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Conserved domains on  [gi|501707039|ref|WP_012621875|]
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N-acetylmuramic acid 6-phosphate etherase [Glaesserella parasuis]

Protein Classification

N-acetylmuramic acid 6-phosphate etherase( domain architecture ID 11450007)

N-acetylmuramic acid 6-phosphate etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate, a bacterial cell wall sugar.

PubMed:  24251551

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 7-300 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: 506.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   7 LKTLGQLITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVL 86
Cdd:COG2103    1 MMDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  87 DASECPPTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGA 166
Cdd:COG2103   81 DASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 167 ITVSIASNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAI 246
Cdd:COG2103  161 LTVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501707039 247 RIVMQATECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKISR 300
Cdd:COG2103  241 RIVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRK 294
 
Name Accession Description Interval E-value
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 7-300 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: 506.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   7 LKTLGQLITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVL 86
Cdd:COG2103    1 MMDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  87 DASECPPTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGA 166
Cdd:COG2103   81 DASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 167 ITVSIASNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAI 246
Cdd:COG2103  161 LTVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501707039 247 RIVMQATECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKISR 300
Cdd:COG2103  241 RIVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRK 294
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 10-300 0e+00

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 505.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  10 LGQLITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVLDAS 89
Cdd:PRK05441   3 LENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  90 ECPPTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITV 169
Cdd:PRK05441  83 ECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 170 SIASNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAIRIV 249
Cdd:PRK05441 163 GISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRIV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501707039 250 MQATECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKISR 300
Cdd:PRK05441 243 MEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRK 293
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
 13-298 2.91e-149

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: 420.40  E-value: 2.91e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   13 LITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVLDASECP 92
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   93 PTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIA 172
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  173 SNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAIRIVMQA 252
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 501707039  253 TECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKI 298
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFL 286
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 21-277 1.23e-146

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: 412.30  E-value: 1.23e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  21 NSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVLDASECPPTFGVSPE 100
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 101 MVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMS 180
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 181 QIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAIRIVMQATECSREIA 260
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240

                        250
                 ....*....|....*..
gi 501707039 261 ETTLALAENNAKLAIMM 277
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 137-218 2.66e-10

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: 57.31  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  137 SPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEVLTGSsrMKSGTAQKLVLNMLT 216
Cdd:pfam01380  52 DEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAS--TKSITAQLAALDALA 129


                  ..
gi 501707039  217 TA 218
Cdd:pfam01380 130 VA 131
 
Name Accession Description Interval E-value
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
 7-300 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: 506.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   7 LKTLGQLITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVL 86
Cdd:COG2103    1 MMDLGKLTTEQRNPRSLDLDTLSTLEILRLINEEDAKVAAAVRAALPAIAAAVDAIAEALRAGGRLIYVGAGTSGRLGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  87 DASECPPTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGA 166
Cdd:COG2103   81 DASECPPTFGTPPERVVGLIAGGEEALFRAVEGAEDDEEAGAADLKALGLGPGDVVVGIAASGRTPYVIGALEYARARGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 167 ITVSIASNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAI 246
Cdd:COG2103  161 LTVAIACNPGSPLSAAADIAIELVTGPEVITGSTRLKAGTAQKLVLNMLSTAAMIRLGKVYGNLMVDVRATNAKLRDRAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501707039 247 RIVMQATECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKISR 300
Cdd:COG2103  241 RIVMEATGCDEEEAEEALEAAGGHVKTAILMILTGLDAEEAEALLARAGGFLRK 294
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 10-300 0e+00

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 505.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  10 LGQLITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVLDAS 89
Cdd:PRK05441   3 LENLTTEQRNPASMDLDQLSTLEILRLINEEDKKVALAVEKALPQIAAAVDAAAAALRQGGRLIYIGAGTSGRLGVLDAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  90 ECPPTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITV 169
Cdd:PRK05441  83 ECPPTFGVPPELVVGLIAGGEKALTKAVEGAEDDAELGAADLKAINLTAKDVVVGIAASGRTPYVIGALEYARERGALTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 170 SIASNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAIRIV 249
Cdd:PRK05441 163 GISCNPGSPLSKEADIAIEVVVGPEVLTGSTRMKAGTAQKLVLNMISTGVMIRLGKVYGNLMVDVKATNEKLVDRAVRIV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501707039 250 MQATECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKISR 300
Cdd:PRK05441 243 MEATGVSREEAEAALEAADGSVKLAIVMILTGLDAAEAKALLARHGGFLRK 293
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 12-300 1.84e-167

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 466.48  E-value: 1.84e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  12 QLITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVLDASEC 91
Cdd:PRK12570   1 HLVSEGRNPATMDIDLLSSLDIVTLINQEDKKVPLAVEKVLPQIAQAVDKIVAAFKKGGRLIYMGAGTSGRLGVLDASEC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  92 PPTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSI 171
Cdd:PRK12570  81 PPTFSVSPEMVIGLIAGGPEAMFTAVEGAEDDPELGAQDLKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 172 ASNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAIRIVMQ 251
Cdd:PRK12570 161 SCNPDSPIAKIADIAISPVVGPEVLTGSTRLKSGTAQKMVLNMLSTASMIRLGKSYQNLMVDVKATNEKLVARAVRIVMQ 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 501707039 252 ATECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKISR 300
Cdd:PRK12570 241 ATGCSEDEAKELLKESDNDVKLAILMILTGMDVEQARAALSHADGFLRK 289
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
 13-298 2.91e-149

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: 420.40  E-value: 2.91e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   13 LITEQRNPNSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVLDASECP 92
Cdd:TIGR00274   1 LITEQRNPQSVEIDRQSTLEIVRLINEEDKLVPLAIESVLPDIAAAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   93 PTFGVSPEMVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIA 172
Cdd:TIGR00274  81 PTFGVSPELVKGIIAGGECAILHAVEGAEDSTEAGANDLQNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  173 SNPNSAMSQIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAIRIVMQA 252
Cdd:TIGR00274 161 CNPKSAMSEIADIAIETIVGPEILTGSSRLKAGTAQKMVLNMLSTASMIKLGKVYENLMVDVQASNEKLKARAVRIVMQA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 501707039  253 TECSREIAETTLALAENNAKLAIMMILADLDKDGAEQLLSQQQGKI 298
Cdd:TIGR00274 241 TDCNKELAEQTLLAADQNVKLAIVMILSTLSASEAKVLLDRHGGFL 286
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 21-277 1.23e-146

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: 412.30  E-value: 1.23e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  21 NSMQIDTLSAYEIVQIINNEDKQVPLAIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGRLGVLDASECPPTFGVSPE 100
Cdd:cd05007    1 RSADLDRLSTLEILRLLNEEDKKVAAAVEAALPQIARAVDAAAERLRAGGRLIYVGAGTSGRLGVLDASELPPTFGTPPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 101 MVKGIIAGGERALRHPIEGAEDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMS 180
Cdd:cd05007   81 RVVGLIAGGEPALTRAVEGAEDDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 181 QIADIVIDTVVGAEVLTGSSRMKSGTAQKLVLNMLTTASMILIGKCYQNLMVDVQASNQKLVARAIRIVMQATECSREIA 260
Cdd:cd05007  161 QLADIAIALITGPEVVAGSTRLKAGTAQKLALNMLSTAVMIRLGKVYGNLMVDVRATNEKLRERAIRIVMEATGVSRDEA 240

                        250
                 ....*....|....*..
gi 501707039 261 ETTLALAENNAKLAIMM 277
Cdd:cd05007  241 EAALEQAGGDVKTAILM 257
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 133-216 4.10e-14

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: 67.91  E-value: 4.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 133 AVEF-------SPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEVltGSSRMKSG 205
Cdd:cd05008   34 ASEFryrrpllDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLRAGPEI--SVAATKAF 111

                         90
                 ....*....|.
gi 501707039 206 TAQKLVLNMLT 216
Cdd:cd05008  112 TSQLLALLLLA 122
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 129-218 1.27e-11

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: 61.09  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 129 QDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVgAEVLTGSSRMKSGTAQ 208
Cdd:cd05013   51 QLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSS-EEGDFRSSAFSSRIAQ 129

                         90
                 ....*....|
gi 501707039 209 KLVLNMLTTA 218
Cdd:cd05013  130 LALIDALFLA 139
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 129-218 5.04e-11

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 62.25  E-value: 5.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 129 QDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIdTVVGAEVLTGSSRMKSGTAQ 208
Cdd:COG1737  173 QAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVL-YVPSEEPTLRSSAFSSRVAQ 251

                         90
                 ....*....|
gi 501707039 209 KLVLNMLTTA 218
Cdd:COG1737  252 LALIDALAAA 261
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 137-218 2.66e-10

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: 57.31  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  137 SPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEVLTGSsrMKSGTAQKLVLNMLT 216
Cdd:pfam01380  52 DEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVAS--TKSITAQLAALDALA 129


                  ..
gi 501707039  217 TA 218
Cdd:pfam01380 130 VA 131
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 115-226 2.72e-10

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: 57.17  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 115 HPIEgaednkeAGKQDLQAVefSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAE 194
Cdd:cd05014   33 HPTE-------ALHGDLGMV--TPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEE 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501707039 195 VLTgssrmksgtaqklvLNMLTTAS---MILIGKC 226
Cdd:cd05014  104 ACP--------------LGLAPTTSttaMLALGDA 124
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 42-222 4.46e-10

Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 59.53  E-value: 4.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  42 KQVPLAIEKVLPQIAQAVEKIVEAF--QQGGRLVYIGAGTSGRLGVLDASECpptfgvspEMVKGI----IAGGErALRH 115
Cdd:COG2222    5 AQQPEAWRRALAALAAAIAALLARLraKPPRRVVLVGAGSSDHAAQAAAYLL--------ERLLGIpvaaLAPSE-LVVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 116 PIEGAEDnkeagkqdlqavefspKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEv 195
Cdd:COG2222   76 PAYLKLE----------------GTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPE- 138

                        170       180
                 ....*....|....*....|....*..
gi 501707039 196 ltgssrmKSGTAQKLVLNMLTTASMIL 222
Cdd:COG2222  139 -------KSVAATKSFTTMLLALLALL 158
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 47-187 3.22e-09

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: 55.21  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  47 AIEKVLPQIAQAVEKIVEAFQQGGRLVYIGAGTSGrlgvLDASEcpptfgVSPEMVKGIIaGGERALrhPIEGAEDNKEA 126
Cdd:cd05006   11 LLELLAEAIEQAAQLLAEALLNGGKILICGNGGSA----ADAQH------FAAELVKRFE-KERPGL--PAIALTTDTSI 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501707039 127 gkqdLQAVE--------FS--------PKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVI 187
Cdd:cd05006   78 ----LTAIAndygyeevFSrqvealgqPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEI 150
COG4821 COG4821
Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain ...
 53-189 6.75e-09

Uncharacterized conserved protein, contains SIS (Sugar ISomerase) phosphosugar binding domain [General function prediction only];


Pssm-ID: 443849 [Multi-domain]  Cd Length: 250  Bit Score: 55.59  E-value: 6.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  53 PQIAQAVEKIVEAFQQGGrLVYI-GAGTSgRLGVLDasecppTF-------GVSPEMVKGIiaggerALRHPIEGA---- 120
Cdd:COG4821   25 EAIEKAADLIADSIAAGG-LVHLfGTGHS-HLLAEE------VFyragglvGFNPILDPSL------MLHNGAPGVlqss 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 121 --EDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSA-----------MSQIADIVI 187
Cdd:COG4821   91 flERVEGYAEIILENYPIRPGDVLIVISNSGRNAVPIEMALEAKERGLKVIAITSLEHSKavpsrhssgkrLFELADVVI 170


                 ..
gi 501707039 188 DT 189
Cdd:COG4821  171 DN 172
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 55-173 1.46e-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.


Pssm-ID: 433326 [Multi-domain]  Cd Length: 138  Bit Score: 52.60  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039   55 IAQAVEKIVEAFQQGGRLVYIGAGTSGrlgvLDASECPPTFG----VSPeMVKGIIAGGERALRHPIEGAEDNKEAGKQD 130
Cdd:pfam13580  21 IEKAADLIAASLANGGKVYAFGTGHSA----APAEELFARAGglagFEP-ILLPALALHTDASATISTALERDEGYARQI 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 501707039  131 LQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIAS 173
Cdd:pfam13580  96 LALYPGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 136-187 3.39e-08

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: 52.19  E-value: 3.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501707039 136 FSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVI 187
Cdd:cd05005   73 IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVV 124
PRK02947 PRK02947
sugar isomerase domain-containing protein;
55-189 4.57e-08

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 52.95  E-value: 4.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  55 IAQAVEKIVEAFQQGGRLVYIGAGTSgRLGVLDasecppTFGVspemvkgiiAGGeRALRHPI--------EGA------ 120
Cdd:PRK02947  26 IEKAADLIADSIRNGGLIYVFGTGHS-HILAEE------VFYR---------AGG-LAPVNPIlepslmlhEGAvassyl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 121 EDNKEAGKQDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQ-----------IADIVIDT 189
Cdd:PRK02947  89 ERVEGYAKAILDRYDIRPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVTSLAYSASVAsrhssgkrlaeVADVVLDN 168
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
137-261 1.33e-07

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 52.74  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 137 SPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEVLTGSSrmKSGTAQKLVLNMLT 216
Cdd:PRK00331 335 SPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVAST--KAFTAQLAVLYLLA 412

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501707039 217 TASMILIGKCYQNLMVDVQASNQKLvARAIRIVMQATECSREIAE 261
Cdd:PRK00331 413 LALAKARGTLSAEEEADLVHELREL-PALIEQVLDLKEQIEELAE 456
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 72-172 2.31e-07

SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 47.75  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  72 LVYIGAGTSGRLGVLDASECPPTFGVSpemVKGIIAGGERALRHPIEGAEDnkeagkqdlqavefspkDVLVGIAASGRT 151
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIE---VVALIATELEHASLLSLLRKG-----------------DVVIALSYSGRT 60

                         90       100
                 ....*....|....*....|.
gi 501707039 152 PYVLGALAYAKELGAITVSIA 172
Cdd:cd04795   61 EELLAALEIAKELGIPVIAIT 81
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 47-194 3.06e-07

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: 51.13  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  47 AIEKVLPQI----AQAVEKIVEAfqqGGRLVYIGAGTSGrlgvldasecpptfgvspemvkgIIAG---------GERAL 113
Cdd:COG0794   21 ALAALAERLdesfEKAVELILNC---KGRVVVTGMGKSG-----------------------HIARkiaatlastGTPAF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039 114 -RHPIEgaednkeAGKQDLQAVefSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVG 192
Cdd:COG0794   75 fLHPAE-------ASHGDLGMI--TPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVE 145


                 ..
gi 501707039 193 AE 194
Cdd:COG0794  146 RE 147
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 138-188 4.24e-07

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 49.47  E-value: 4.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501707039 138 PKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVID 188
Cdd:PRK13937 106 PGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLI 156
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
42-185 9.88e-05

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 43.17  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501707039  42 KQVpLAIEKV-LPQIAQ--------AVEKIveaFQQGGRLVYIGAGTSGRLG----VLDASECPPTFGVSPemvkgiiag 108
Cdd:PRK10892  15 KEV-LAIEREgLAELDQyinqdftlACEKM---FWCKGKVVVMGMGKSGHIGrkmaATFASTGTPSFFVHP--------- 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501707039 109 geralrhpiegaednKEAGKQDLQAVefSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADI 185
Cdd:PRK10892  82 ---------------GEAAHGDLGMV--TPQDVVIAISNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADI 141
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 140-218 9.98e-05

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 9.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501707039 140 DVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEVltGSSRMKSGTAQKLVLNMLTTA 218
Cdd:PLN02981 412 DTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEI--GVASTKAYTSQIVAMTMLALA 488
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 140-215 1.24e-04

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 43.33  E-value: 1.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501707039 140 DVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEVltGSSRMKSGTAQKLVLNML 215
Cdd:PTZ00394 403 DVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEV--GVASTKAYTSQVVVLTLV 476
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
137-215 1.63e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 42.44  E-value: 1.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501707039 137 SPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGAEVLTGssrmKSGTAQKLVLNML 215
Cdd:PRK11337 186 QEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLG----ENAAARIAQLNIL 260
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
140-215 2.47e-04

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 41.99  E-value: 2.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501707039 140 DVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDTVVGaEVLTGSSRMKSGTAQKLVLNML 215
Cdd:PRK15482 184 DVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG-ETEWRSSSMSTRTAQNSVTDLL 258
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 136-189 3.66e-04

A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240214 [Multi-domain]  Cd Length: 120  Bit Score: 39.48  E-value: 3.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501707039 136 FSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNPNSAMSQIADIVIDT 189
Cdd:cd05710   45 LTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIVY 98
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
129-189 9.30e-03

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 37.59  E-value: 9.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501707039 129 QDLQAVEFSPKDVLVGIAASGRTPYVLGALAYAKELGAITVSIASNpNSAMSQIADIVIDT 189
Cdd:PRK14101 506 QAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSS-NTPLAKRATVALET 565
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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