|
Name |
Accession |
Description |
Interval |
E-value |
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
1-294 |
1.53e-180 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 499.31 E-value: 1.53e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 1 MLENLSTEHRNEKTTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDA 80
Cdd:PRK05441 2 MLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 81 VECPPTFGTDDKMVQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGAST 160
Cdd:PRK05441 82 SECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 161 ASISCNKNAEISKYAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRI 240
Cdd:PRK05441 162 IGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446815120 241 IVEATGVSYEVAAEYYEKANRNVKVAIVMVLLQCEYGEALEKLKEAKGFVKKAL 294
Cdd:PRK05441 242 VMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKAL 295
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
1-294 |
2.06e-178 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 493.84 E-value: 2.06e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 1 MLENLSTEHRNEKTTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDA 80
Cdd:COG2103 3 DLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 81 VECPPTFGTDDKMVQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGAST 160
Cdd:COG2103 83 SECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGALT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 161 ASISCNKNAEISKYAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRI 240
Cdd:COG2103 163 VAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIRI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446815120 241 IVEATGVSYEVAAEYYEKANRNVKVAIVMVLLQCEYGEALEKLKEAKGFVKKAL 294
Cdd:COG2103 243 VMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKAL 296
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
14-269 |
1.26e-138 |
|
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: 391.50 E-value: 1.26e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 14 TTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDAVECPPTFGTDDKM 93
Cdd:cd05007 2 SADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 94 VQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISK 173
Cdd:cd05007 82 VVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 174 YAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRIIVEATGVSYEVAA 253
Cdd:cd05007 162 LADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEAE 241
|
250
....*....|....*.
gi 446815120 254 EYYEKANRNVKVAIVM 269
Cdd:cd05007 242 AALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
5-294 |
3.44e-120 |
|
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: 346.06 E-value: 3.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 5 LSTEHRNEKTTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDAVECP 84
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 85 PTFGTDDKMVQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASIS 164
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 165 CNKNAEISKYAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRIIVEA 244
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446815120 245 TGVSYEVAAEYYEKANRNVKVAIVMVLLQCEYGEALEKLKEAKGFVKKAL 294
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
128-210 |
3.36e-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. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 45.75 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 128 LNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETGAEILTGSTrlKAGTAQKLVLNMI 207
Cdd:pfam01380 51 VDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDAL 128
|
...
gi 446815120 208 STA 210
Cdd:pfam01380 129 AVA 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
1-294 |
1.53e-180 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 499.31 E-value: 1.53e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 1 MLENLSTEHRNEKTTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDA 80
Cdd:PRK05441 2 MLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 81 VECPPTFGTDDKMVQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGAST 160
Cdd:PRK05441 82 SECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 161 ASISCNKNAEISKYAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRI 240
Cdd:PRK05441 162 IGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446815120 241 IVEATGVSYEVAAEYYEKANRNVKVAIVMVLLQCEYGEALEKLKEAKGFVKKAL 294
Cdd:PRK05441 242 VMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKAL 295
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
1-294 |
2.06e-178 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 493.84 E-value: 2.06e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 1 MLENLSTEHRNEKTTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDA 80
Cdd:COG2103 3 DLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 81 VECPPTFGTDDKMVQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGAST 160
Cdd:COG2103 83 SECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGALT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 161 ASISCNKNAEISKYAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRI 240
Cdd:COG2103 163 VAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIRI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446815120 241 IVEATGVSYEVAAEYYEKANRNVKVAIVMVLLQCEYGEALEKLKEAKGFVKKAL 294
Cdd:COG2103 243 VMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKAL 296
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
5-294 |
2.86e-143 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 404.84 E-value: 2.86e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 5 LSTEHRNEKTTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDAVECP 84
Cdd:PRK12570 2 LVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASECP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 85 PTFGTDDKMVQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASIS 164
Cdd:PRK12570 82 PTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 165 CNKNAEISKYAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRIIVEA 244
Cdd:PRK12570 162 CNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446815120 245 TGVSYEVAAEYYEKANRNVKVAIVMVLLQCEYGEALEKLKEAKGFVKKAL 294
Cdd:PRK12570 242 TGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAI 291
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
14-269 |
1.26e-138 |
|
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: 391.50 E-value: 1.26e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 14 TTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDAVECPPTFGTDDKM 93
Cdd:cd05007 2 SADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 94 VQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISK 173
Cdd:cd05007 82 VVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 174 YAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRIIVEATGVSYEVAA 253
Cdd:cd05007 162 LADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEAE 241
|
250
....*....|....*.
gi 446815120 254 EYYEKANRNVKVAIVM 269
Cdd:cd05007 242 AALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
5-294 |
3.44e-120 |
|
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: 346.06 E-value: 3.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 5 LSTEHRNEKTTNLDEMSIKEVLQSMNEEDRTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDAVECP 84
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 85 PTFGTDDKMVQGFIAGGLKAFTKAVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASIS 164
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 165 CNKNAEISKYAKLNVEVETGAEILTGSTRLKAGTAQKLVLNMISTASMIGVGKVYKNLMVDVQSTNEKLVERSKRIIVEA 244
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446815120 245 TGVSYEVAAEYYEKANRNVKVAIVMVLLQCEYGEALEKLKEAKGFVKKAL 294
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
128-208 |
3.11e-09 |
|
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: 54.04 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 128 LNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETGAEILTGSTrlKAGTAQKLVLNMI 207
Cdd:cd05008 44 LDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEISVAAT--KAFTSQLLALLLL 121
|
.
gi 446815120 208 S 208
Cdd:cd05008 122 A 122
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
34-183 |
1.98e-06 |
|
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: 47.12 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 34 RTVALAVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTSGRLGILDAVEcpptfgtddkMVQGFIAG--GLKAFTKAVEG 111
Cdd:cd05006 6 QLKEALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAE----------LVKRFEKErpGLPAIALTTDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 112 A--------EDREELAEEDLKSIGlNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVET 183
Cdd:cd05006 76 SiltaiandYGYEEVFSRQVEALG-QPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPS 154
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
128-210 |
3.36e-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. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 45.75 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 128 LNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETGAEILTGSTrlKAGTAQKLVLNMI 207
Cdd:pfam01380 51 VDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDAL 128
|
...
gi 446815120 208 STA 210
Cdd:pfam01380 129 AVA 131
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
128-210 |
4.43e-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: 45.30 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 128 LNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETgAEILTGSTRLKAGTAQKLVLNMI 207
Cdd:cd05013 58 LTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSS-EEGDFRSSAFSSRIAQLALIDAL 136
|
...
gi 446815120 208 STA 210
Cdd:cd05013 137 FLA 139
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
62-192 |
6.53e-06 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 44.84 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 62 GRLIYIGAGTSGRLGildavecpptfgtdDKMVQGFIAGGLKAF----TKAVEGaedreelaeeDLKSIglNEKDTVIGI 137
Cdd:cd05014 1 GKVVVTGVGKSGHIA--------------RKIAATLSSTGTPAFflhpTEALHG----------DLGMV--TPGDVVIAI 54
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815120 138 AASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYA--KLNVEVETGAEIL----TGST 192
Cdd:cd05014 55 SNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSdvVLDLPVEEEACPLglapTTST 115
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
128-210 |
2.04e-05 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 45.30 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 128 LNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETgAEILTGSTRLKAGTAQKLVLNMI 207
Cdd:COG1737 180 LGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPS-EEPTLRSSAFSSRVAQLALIDAL 258
|
...
gi 446815120 208 STA 210
Cdd:COG1737 259 AAA 261
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
64-164 |
2.60e-04 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 39.28 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 64 LIYIGAGTSGRLGILDAVECPPTFGTDdkmVQGFIAGGLKAFTKAVEGAEDreelaeedlksiglnekDTVIGIAASGRT 143
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIE---VVALIATELEHASLLSLLRKG-----------------DVVIALSYSGRT 60
|
90 100
....*....|....*....|.
gi 446815120 144 PYVIGGLKYAHSVGASTASIS 164
Cdd:cd04795 61 EELLAALEIAKELGIPVIAIT 81
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
129-186 |
4.18e-04 |
|
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: 41.42 E-value: 4.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446815120 129 NEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETGAE 186
Cdd:COG2222 81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPE 138
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
39-164 |
4.30e-04 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 433326 [Multi-domain] Cd Length: 138 Bit Score: 39.50 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 39 AVEKEIEHIEKVVQTVIKSFEEEGRLIYIGAGTS--------GRLGILDAVE---CPPTFGTDDkmvqgfiagglkAFTK 107
Cdd:pfam13580 13 VVETQADAIEKAADLIAASLANGGKVYAFGTGHSaapaeelfARAGGLAGFEpilLPALALHTD------------ASAT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446815120 108 AVEGAEDREELAEEDLKSIGLNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASIS 164
Cdd:pfam13580 81 ISTALERDEGYARQILALYPGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALT 137
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
132-210 |
2.19e-03 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 39.35 E-value: 2.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446815120 132 DTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETGAEILTGSTrlKAGTAQKLVLNMISTA 210
Cdd:PLN02981 412 DTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVAST--KAYTSQIVAMTMLALA 488
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
128-182 |
2.39e-03 |
|
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: 37.94 E-value: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446815120 128 LNEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVE 182
Cdd:cd05005 73 IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIP 127
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
129-294 |
4.56e-03 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 38.46 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 129 NEKDTVIGIAASGRTPYVIGGLKYAHSVGASTASISCNKNAEISKYAKLNVEVETGAEILTGSTrlKAGTAQKLVLnmis 208
Cdd:PTZ00295 368 DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVAST--KAFTSQVTVL---- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815120 209 taSMIGVGKVYKNLMVDVQSTNEKLVERSKRIIVeATGVSYEVAAEYYEK-ANRNVKVAIVMVLLQ-CEYGEALE---KL 283
Cdd:PTZ00295 442 --SLIALWFAQNKEYSCSNYKCSSLINSLHRLPT-YIGMTLKSCEEQCKRiAEKLKNAKSMFILGKgLGYPIALEgalKI 518
|
170
....*....|....*.
gi 446815120 284 KE-----AKGFVKKAL 294
Cdd:PTZ00295 519 KEityihAEGFSGGAL 534
|
|
| |
