|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 511.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 3 IDLSKLLTERRNANSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILD 82
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 83 ASECPPTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAF 162
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 163 VAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVS 242
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1123849898 243 IVMEATDCDRPTARKALEACGRHCKTAIVMVLADLSAEAAQSLLAKNNGYIRKALSN 299
Cdd:COG2103 242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALAA 298
|
|
| 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: 502.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 3 IDLSKLLTERRNANSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILD 82
Cdd:PRK05441 1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 83 ASECPPTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAF 162
Cdd:PRK05441 81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 163 VAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVS 242
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1123849898 243 IVMEATDCDRPTARKALEACGRHCKTAIVMVLADLSAEAAQSLLAKNNGYIRKALSN 299
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
16-272 |
1.60e-145 |
|
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: 409.22 E-value: 1.60e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 16 NSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILDASECPPTFGTRPE 95
Cdd:cd05007 1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 96 QVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMA 175
Cdd:cd05007 81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 176 QLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVSIVMEATDCDRPTA 255
Cdd:cd05007 161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
|
250
....*....|....*..
gi 1123849898 256 RKALEACGRHCKTAIVM 272
Cdd:cd05007 241 EAALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
8-298 |
1.17e-138 |
|
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: 393.05 E-value: 1.17e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 8 LLTERRNANSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILDASECP 87
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 88 PTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVS 167
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 168 CNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVSIVMEA 247
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1123849898 248 TDCDRPTARKALEACGRHCKTAIVMVLADLSAEAAQSLLAKNNGYIRKALS 298
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
50-167 |
2.71e-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: 40.27 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 50 IAEVVDKVATALQAGGRLIYIGAGTSGrlgiLDASECPPTFGTRPEqVVGII-------AGGHKAILSAVENVEDnKAQG 122
Cdd:pfam13580 21 IEKAADLIAASLANGGKVYAFGTGHSA----APAEELFARAGGLAG-FEPILlpalalhTDASATISTALERDEG-YARQ 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1123849898 123 AMDLQNLNfsHRDVLVGLAASGRTPYVIGAMEYAHRQNAFV-AIVS 167
Cdd:pfam13580 95 ILALYPGR--PGDVLIVISNSGINAVPVEAALEAKERGMKViALTS 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 511.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 3 IDLSKLLTERRNANSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILD 82
Cdd:COG2103 2 MDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 83 ASECPPTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAF 162
Cdd:COG2103 82 ASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 163 VAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVS 242
Cdd:COG2103 162 TVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAIR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1123849898 243 IVMEATDCDRPTARKALEACGRHCKTAIVMVLADLSAEAAQSLLAKNNGYIRKALSN 299
Cdd:COG2103 242 IVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRKALAA 298
|
|
| 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: 502.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 3 IDLSKLLTERRNANSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILD 82
Cdd:PRK05441 1 MMLENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 83 ASECPPTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAF 162
Cdd:PRK05441 81 ASECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 163 VAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVS 242
Cdd:PRK05441 161 TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1123849898 243 IVMEATDCDRPTARKALEACGRHCKTAIVMVLADLSAEAAQSLLAKNNGYIRKALSN 299
Cdd:PRK05441 241 IVMEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRKALAE 297
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
7-299 |
1.63e-150 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 423.33 E-value: 1.63e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 7 KLLTERRNANSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILDASEC 86
Cdd:PRK12570 1 HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 87 PPTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIV 166
Cdd:PRK12570 81 PPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 167 SCNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVSIVME 246
Cdd:PRK12570 161 SCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1123849898 247 ATDCDRPTARKALEACGRHCKTAIVMVLADLSAEAAQSLLAKNNGYIRKALSN 299
Cdd:PRK12570 241 ATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRKAIEA 293
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
16-272 |
1.60e-145 |
|
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: 409.22 E-value: 1.60e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 16 NSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILDASECPPTFGTRPE 95
Cdd:cd05007 1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 96 QVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMA 175
Cdd:cd05007 81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 176 QLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVSIVMEATDCDRPTA 255
Cdd:cd05007 161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240
|
250
....*....|....*..
gi 1123849898 256 RKALEACGRHCKTAIVM 272
Cdd:cd05007 241 EAALEQAGGDVKTAILM 257
|
|
| TIGR00274 |
TIGR00274 |
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ... |
8-298 |
1.17e-138 |
|
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: 393.05 E-value: 1.17e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 8 LLTERRNANSANIDTLSTLDMLTVINQEDQQVAQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILDASECP 87
Cdd:TIGR00274 1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 88 PTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVS 167
Cdd:TIGR00274 81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 168 CNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKLIERQVSIVMEA 247
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1123849898 248 TDCDRPTARKALEACGRHCKTAIVMVLADLSAEAAQSLLAKNNGYIRKALS 298
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFLRQALD 291
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
128-211 |
2.48e-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: 54.43 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 128 NLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTrlKAGTAQKLVL 207
Cdd:cd05008 41 RPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEISVAAT--KAFTSQLLAL 118
|
....
gi 1123849898 208 NMIS 211
Cdd:cd05008 119 LLLA 122
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
34-182 |
2.90e-07 |
|
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: 49.43 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 34 QEDQQVAQAI-TPYLPQIAEVVDKVATALQAGGRLIYIGAGTSGRLGILDASECPPTFGT-RPEQVVgiIA-GGHKAILS 110
Cdd:cd05006 2 QESIQLKEALlELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKeRPGLPA--IAlTTDTSILT 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1123849898 111 AVENVEDNKAQGAMDLQNLnFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAI 182
Cdd:cd05006 80 AIANDYGYEEVFSRQVEAL-GQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEI 150
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
132-219 |
1.16e-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: 46.77 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 132 SHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAITPVVGPEVVTgstrlkagtaqklvLNM-- 209
Cdd:cd05014 46 TPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEACP--------------LGLap 111
|
90
....*....|.
gi 1123849898 210 -ISTGAMIRVG 219
Cdd:cd05014 112 tTSTTAMLALG 122
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
134-196 |
2.28e-06 |
|
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: 48.36 E-value: 2.28e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123849898 134 RDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTR 196
Cdd:COG2222 83 GTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATK 145
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
124-213 |
8.62e-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: 44.53 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 124 MDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAItPVVGPEVVTGSTRLKAGTAQ 203
Cdd:cd05013 51 QLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVL-LVSSEEGDFRSSAFSSRIAQ 129
|
90
....*....|
gi 1123849898 204 KLVLNMISTG 213
Cdd:cd05013 130 LALIDALFLA 139
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
123-236 |
1.99e-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: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 123 AMDLQNLNfsHRDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAI-TPVVGPEVVTGSTRLKagT 201
Cdd:COG1737 174 AESAALLG--PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLyVPSEEPTLRSSAFSSR--V 249
|
90 100 110
....*....|....*....|....*....|....*
gi 1123849898 202 AQKLVLNMISTGAMIRVGKVYSNLMVDVEATNAKL 236
Cdd:COG1737 250 AQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
135-182 |
3.18e-05 |
|
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: 43.72 E-value: 3.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1123849898 135 DVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAI 182
Cdd:cd05005 77 DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
67-167 |
2.27e-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: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 67 LIYIGAGTSGRLGILDASECPPTFGtrpEQVVGIIAGGhkailsavenvednkaqGAMDLQNLNFSHRDVLVGLAASGRT 146
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTG---IEVVALIATE-----------------LEHASLLSLLRKGDVVIALSYSGRT 60
|
90 100
....*....|....*....|.
gi 1123849898 147 PYVIGAMEYAHRQNAFVAIVS 167
Cdd:cd04795 61 EELLAALEIAKELGIPVIAIT 81
|
|
| SIS_2 |
pfam13580 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
50-167 |
2.71e-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: 40.27 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 50 IAEVVDKVATALQAGGRLIYIGAGTSGrlgiLDASECPPTFGTRPEqVVGII-------AGGHKAILSAVENVEDnKAQG 122
Cdd:pfam13580 21 IEKAADLIAASLANGGKVYAFGTGHSA----APAEELFARAGGLAG-FEPILlpalalhTDASATISTALERDEG-YARQ 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1123849898 123 AMDLQNLNfsHRDVLVGLAASGRTPYVIGAMEYAHRQNAFV-AIVS 167
Cdd:pfam13580 95 ILALYPGR--PGDVLIVISNSGINAVPVEAALEAKERGMKViALTS 138
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
40-183 |
3.27e-04 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 40.61 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 40 AQAITPYLPQIAEVVDKVATALQAGGRLIYIGAGTS------------GRLgildASECPPtfgtrpeqVVGIIAGGHKA 107
Cdd:PRK13937 14 EAFLESLLEAIAKVAEALIEALANGGKILLCGNGGSaadaqhiaaelvGRF----KKERPA--------LPAIALTTDTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 108 ILSAVEN-----------VEDNKAQGamdlqnlnfshrDVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQ 176
Cdd:PRK13937 82 ALTAIGNdygfervfsrqVEALGRPG------------DVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKE 149
|
....*..
gi 1123849898 177 LADVAIT 183
Cdd:PRK13937 150 LCDHLLI 156
|
|
| gmhA |
PRK00414 |
D-sedoheptulose 7-phosphate isomerase; |
135-182 |
6.77e-04 |
|
D-sedoheptulose 7-phosphate isomerase;
Pssm-ID: 179012 [Multi-domain] Cd Length: 192 Bit Score: 40.10 E-value: 6.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1123849898 135 DVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAI 182
Cdd:PRK00414 113 DVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGLADIEI 160
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
135-209 |
1.07e-03 |
|
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: 38.43 E-value: 1.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123849898 135 DVLVGLAASGRTPYVIGAMEYAHRQNAFVAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTrlKAGTAQKLVLNM 209
Cdd:pfam01380 55 DLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAST--KSITAQLAALDA 127
|
|
| COG4821 |
COG4821 |
Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain ... |
48-167 |
1.27e-03 |
|
Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain [General function prediction only];
Pssm-ID: 443849 [Multi-domain] Cd Length: 250 Bit Score: 39.41 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123849898 48 PQIAEVVDKVATALQAGGrLIYI-GAGTSgRLGILDasecppTFGtRPEQVVGIIA---------GGHKAIL--SAVENV 115
Cdd:COG4821 25 EAIEKAADLIADSIAAGG-LVHLfGTGHS-HLLAEE------VFY-RAGGLVGFNPildpslmlhNGAPGVLqsSFLERV 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1123849898 116 EdnkAQGAMDLQNLNFSHRDVLVGLAASGRTPYVIGAMEYAHRQNAFV-AIVS 167
Cdd:COG4821 96 E---GYAEIILENYPIRPGDVLIVISNSGRNAVPIEMALEAKERGLKViAITS 145
|
|
| |
