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Conserved domains on  [gi|488377883|ref|WP_002447268|]
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MULTISPECIES: N-acetylmuramic acid 6-phosphate etherase [Staphylococcus]

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.

EC:  4.2.1.126
Gene Ontology:  GO:0097367|GO:0016835|GO:0046348|GO:0005975|GO:0097173
PubMed:  18049859|24251551

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
 1-294 6.09e-174

N-acetylmuramic acid-6-phosphate etherase; Reviewed


:

Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 482.36  E-value: 6.09e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   1 MNHLTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAA 80
Cdd:PRK05441   3 LENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  81 ECVPTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETV 160
Cdd:PRK05441  83 ECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 161 ALSCNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRII 240
Cdd:PRK05441 163 GISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRIV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377883 241 QDVCDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:PRK05441 243 MEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 1-294 6.09e-174

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 482.36  E-value: 6.09e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   1 MNHLTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAA 80
Cdd:PRK05441   3 LENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  81 ECVPTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETV 160
Cdd:PRK05441  83 ECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 161 ALSCNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRII 240
Cdd:PRK05441 163 GISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRIV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377883 241 QDVCDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:PRK05441 243 MEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 1-294 1.60e-172

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 478.82  E-value: 1.60e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   1 MNHLTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAA 80
Cdd:COG2103    4 LGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLDAS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  81 ECVPTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETV 160
Cdd:COG2103   84 ECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGALTV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 161 ALSCNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRII 240
Cdd:COG2103  164 AIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIRIV 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377883 241 QDVCDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:COG2103  244 MEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALA 297
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 12-268 3.42e-135

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: 382.64  E-value: 3.42e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  12 QTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAAECVPTFNVSPN 91
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  92 DIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDIS 171
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 172 KNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRIIQDVCDLNHQEA 251
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240

                        250
                 ....*....|....*..
gi 488377883 252 IELYEKSDHNIKIAIVM 268
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
 4-294 1.64e-124

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: 357.23  E-value: 1.64e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883    4 LTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAAECV 83
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   84 PTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALS 163
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  164 CNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRIIQDV 243
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488377883  244 CDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 61-205 8.15e-11

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: 58.46  E-value: 8.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   61 GRIIYIGAGTSGRLgvldAAECVPTFNVspndiigiIAGgqkaMTVAIEGAEDDaeqgaQDLKNIHLQSKDIVVGISASG 140
Cdd:pfam01380   6 KRIFVIGRGTSYAI----ALELALKFEE--------IGY----KVVEVELASEL-----RHGVLALVDEDDLVIAISYSG 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488377883  141 RTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPEVLTGSTrlKSGTAQKLVLNM 205
Cdd:pfam01380  65 ETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
 
Name Accession Description Interval E-value
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 1-294 6.09e-174

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 482.36  E-value: 6.09e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   1 MNHLTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAA 80
Cdd:PRK05441   3 LENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  81 ECVPTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETV 160
Cdd:PRK05441  83 ECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 161 ALSCNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRII 240
Cdd:PRK05441 163 GISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRIV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377883 241 QDVCDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:PRK05441 243 MEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 1-294 1.60e-172

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


Pssm-ID: 441706 [Multi-domain]  Cd Length: 301  Bit Score: 478.82  E-value: 1.60e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   1 MNHLTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAA 80
Cdd:COG2103    4 LGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLDAS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  81 ECVPTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETV 160
Cdd:COG2103   84 ECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGALTV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 161 ALSCNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRII 240
Cdd:COG2103  164 AIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIRIV 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377883 241 QDVCDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:COG2103  244 MEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALA 297
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 3-294 1.19e-143

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 405.61  E-value: 1.19e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   3 HLTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAAEC 82
Cdd:PRK12570   1 HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASEC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  83 VPTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVAL 162
Cdd:PRK12570  81 PPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 163 SCNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRIIQD 242
Cdd:PRK12570 161 SCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQ 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488377883 243 VCDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:PRK12570 241 ATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIE 292
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 12-268 3.42e-135

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: 382.64  E-value: 3.42e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  12 QTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAAECVPTFNVSPN 91
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  92 DIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDIS 171
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 172 KNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRIIQDVCDLNHQEA 251
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240

                        250
                 ....*....|....*..
gi 488377883 252 IELYEKSDHNIKIAIVM 268
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
 4-294 1.64e-124

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: 357.23  E-value: 1.64e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883    4 LTTETRNIQTMHLDEMNLKDALKTMNQEDQFVPKAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAAECV 83
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   84 PTFNVSPNDIIGIIAGGQKAMTVAIEGAEDDAEQGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALS 163
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  164 CNVHSDISKNSNHVLEINVGPEVLTGSTRLKSGTAQKLVLNMISTMTMIGVGKVYDNLMVDLRPTNQKLIHRSIRIIQDV 243
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488377883  244 CDLNHQEAIELYEKSDHNIKIAIVMHLCSTTQQDARLRLKQNNGVIKQAIN 294
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 124-207 1.78e-13

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: 65.98  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 124 NIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPEVLTGSTrlKSGTAQKLVL 203
Cdd:cd05008   41 RPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEISVAAT--KAFTSQLLAL 118


                 ....
gi 488377883 204 NMIS 207
Cdd:cd05008  119 LLLA 122
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 61-205 8.15e-11

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: 58.46  E-value: 8.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883   61 GRIIYIGAGTSGRLgvldAAECVPTFNVspndiigiIAGgqkaMTVAIEGAEDDaeqgaQDLKNIHLQSKDIVVGISASG 140
Cdd:pfam01380   6 KRIFVIGRGTSYAI----ALELALKFEE--------IGY----KVVEVELASEL-----RHGVLALVDEDDLVIAISYSG 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488377883  141 RTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPEVLTGSTrlKSGTAQKLVLNM 205
Cdd:pfam01380  65 ETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 36-185 2.95e-10

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


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 59.91  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  36 PKAIEPVIPNLTKVIESAIQRF--NNGGRIIYIGAGTSGRLGVLDAAEC-----VPTFNVSPNDIIGiiaggqkamtvai 108
Cdd:COG2222    8 PEAWRRALAALAAAIAALLARLraKPPRRVVLVGAGSSDHAAQAAAYLLerllgIPVAALAPSELVV------------- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488377883 109 egaeddaeqGAQDLKNihlqSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPE 185
Cdd:COG2222   75 ---------YPAYLKL----EGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPE 138
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 61-215 2.24e-09

KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.


Pssm-ID: 240145 [Multi-domain]  Cd Length: 128  Bit Score: 54.47  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  61 GRIIYIGAGTSGRLGVLDAAECV----PTFNVSPNDiigiiaggqkamtvAIEGaeddaeqgaqDLKniHLQSKDIVVGI 136
Cdd:cd05014    1 GKVVVTGVGKSGHIARKIAATLSstgtPAFFLHPTE--------------ALHG----------DLG--MVTPGDVVIAI 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 137 SASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPEVLTgstrlksgtaqklvLNM---ISTMTMIG 213
Cdd:cd05014   55 SNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEACP--------------LGLaptTSTTAMLA 120


                 ..
gi 488377883 214 VG 215
Cdd:cd05014  121 LG 122
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 126-209 2.01e-07

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 51.08  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 126 HLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVgPEVLTGSTRLKSGTAQKLVLNM 205
Cdd:COG1737  179 LLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPS-EEPTLRSSAFSSRVAQLALIDA 257


                 ....
gi 488377883 206 ISTM 209
Cdd:COG1737  258 LAAA 261
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 125-209 1.20e-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: 47.22  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 125 IHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVgPEVLTGSTRLKSGTAQKLVLN 204
Cdd:cd05013   56 ANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSS-EEGDFRSSAFSSRIAQLALID 134


                 ....*
gi 488377883 205 MISTM 209
Cdd:cd05013  135 ALFLA 139
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
124-207 8.39e-06

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 46.96  E-value: 8.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 124 NIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALsCNVH-SDISKNSNHVLEINVGPEVLTGSTrlKSGTAQKLV 202
Cdd:PRK00331 331 DPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAI-CNVPgSTIARESDAVLYTHAGPEIGVAST--KAFTAQLAV 407


                 ....*
gi 488377883 203 LNMIS 207
Cdd:PRK00331 408 LYLLA 412
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 63-163 2.51e-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: 41.98  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  63 IIYIGAGTSGRLGVLDAAECVPTFNVspnDIIGIIAGGQKAMTVAIEGAEDDAeqgaqdlknihlqskdiVVGISASGRT 142
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGI---EVVALIATELEHASLLSLLRKGDV-----------------VIALSYSGRT 60

                         90       100
                 ....*....|....*....|.
gi 488377883 143 PYVKGALDYANKLNAETVALS 163
Cdd:cd04795   61 EELLAALEIAKELGIPVIAIT 81
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 14-185 2.72e-05

D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 44.97  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  14 MHLDEMNLKDALKTMNQEDQfvpkAIEPVIPNLTKVIESAIQR-FNNGGRIIYIGAGTSGRLGVLDAAecvpTFN----- 87
Cdd:COG0794    1 MTDAEDILESAREVLEIEAE----ALAALAERLDESFEKAVELiLNCKGRVVVTGMGKSGHIARKIAA----TLAstgtp 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  88 ---VSPNDiigiiaggqkamtvAIEGaeddaeqgaqDLKNIhlQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSC 164
Cdd:COG0794   73 affLHPAE--------------ASHG----------DLGMI--TPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITG 126

                        170       180
                 ....*....|....*....|.
gi 488377883 165 NVHSDISKNSNHVLEINVGPE 185
Cdd:COG0794  127 NPDSTLARAADVVLDLPVERE 147
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 119-208 2.82e-05

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 45.40  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 119 AQDLKNIHLQSKDI-VVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPEVLTGSTrlKSGT 197
Cdd:PTZ00295 358 ASELTLYRLPDEDAgVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVAST--KAFT 435

                         90
                 ....*....|.
gi 488377883 198 AQKLVLNMIST 208
Cdd:PTZ00295 436 SQVTVLSLIAL 446
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 131-207 5.13e-04

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 41.27  E-value: 5.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488377883 131 DIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPEVLTGSTrlKSGTAQKLVLNMIS 207
Cdd:PLN02981 412 DTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVAST--KAYTSQIVAMTMLA 486
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 127-180 6.48e-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: 39.87  E-value: 6.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377883 127 LQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEI 180
Cdd:cd05005   73 IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVI 126
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 127-207 7.09e-04

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 41.02  E-value: 7.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883 127 LQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVLEINVGPEVLTGSTrlKSGTAQKLVLNMI 206
Cdd:PTZ00394 399 IQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVAST--KAYTSQVVVLTLV 476


                 .
gi 488377883 207 S 207
Cdd:PTZ00394 477 A 477
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 37-163 8.17e-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: 39.42  E-value: 8.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377883  37 KAIEPVIPNLTKVIESAIQRFNNGGRIIYIGAGTSGRLGVLDAAECVPTFNVSPNDIIGIIAGGQKAMTVAIeGAEDDAE 116
Cdd:cd05006   10 ALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTTDTSILTAI-ANDYGYE 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488377883 117 QGAQDLKNIHLQSKDIVVGISASGRTPYVKGALDYANKLNAETVALS 163
Cdd:cd05006   89 EVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALT 135
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
127-178 6.16e-03

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 37.43  E-value: 6.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488377883 127 LQSKDIVVGISASGRTPYVKGALDYANKLNAETVALSCNVHSDISKNSNHVL 178
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 128-163 7.22e-03

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 36.76  E-value: 7.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 488377883 128 QSKDIVVGISASGRTPYVKGALDYANKLNAETVALS 163
Cdd:PRK13937 105 RPGDVLIGISTSGNSPNVLAALEKARELGMKTIGLT 140
 
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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