658548680 240 RMVMEATGAGREEAEAVLKQTDHDVKPAILMI 271
Cdd:cd14359    8 ELVMEQTGVSREEARKALEESGGDLAEAILKL 39
EGD2 COG1308
Transcription factor homologous to NACalpha-BTF3 [Transcription];
240-274 4.63e-03

Transcription factor homologous to NACalpha-BTF3 [Transcription];


Pssm-ID: 440919 [Multi-domain]  Cd Length: 116  Bit Score: 36.36  E-value: 4.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 658548680 240 RMVMEATGAGREEAEAVLKQTDHDVKPAILMILSG 274
Cdd:COG1308   82 ELVAEQTGVSEEEAREALEEANGDLAEAILKLEEE 116
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
126-209 5.43e-03

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 38.07  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548680 126 DLNLTAKDLVVGLAASGRTPYVIGGLEYANRTGCTTVAIsCN-PGSPIAQVAAIAISPVVGPE---AltgSTrlKSGTAQ 201
Cdd:COG0449  336 DPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAI-CNvVGSTIARESDAVLYTHAGPEigvA---ST--KAFTTQ 409

                 ....*...
gi 658548680 202 KLVLNMIS 209
Cdd:COG0449  410 LAALYLLA 417
 
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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