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Conserved domains on  [gi|447098344|ref|WP_001175600|]
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MULTISPECIES: N-acetylmuramic acid 6-phosphate etherase [Escherichia]

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 0e+00

N-acetylmuramic acid-6-phosphate etherase; Reviewed


:

Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 503.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   1 MQLEKMITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  81 ASECPPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCR 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 161 TVGISCNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVN 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447098344 241 IVKNATGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLDK 297
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
1-297 0e+00

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 503.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   1 MQLEKMITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  81 ASECPPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCR 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 161 TVGISCNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVN 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447098344 241 IVKNATGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLDK 297
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
6-296 0e+00

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: 502.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344    6 MITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILDASECP 85
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   86 PTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGIS 165
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  166 CNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVNIVKNA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 447098344  246 TGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLD 296
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
1-297 7.33e-180

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 497.69  E-value: 7.33e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   1 MQLEKMITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILD 80
Cdd:COG2103    2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  81 ASECPPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCR 160
Cdd:COG2103   82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 161 TVGISCNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVN 240
Cdd:COG2103  162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447098344 241 IVKNATGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLDK 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 9.89e-143

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: 401.90  E-value: 9.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  14 ASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILDASECPPTYGVKPG 93
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  94 LVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVS 173
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 174 TTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVNIVKNATGCNAEQA 253
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
                        250
                 ....*....|....*..
gi 447098344 254 EAALIACERNCKTAIVM 270
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
63-208 2.20e-07

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: 48.83  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   63 GRLIYIGAGTSGRLGildasecpptygVKPGLVVGLIAGgeyaIQHAVEGAEDSREGGVNDLkniglTAQDVVVGIAASG 142
Cdd:pfam01380   6 KRIFVIGRGTSYAIA------------LELALKFEEIGY----KVVEVELASELRHGVLALV-----DEDDLVIAISYSG 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447098344  143 RTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAITPVVGAEVVTGSsrMKAGTAQKLVLNML 208
Cdd:pfam01380  65 ETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAS--TKSITAQLAALDAL 128
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
1-297 0e+00

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 503.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   1 MQLEKMITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILD 80
Cdd:PRK05441   1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  81 ASECPPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCR 160
Cdd:PRK05441  81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 161 TVGISCNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVN 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447098344 241 IVKNATGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLDK 297
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
6-296 0e+00

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: 502.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344    6 MITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILDASECP 85
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   86 PTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGIS 165
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  166 CNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVNIVKNA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 447098344  246 TGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLD 296
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
1-297 7.33e-180

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 497.69  E-value: 7.33e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   1 MQLEKMITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILD 80
Cdd:COG2103    2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  81 ASECPPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCR 160
Cdd:COG2103   82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 161 TVGISCNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVN 240
Cdd:COG2103  162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447098344 241 IVKNATGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLDK 297
Cdd:COG2103  242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALAA 298
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
5-295 1.01e-149

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 421.41  E-value: 1.01e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   5 KMITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILDASEC 84
Cdd:PRK12570   1 HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASEC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  85 PPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGI 164
Cdd:PRK12570  81 PPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 165 SCNPGSAVSTTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVNIVKN 244
Cdd:PRK12570 161 SCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQ 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447098344 245 ATGCNAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVL 295
Cdd:PRK12570 241 ATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAI 291
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
14-270 9.89e-143

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: 401.90  E-value: 9.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  14 ASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVSGGGRLIYIGAGTSGRLGILDASECPPTYGVKPG 93
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  94 LVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVS 173
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 174 TTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVNIVKNATGCNAEQA 253
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
                        250
                 ....*....|....*..
gi 447098344 254 EAALIACERNCKTAIVM 270
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
64-209 7.07e-12

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: 61.36  E-value: 7.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  64 RLIYIGAGTSgrlgildasecpptygvkpgLVVGLIAggEYAIQH------AVEGAEDSREGGVNDLKNigltaqDVVVG 137
Cdd:cd05008    1 RILIVGCGTS--------------------YHAALVA--KYLLERlagipvEVEAASEFRYRRPLLDED------TLVIA 52
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447098344 138 IAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAITPVVGAEVvtGSSRMKAGTAQKLVLNMLS 209
Cdd:cd05008   53 ISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEI--SVAATKAFTSQLLALLLLA 122
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
38-214 1.73e-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: 60.68  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  38 PLAVERVLPDIAAAIDVIHAQVS--GGGRLIYIGAGTSGRLGILDAsecpPTYGVKPGLVVGLIAGGEYAIQHAvegaed 115
Cdd:COG2222    8 PEAWRRALAALAAAIAALLARLRakPPRRVVLVGAGSSDHAAQAAA----YLLERLLGIPVAALAPSELVVYPA------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 116 sreggvnDLKNIGltaqDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAITPVVGAEvvtgssrm 195
Cdd:COG2222   78 -------YLKLEG----TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPE-------- 138
                        170
                 ....*....|....*....
gi 447098344 196 KAGTAQKLVLNMLSTGLMI 214
Cdd:COG2222  139 KSVAATKSFTTMLLALLAL 157
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
129-218 7.08e-09

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 55.70  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAITpVVGAEVVTGSSRMKAGTAQKLVLNML 208
Cdd:COG1737  180 LGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY-VPSEEPTLRSSAFSSRVAQLALIDAL 258
                         90
                 ....*....|
gi 447098344 209 STGLMIKSGK 218
Cdd:COG1737  259 AAAVAQRDGD 268
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
63-208 2.20e-07

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: 48.83  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   63 GRLIYIGAGTSGRLGildasecpptygVKPGLVVGLIAGgeyaIQHAVEGAEDSREGGVNDLkniglTAQDVVVGIAASG 142
Cdd:pfam01380   6 KRIFVIGRGTSYAIA------------LELALKFEEIGY----KVVEVELASELRHGVLALV-----DEDDLVIAISYSG 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447098344  143 RTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAITPVVGAEVVTGSsrMKAGTAQKLVLNML 208
Cdd:pfam01380  65 ETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAS--TKSITAQLAALDAL 128
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
65-165 1.11e-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: 45.83  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344  65 LIYIGAGTSGRLGILDASECPPTYGVkpgLVVGLIAGGEYAIQHAVEGAEDsreggvndlknigltaqDVVVGIAASGRT 144
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGI---EVVALIATELEHASLLSLLRKG-----------------DVVIALSYSGRT 60
                         90       100
                 ....*....|....*....|.
gi 447098344 145 PYVIAGLEYARQLGCRTVGIS 165
Cdd:cd04795   61 EELLAALEIAKELGIPVIAIT 81
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
133-163 1.42e-06

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 47.93  E-value: 1.42e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 447098344 133 DVVVGIAASGRTPYVIAGLEYARQLGCRTVG 163
Cdd:PRK13937 108 DVLIGISTSGNSPNVLAALEKARELGMKTIG 138
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
129-211 2.82e-06

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: 46.07  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAItPVVGAEVVTGSSRMKAGTAQKLVLNML 208
Cdd:cd05013   58 LTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVL-LVSSEEGDFRSSAFSSRIAQLALIDAL 136

                 ...
gi 447098344 209 STG 211
Cdd:cd05013  137 FLA 139
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
129-181 4.10e-06

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: 45.23  E-value: 4.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAIT 181
Cdd:cd05014   45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLD 97
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
133-209 6.45e-05

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 44.48  E-value: 6.45e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447098344 133 DVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAITPVVGAEVVTGSSrmKAGTAQKLVLNMLS 209
Cdd:PTZ00394 403 DVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVAST--KAYTSQVVVLTLVA 477
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
129-181 8.67e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 43.21  E-value: 8.67e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAIT 181
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVIC 237
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
132-212 8.83e-05

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 43.97  E-value: 8.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 132 QDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAITPVVGAEVvtGSSRMKAGTAQKLVLNMLSTG 211
Cdd:PLN02981 411 EDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEI--GVASTKAYTSQIVAMTMLALA 488

                 .
gi 447098344 212 L 212
Cdd:PLN02981 489 L 489
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
129-165 9.10e-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: 42.11  E-value: 9.10e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGIS 165
Cdd:cd05006   99 GQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALT 135
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
129-180 3.41e-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: 40.64  E-value: 3.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAI 180
Cdd:cd05005   73 IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
48-165 6.48e-04

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: 39.12  E-value: 6.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344   48 IAAAIDVIHAQVSGGGRLIYIGAGTS--------GRLGILDASECPptygVKPGLVvgLIAGGEYAIQHAVEGaedsREG 119
Cdd:pfam13580  21 IEKAADLIAASLANGGKVYAFGTGHSaapaeelfARAGGLAGFEPI----LLPALA--LHTDASATISTALER----DEG 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 447098344  120 -GVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGIS 165
Cdd:pfam13580  91 yARQILALYPGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALT 137
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
129-229 2.06e-03

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 39.64  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGIsCN-PGSAVSTTAEFAITPVVGAEVVTGSSrmKAGTAQKLVLNM 207
Cdd:PRK00331 334 LSPKTLVIAISQSGETADTLAALRLAKELGAKTLAI-CNvPGSTIARESDAVLYTHAGPEIGVAST--KAFTAQLAVLYL 410
                         90       100
                 ....*....|....*....|..
gi 447098344 208 LSTGLMIKSGKVFGNLMVDVVA 229
Cdd:PRK00331 411 LALALAKARGTLSAEEEADLVH 432
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
129-184 5.11e-03

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: 38.03  E-value: 5.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAI-TPVV 184
Cdd:COG0794   89 ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLdLPVE 145
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
129-181 5.93e-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: 36.01  E-value: 5.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447098344 129 LTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAIT 181
Cdd:cd05710   45 LTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIV 97
 
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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