|
Name |
Accession |
Description |
Interval |
E-value |
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
1-296 |
3.25e-180 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 498.54 E-value: 3.25e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:PRK05441 1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:PRK05441 81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
1-296 |
1.40e-174 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 484.21 E-value: 1.40e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 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 |
1.34e-140 |
|
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: 396.51 E-value: 1.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 14 DTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECPPTFGVPHG 93
Cdd:cd05007 1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 94 VVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIA 173
Cdd:cd05007 81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 174 EAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEATGVTREEA 253
Cdd:cd05007 161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
|
250
....*....|....*..
gi 490521950 254 EAVLTQTEYEVKPAILM 270
Cdd:cd05007 241 EAALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
6-295 |
4.69e-130 |
|
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: 371.10 E-value: 4.69e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 6 LVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECP 85
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 86 PTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAIS 165
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 166 CNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490521950 246 TGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAAL 295
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQAL 290
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
59-207 |
8.27e-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: 50.38 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 59 LTCGGRLIYMGAGTSGRLGVldasecpptFGVPHgvvVGLIAGgpgallKAVEGaEDNAQLGEDDLKAIglNARDMVVGL 138
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIAL---------ELALK---FEEIGY------KVVEV-ELASELRHGVLALV--DEDDLVIAI 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490521950 139 AASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEALTGSTrlKSGTAQKLVLNM 207
Cdd:pfam01380 61 SYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
1-296 |
3.25e-180 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 498.54 E-value: 3.25e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:PRK05441 1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:PRK05441 81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALA 296
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
1-296 |
1.40e-174 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 484.21 E-value: 1.40e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 1 MNLGSLVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLD 80
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 81 ASECPPTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCA 160
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 161 TAAISCNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACR 240
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 241 MVMEATGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:COG2103 242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALA 297
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
6-296 |
1.40e-158 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 443.75 E-value: 1.40e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 6 LVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECP 85
Cdd:PRK12570 2 LVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASECP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 86 PTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAIS 165
Cdd:PRK12570 82 PTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 166 CNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEA 245
Cdd:PRK12570 162 CNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490521950 246 TGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAALQ 296
Cdd:PRK12570 242 TGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIE 292
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
14-270 |
1.34e-140 |
|
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: 396.51 E-value: 1.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 14 DTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECPPTFGVPHG 93
Cdd:cd05007 1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 94 VVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIA 173
Cdd:cd05007 81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 174 EAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEATGVTREEA 253
Cdd:cd05007 161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
|
250
....*....|....*..
gi 490521950 254 EAVLTQTEYEVKPAILM 270
Cdd:cd05007 241 EAALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
6-295 |
4.69e-130 |
|
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: 371.10 E-value: 4.69e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 6 LVSETRNPDTLDLDALPTLEMLRRFNEEDKRVAHAVSETLPEVAKAVDAAAAALTCGGRLIYMGAGTSGRLGVLDASECP 85
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 86 PTFGVPHGVVVGLIAGGPGALLKAVEGAEDNAQLGEDDLKAIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAIS 165
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 166 CNPGSPIAEAAEIAISPVVGPEALTGSTRLKSGTAQKLVLNMISTGAMVKCGKVYQNLMVDMKATNVKLVDRACRMVMEA 245
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490521950 246 TGVTREEAEAVLTQTEYEVKPAILMVLTGLDAQAAHARLAAHNGFLRAAL 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 ... |
129-209 |
3.69e-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: 56.74 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEALTGSTrlKSGTAQKLVLNMI 208
Cdd:cd05008 44 LDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEISVAAT--KAFTSQLLALLLL 121
|
.
gi 490521950 209 S 209
Cdd:cd05008 122 A 122
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
126-218 |
4.73e-08 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 53.01 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 126 AIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIsPVVGPEALTGSTRLKSGTAQKLVL 205
Cdd:COG1737 177 AALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVL-YVPSEEPTLRSSAFSSRVAQLALI 255
|
90
....*....|...
gi 490521950 206 NMISTGAMVKCGK 218
Cdd:COG1737 256 DALAAAVAQRDGD 268
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
126-211 |
5.87e-08 |
|
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: 50.69 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 126 AIGLNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIsPVVGPEALTGSTRLKSGTAQKLVL 205
Cdd:cd05013 55 AANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVL-LVSSEEGDFRSSAFSSRIAQLALI 133
|
....*.
gi 490521950 206 NMISTG 211
Cdd:cd05013 134 DALFLA 139
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
59-207 |
8.27e-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: 50.38 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 59 LTCGGRLIYMGAGTSGRLGVldasecpptFGVPHgvvVGLIAGgpgallKAVEGaEDNAQLGEDDLKAIglNARDMVVGL 138
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIAL---------ELALK---FEEIGY------KVVEV-ELASELRHGVLALV--DEDDLVIAI 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490521950 139 AASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEALTGSTrlKSGTAQKLVLNM 207
Cdd:pfam01380 61 SYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
130-214 |
3.43e-07 |
|
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: 50.67 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 130 NARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIspvvgpeaLTGSTRLKSGTAQKLVLNMIS 209
Cdd:COG2222 81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL--------PLPAGPEKSVAATKSFTTMLL 152
|
....*
gi 490521950 210 TGAMV 214
Cdd:COG2222 153 ALLAL 157
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
129-188 |
1.40e-05 |
|
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: 43.69 E-value: 1.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAISPVVGPEA 188
Cdd:cd05014 45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEA 104
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
65-165 |
1.51e-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: 42.75 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490521950 65 LIYMGAGTSGRLGVLDASECPPTFGVPhgvVVGLIAGGpgallkavegaednaqlGEDDLKAIGLNARDMVVGLAASGRT 144
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIE---VVALIATE-----------------LEHASLLSLLRKGDVVIALSYSGRT 60
|
90 100
....*....|....*....|.
gi 490521950 145 PYVIGGLKYARALGCATAAIS 165
Cdd:cd04795 61 EELLAALEIAKELGIPVIAIT 81
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
124-180 |
7.15e-05 |
|
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).
Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 42.50 E-value: 7.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490521950 124 LKAIGlNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:cd05006 95 VEALG-QPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEI 150
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
129-181 |
1.41e-04 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 42.68 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAIS 181
Cdd:PRK11382 90 LDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSID 142
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
133-180 |
2.21e-04 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 41.38 E-value: 2.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490521950 133 DMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:PRK13937 108 DVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLL 155
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
129-188 |
2.39e-04 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 42.05 E-value: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 129 LNARDMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI------SPVVGPEA 188
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVIcstaqgSPLLGENA 250
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
115-180 |
1.30e-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: 37.94 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490521950 115 DNAQLGEDDLkaiglnardmVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:cd05710 41 GPKRLTEKSV----------VILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
133-180 |
2.61e-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: 2.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490521950 133 DMVVGLAASGRTPYVIGGLKYARALGCATAAISCNPGSPIAEAAEIAI 180
Cdd:cd05005 77 DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
|
|
|