|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
5-296 |
1.42e-167 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 466.48 E-value: 1.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 5 GLTTEARNEATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALDAIEL 84
Cdd:PRK12570 1 HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 85 TPTYSVSPERAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISV 164
Cdd:PRK12570 81 PPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 165 TCNNQSPMNQLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATNIIKE 244
Cdd:PRK12570 161 SCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488289990 245 AAEIEESQAKEYLEAAQLEVAPAIVMAKAHVDFQKAKQLLAEHDGRISEVLA 296
Cdd:PRK12570 241 ATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIE 292
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
1-296 |
4.15e-161 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 450.31 E-value: 4.15e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 1 MNLEGLTTEARNEATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALD 80
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 81 AIELTPTYSVSPERAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGAL 160
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 161 TISVTCNNQSPMNQLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATN 240
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289990 241 IIKEAAEIEESQAKEYLEAAQLEVAPAIVMAKAHVDFQKAKQLLAEHDGRISEVLA 296
Cdd:COG2103 242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALA 297
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
14-270 |
2.56e-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: 383.03 E-value: 2.56e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 14 ATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALDAIELTPTYSVSPE 93
Cdd:cd05007 1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 94 RAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMN 173
Cdd:cd05007 81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 174 QLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATNIIKEAAEIEESQA 253
Cdd:cd05007 161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
|
250
....*....|....*..
gi 488289990 254 KEYLEAAQLEVAPAIVM 270
Cdd:cd05007 241 EAALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
6-295 |
6.31e-118 |
|
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: 340.67 E-value: 6.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 6 LTTEARNEATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALDAIELT 85
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 86 PTYSVSPERAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVT 165
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 166 CNNQSPMNQLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATNIIKEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488289990 246 AEIEESQAKEYLEAAQLEVAPAIVMAKAHVDFQKAKQLLAEHDGRISEVL 295
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
129-208 |
1.06e-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: 52.69 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 129 LTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGIAPIVGPEVITGSTrmKAGSAQKMVLNMF 208
Cdd:pfam01380 51 VDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDAL 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
5-296 |
1.42e-167 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 466.48 E-value: 1.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 5 GLTTEARNEATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALDAIEL 84
Cdd:PRK12570 1 HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 85 TPTYSVSPERAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISV 164
Cdd:PRK12570 81 PPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 165 TCNNQSPMNQLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATNIIKE 244
Cdd:PRK12570 161 SCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488289990 245 AAEIEESQAKEYLEAAQLEVAPAIVMAKAHVDFQKAKQLLAEHDGRISEVLA 296
Cdd:PRK12570 241 ATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIE 292
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
1-296 |
4.15e-161 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 450.31 E-value: 4.15e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 1 MNLEGLTTEARNEATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALD 80
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 81 AIELTPTYSVSPERAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGAL 160
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 161 TISVTCNNQSPMNQLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATN 240
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289990 241 IIKEAAEIEESQAKEYLEAAQLEVAPAIVMAKAHVDFQKAKQLLAEHDGRISEVLA 296
Cdd:COG2103 242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALA 297
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
1-296 |
2.95e-158 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 442.69 E-value: 2.95e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 1 MNLEGLTTEARNEATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALD 80
Cdd:PRK05441 1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 81 AIELTPTYSVSPERAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGAL 160
Cdd:PRK05441 81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 161 TISVTCNNQSPMNQLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATN 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289990 241 IIKEAAEIEESQAKEYLEAAQLEVAPAIVMAKAHVDFQKAKQLLAEHDGRISEVLA 296
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
14-270 |
2.56e-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: 383.03 E-value: 2.56e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 14 ATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALDAIELTPTYSVSPE 93
Cdd:cd05007 1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 94 RAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMN 173
Cdd:cd05007 81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 174 QLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATNIIKEAAEIEESQA 253
Cdd:cd05007 161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
|
250
....*....|....*..
gi 488289990 254 KEYLEAAQLEVAPAIVM 270
Cdd:cd05007 241 EAALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
6-295 |
6.31e-118 |
|
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: 340.67 E-value: 6.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 6 LTTEARNEATKKIDQVSTLEMVTLINQEDQKVAQAIEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSGRLGALDAIELT 85
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 86 PTYSVSPERAFGILAGGEKAMYQAIEGAEDSKELAIEDLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVT 165
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 166 CNNQSPMNQLAEIGIAPIVGPEVITGSTRMKAGSAQKMVLNMFSTGIMVKVGNIYQNLMVNVQPTNEKLMQRATNIIKEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488289990 246 AEIEESQAKEYLEAAQLEVAPAIVMAKAHVDFQKAKQLLAEHDGRISEVL 295
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
132-209 |
2.92e-10 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 57.12 E-value: 2.92e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289990 132 RDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGIAPIVGPEVitGSTRMKAGSAQKMVLNMFS 209
Cdd:cd05008 47 DTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEI--SVAATKAFTSQLLALLLLA 122
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
129-208 |
1.06e-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: 52.69 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 129 LTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGIAPIVGPEVITGSTrmKAGSAQKMVLNMF 208
Cdd:pfam01380 51 VDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDAL 128
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
58-177 |
3.13e-08 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 54.13 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 58 RFKKGGRLIYCGAGTSGRLGaldaieltptYSVSP--ERAFGILAggekamyQAIEGAEdskelAIEDLTQHQLtARDVV 135
Cdd:COG2222 30 RAKPPRRVVLVGAGSSDHAA----------QAAAYllERLLGIPV-------AALAPSE-----LVVYPAYLKL-EGTLV 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488289990 136 IAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAE 177
Cdd:COG2222 87 VAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAAD 128
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
63-178 |
1.11e-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: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 63 GRLIYCGAGTSGRLgaldAIELTPTYSVSPERAFgILAGGEkamyqAIEGaedskelaieDLTQhqLTARDVVIAIAASG 142
Cdd:cd05014 1 GKVVVTGVGKSGHI----ARKIAATLSSTGTPAF-FLHPTE-----ALHG----------DLGM--VTPGDVVIAISNSG 58
|
90 100 110
....*....|....*....|....*....|....*.
gi 488289990 143 RTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEI 178
Cdd:cd05014 59 ETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDV 94
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
128-215 |
5.03e-07 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 49.93 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 128 QLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGIaPIVGPEVITGSTRMKAGSAQKMVLNM 207
Cdd:COG1737 179 LLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVL-YVPSEEPTLRSSAFSSRVAQLALIDA 257
|
....*...
gi 488289990 208 FSTGIMVK 215
Cdd:COG1737 258 LAAAVAQR 265
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
60-165 |
2.91e-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: 433326 [Multi-domain] Cd Length: 138 Bit Score: 46.05 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 60 KKGGRLIYCGAGTSgrlgALDAIELTPtysvspeRAFGI----------LAGGEKAMYQAIEGAEDSKELAIEDLTQHQL 129
Cdd:pfam13580 33 ANGGKVYAFGTGHS----AAPAEELFA-------RAGGLagfepillpaLALHTDASATISTALERDEGYARQILALYPG 101
|
90 100 110
....*....|....*....|....*....|....*.
gi 488289990 130 TARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVT 165
Cdd:pfam13580 102 RPGDVLIVISNSGINAVPVEAALEAKERGMKVIALT 137
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
133-178 |
4.23e-06 |
|
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: 46.03 E-value: 4.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488289990 133 DVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEI 178
Cdd:cd05005 77 DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADV 122
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
25-180 |
1.63e-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: 44.42 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 25 EMVTLINQEDQKVAQAIEKVlpqiaaaIDAAAERFKKGGRLIYCGAGTSGRLGALDAIELTPTYSVsPERAFGILA-GGE 103
Cdd:cd05006 3 ESIQLKEALLELLAEAIEQA-------AQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEK-ERPGLPAIAlTTD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 104 KAMYQAIegAEDskeLAIEDLTQHQLTAR----DVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIG 179
Cdd:cd05006 75 TSILTAI--AND---YGYEEVFSRQVEALgqpgDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIE 149
|
.
gi 488289990 180 I 180
Cdd:cd05006 150 I 150
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
65-165 |
2.26e-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: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 65 LIYCGAGTSGRLGALDAIELTPTYSVspeRAFGILAGGEKAMYQAIEGAEDskelaiedltqhqltarDVVIAIAASGRT 144
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGI---EVVALIATELEHASLLSLLRKG-----------------DVVIALSYSGRT 60
|
90 100
....*....|....*....|.
gi 488289990 145 PYAVSAIEYGKKVGALTISVT 165
Cdd:cd04795 61 EELLAALEIAKELGIPVIAIT 81
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
57-207 |
1.04e-04 |
|
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: 41.45 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 57 ERFKKGGRLIYCGAGTSGRLgALDAieltptysvspERAFGILagGEKAMYqaiegAEDSKELAIEDLTqhqLTARDVVI 136
Cdd:cd05013 8 DLLAKARRIYIFGVGSSGLV-AEYL-----------AYKLLRL--GKPVVL-----LSDPHLQLMSAAN---LTPGDVVI 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289990 137 AIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGIaPIVGPEVITGSTRMKAGSAQKMVLNM 207
Cdd:cd05013 66 AISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVL-LVSSEEGDFRSSAFSSRIAQLALIDA 135
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
123-181 |
1.81e-04 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 42.68 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289990 123 DLTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGIA 181
Cdd:PRK11382 84 DNTPYRLDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSID 142
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
129-180 |
3.32e-04 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 41.67 E-value: 3.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488289990 129 LTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGI 180
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
|
|
| PRK15482 |
PRK15482 |
HTH-type transcriptional regulator MurR; |
133-225 |
1.19e-03 |
|
HTH-type transcriptional regulator MurR;
Pssm-ID: 185379 [Multi-domain] Cd Length: 285 Bit Score: 39.68 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 133 DVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEIGIAPIVGpEVITGSTRMKAGSAQKMVLNMFSTGi 212
Cdd:PRK15482 184 DVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG-ETEWRSSSMSTRTAQNSVTDLLFVG- 261
|
90
....*....|...
gi 488289990 213 MVKVGNIYQNLMV 225
Cdd:PRK15482 262 LVQLNDVESLKMI 274
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
128-178 |
1.36e-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: 39.57 E-value: 1.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488289990 128 QLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQLAEI 178
Cdd:COG0794 88 MITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADV 138
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
32-178 |
1.82e-03 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 38.68 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 32 QEDQKVAQA-IEKVLPQIAAAIDAAAERFKKGGRLIYCGAGTSgrlgALDA----IELTPTYSVsperafgilaggEKAM 106
Cdd:PRK13937 7 RESQAVMEAfLESLLEAIAKVAEALIEALANGGKILLCGNGGS----AADAqhiaAELVGRFKK------------ERPA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 107 YQAIEGAEDSKEL-AI------EDLTQHQLTA----RDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPMNQL 175
Cdd:PRK13937 71 LPAIALTTDTSALtAIgndygfERVFSRQVEAlgrpGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKEL 150
|
...
gi 488289990 176 AEI 178
Cdd:PRK13937 151 CDH 153
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
125-213 |
3.14e-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: 36.79 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289990 125 TQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVTCNNQSPmnqLAEIGIAPIVgpeviTGSTRMKAGSAQkMV 204
Cdd:cd05710 41 GPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSP---LAKLADYVIV-----YGFEIDAVEEKY-LL 111
|
....*....
gi 488289990 205 LNMFSTGIM 213
Cdd:cd05710 112 LYMLALRLL 120
|
|
| PRK02947 |
PRK02947 |
sugar isomerase domain-containing protein; |
124-165 |
8.78e-03 |
|
sugar isomerase domain-containing protein;
Pssm-ID: 179510 [Multi-domain] Cd Length: 246 Bit Score: 36.77 E-value: 8.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488289990 124 LTQHQLTARDVVIAIAASGRTPYAVSAIEYGKKVGALTISVT 165
Cdd:PRK02947 99 LDRYDIRPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVT 140
|
|
| |
