|
Name |
Accession |
Description |
Interval |
E-value |
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
3-299 |
0e+00 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 539.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 3 IDLGHLVTESRNHHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILD 82
Cdd:PRK05441 1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 83 ASECPPTYGTPHDMVIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAV 162
Cdd:PRK05441 81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 163 TGAISCNPDSPIAQRADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIR 242
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2136541928 243 IVMQATECDRATAEHALSQCQRHCKTAILMILAGVNAQQATQLLAQNKGFIRQALAK 299
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
3-299 |
0e+00 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 537.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 3 IDLGHLVTESRNHHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILD 82
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 83 ASECPPTYGTPHDMVIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAV 162
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 163 TGAISCNPDSPIAQRADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIR 242
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2136541928 243 IVMQATECDRATAEHALSQCQRHCKTAILMILAGVNAQQATQLLAQNKGFIRQALAK 299
Cdd:COG2103 242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALAA 298
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
17-272 |
2.42e-151 |
|
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: 423.86 E-value: 2.42e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 17 SEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILDASECPPTYGTPHDM 96
Cdd:cd05007 2 SADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 97 VIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQ 176
Cdd:cd05007 82 VVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 177 RADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIRIVMQATECDRATAE 256
Cdd:cd05007 162 LADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEAE 241
|
250
....*....|....*.
gi 2136541928 257 HALSQCQRHCKTAILM 272
Cdd:cd05007 242 AALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
8-297 |
2.11e-147 |
|
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: 415.40 E-value: 2.11e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 8 LVTESRNHHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILDASECP 87
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 88 PTYGTPHDMVIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAIS 167
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 168 CNPDSPIAQRADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIRIVMQA 247
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2136541928 248 TECDRATAEHALSQCQRHCKTAILMILAGVNAQQATQLLAQNKGFIRQAL 297
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
134-212 |
3.22e-08 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 51.53 E-value: 3.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136541928 134 KDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITPIVGPEVVTGSsrMKAGTAQKLILNMITT 212
Cdd:pfam01380 54 DDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAS--TKSITAQLAALDALAV 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
3-299 |
0e+00 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 539.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 3 IDLGHLVTESRNHHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILD 82
Cdd:PRK05441 1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 83 ASECPPTYGTPHDMVIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAV 162
Cdd:PRK05441 81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 163 TGAISCNPDSPIAQRADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIR 242
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2136541928 243 IVMQATECDRATAEHALSQCQRHCKTAILMILAGVNAQQATQLLAQNKGFIRQALAK 299
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
3-299 |
0e+00 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 537.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 3 IDLGHLVTESRNHHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILD 82
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 83 ASECPPTYGTPHDMVIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAV 162
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 163 TGAISCNPDSPIAQRADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIR 242
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2136541928 243 IVMQATECDRATAEHALSQCQRHCKTAILMILAGVNAQQATQLLAQNKGFIRQALAK 299
Cdd:COG2103 242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALAA 298
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
7-298 |
4.22e-164 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 457.62 E-value: 4.22e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 7 HLVTESRNHHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILDASEC 86
Cdd:PRK12570 1 HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 87 PPTYGTPHDMVIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAI 166
Cdd:PRK12570 81 PPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 167 SCNPDSPIAQRADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIRIVMQ 246
Cdd:PRK12570 161 SCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2136541928 247 ATECDRATAEHALSQCQRHCKTAILMILAGVNAQQATQLLAQNKGFIRQALA 298
Cdd:PRK12570 241 ATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIE 292
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
17-272 |
2.42e-151 |
|
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: 423.86 E-value: 2.42e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 17 SEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILDASECPPTYGTPHDM 96
Cdd:cd05007 2 SADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 97 VIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQ 176
Cdd:cd05007 82 VVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 177 RADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIRIVMQATECDRATAE 256
Cdd:cd05007 162 LADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEAE 241
|
250
....*....|....*.
gi 2136541928 257 HALSQCQRHCKTAILM 272
Cdd:cd05007 242 AALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
8-297 |
2.11e-147 |
|
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: 415.40 E-value: 2.11e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 8 LVTESRNHHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGRLGILDASECP 87
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 88 PTYGTPHDMVIGLIAGGHKAILQAVENAEDNVQLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAIS 167
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 168 CNPDSPIAQRADIAITPIVGPEVVTGSSRMKAGTAQKLILNMITTGAMIKMGKVFGNLMVDVEATNAKLIERQIRIVMQA 247
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2136541928 248 TECDRATAEHALSQCQRHCKTAILMILAGVNAQQATQLLAQNKGFIRQAL 297
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
127-211 |
1.41e-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: 63.28 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 127 RQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITPIVGPEVvtGSSRMKAGTAQKLI 206
Cdd:cd05008 40 RRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEI--SVAATKAFTSQLLA 117
|
....*
gi 2136541928 207 LNMIT 211
Cdd:cd05008 118 LLLLA 122
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
42-182 |
3.06e-10 |
|
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: 58.29 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 42 AVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGrlgiLDASecpptygtpH---DMVIGL---------IA-GGHKAI 108
Cdd:cd05006 11 LLELLAEAIEQAAQLLAEALLNGGKILICGNGGSA----ADAQ---------HfaaELVKRFekerpglpaIAlTTDTSI 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2136541928 109 LQAVENAEdnvqlGAEDL--RQLN--FNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAI 182
Cdd:cd05006 78 LTAIANDY-----GYEEVfsRQVEalGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEI 150
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
42-194 |
3.56e-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: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 42 AVEATLPHIARLVDKVvtAFSQGGRLIYCGAGTSGRLGILDASECPPTYGTPHDMVIGLIAGGHKAILQavenaednvql 121
Cdd:COG2222 14 ALAALAAAIAALLARL--RAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLK----------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136541928 122 gaedlrqlnfNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITPIVGPE---VVTGS 194
Cdd:COG2222 81 ----------LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEksvAATKS 146
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
128-213 |
2.10e-09 |
|
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: 54.93 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 128 QLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAItPIVGPEVVTGSSRMKAGTAQKLIL 207
Cdd:cd05013 55 AANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVL-LVSSEEGDFRSSAFSSRIAQLALI 133
|
....*.
gi 2136541928 208 NMITTG 213
Cdd:cd05013 134 DALFLA 139
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
123-220 |
2.57e-09 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 56.86 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 123 AEDLRQLNfnAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITpIVGPEVVTGSSRMKAGTA 202
Cdd:COG1737 174 AESAALLG--PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY-VPSEEPTLRSSAFSSRVA 250
|
90
....*....|....*...
gi 2136541928 203 QKLILNMITTGAMIKMGK 220
Cdd:COG1737 251 QLALIDALAAAVAQRDGD 268
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
134-212 |
3.22e-08 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 51.53 E-value: 3.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136541928 134 KDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITPIVGPEVVTGSsrMKAGTAQKLILNMITT 212
Cdd:pfam01380 54 DDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAS--TKSITAQLAALDALAV 130
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
133-190 |
1.09e-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: 49.85 E-value: 1.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2136541928 133 AKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITPIVGPEV 190
Cdd:cd05014 47 PGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEA 104
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
42-167 |
1.70e-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.
Pssm-ID: 433326 [Multi-domain] Cd Length: 138 Bit Score: 49.52 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 42 AVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTSGrlgiLDASECPPTYGT------PHDMVIGLIAGGHKAILQAVENA 115
Cdd:pfam13580 13 VVETQADAIEKAADLIAASLANGGKVYAFGTGHSA----APAEELFARAGGlagfepILLPALALHTDASATISTALERD 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2136541928 116 EDnvqLGAEDLRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAIS 167
Cdd:pfam13580 89 EG---YARQILALYPGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALT 137
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
130-182 |
1.72e-07 |
|
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: 50.27 E-value: 1.72e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2136541928 130 NFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAI 182
Cdd:cd05005 72 AIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
|
|
| PRK15482 |
PRK15482 |
HTH-type transcriptional regulator MurR; |
15-244 |
6.15e-07 |
|
HTH-type transcriptional regulator MurR;
Pssm-ID: 185379 [Multi-domain] Cd Length: 285 Bit Score: 49.70 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 15 HHSEHIDTLSTLEMLKVINNEDKKVPFAVEATLPHIARLvDKVVTAFSQGGRLIYCGAGTSGRLGildasecpptygtpH 94
Cdd:PRK15482 87 HLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARL-QKIIEVISKAPFIQITGLGGSALVG--------------R 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 95 DMVIGLIAGGHKAILQAVENAEDNVqlgAEDLRQlnfnaKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPI 174
Cdd:PRK15482 152 DLSFKLMKIGYRVACEADTHVQATV---SQALKK-----GDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPL 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 175 AQRADIAITPIVGpEVVTGSSRMKAGTAQKLILNMITTGaMIKMGkvfgnlmvDVEATnaKLIERQIRIV 244
Cdd:PRK15482 224 RRLAHFTLDTVSG-ETEWRSSSMSTRTAQNSVTDLLFVG-LVQLN--------DVESL--KMIQRSSELT 281
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
42-186 |
2.16e-05 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 44.46 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 42 AVEATLPHIARLVDKVVTAFSQGGRLIYCGAGTS------------GRLgildASECPP------TYGTphdmvigliag 103
Cdd:PRK13937 16 FLESLLEAIAKVAEALIEALANGGKILLCGNGGSaadaqhiaaelvGRF----KKERPAlpaialTTDT----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 104 ghkAILQAVENaednvQLGAEDL--RQLNFNAK--DVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRAD 179
Cdd:PRK13937 81 ---SALTAIGN-----DYGFERVfsRQVEALGRpgDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCD 152
|
170
....*....|...
gi 2136541928 180 IAI------TPIV 186
Cdd:PRK13937 153 HLLivpsddTPRI 165
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
135-183 |
3.93e-05 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 44.37 E-value: 3.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2136541928 135 DVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAIT 183
Cdd:PRK11337 189 DVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVIC 237
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
131-182 |
4.04e-05 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 44.61 E-value: 4.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2136541928 131 FNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAI 182
Cdd:PRK11382 90 LDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSI 141
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
67-167 |
5.32e-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: 41.21 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 67 LIYCGAGTSGRLGILDASECPPTYGTPhdmVIGLIAGGHKAILQAVENAEDnvqlgaedlrqlnfnakDVLVGIAASGRT 146
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIE---VVALIATELEHASLLSLLRKG-----------------DVVIALSYSGRT 60
|
90 100
....*....|....*....|.
gi 2136541928 147 PYVIGALEYARSLGAVTGAIS 167
Cdd:cd04795 61 EELLAALEIAKELGIPVIAIT 81
|
|
| PRK14101 |
PRK14101 |
bifunctional transcriptional regulator/glucokinase; |
135-217 |
1.05e-04 |
|
bifunctional transcriptional regulator/glucokinase;
Pssm-ID: 184507 [Multi-domain] Cd Length: 638 Bit Score: 43.75 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 135 DVLVGIAASGRTPYVIGALEYARSLGAVTGAIsCNPDSPIAQRADIAItPIVGPEVVTGSSRMKAGTAQKLILNMITTGA 214
Cdd:PRK14101 517 DVIVAVSKSGRAPELLRVLDVAMQAGAKVIAI-TSSNTPLAKRATVAL-ETDHIEMRESQLSMISRILHLVMIDILAVGV 594
|
...
gi 2136541928 215 MIK 217
Cdd:PRK14101 595 AIR 597
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
131-183 |
1.79e-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: 1.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2136541928 131 FNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAIT 183
Cdd:cd05710 45 LTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIV 97
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
111-210 |
6.49e-04 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 41.02 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 111 AVENAEDNVQlgaedlRQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITPIVGPEV 190
Cdd:PTZ00394 385 SVENASDFLD------RRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEV 458
|
90 100
....*....|....*....|
gi 2136541928 191 VTGSSrmKAGTAQKLILNMI 210
Cdd:PTZ00394 459 GVAST--KAYTSQVVVLTLV 476
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
133-182 |
6.72e-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: 40.73 E-value: 6.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2136541928 133 AKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAI 182
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVL 140
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
123-210 |
4.34e-03 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 38.58 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136541928 123 AEDL--RQLNFNAKDVLVGIAASGRTPYVIGALEYARSLGAVTGAISCNPDSPIAQRADIAITPIVGPEVvtGSSRMKAG 200
Cdd:PLN02981 398 ASDLldRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEI--GVASTKAY 475
|
90
....*....|
gi 2136541928 201 TAQKLILNMI 210
Cdd:PLN02981 476 TSQIVAMTML 485
|
|
| |
