NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|522170705|ref|WP_020679329|]
View 

glucose-1-phosphate thymidylyltransferase RfbA [Marinobacterium rhizophilum]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

sugar nucleotidyltransferase such as glucose-1-phosphate thymidylyltransferase, which catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis

CATH:  3.90.550.10
EC:  2.7.7.-
Gene Ontology:  GO:0016779|GO:0046872|GO:0000271
PubMed:  9445404|12691742
SCOP:  4000694

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 574.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  81 PSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 161 PASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTI 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 522170705 241 EARQGLKVACLEEIAYHQGWLSSEHLARQAEALSKTGYGQYLQGLLSQE 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 574.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  81 PSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 161 PASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTI 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 522170705 241 EARQGLKVACLEEIAYHQGWLSSEHLARQAEALSKTGYGQYLQGLLSQE 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-286 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 557.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   82 SPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  162 ASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 522170705  242 ARQGLKVACLEEIAYHQGWLSSEHLARQAEALSKTGYGQYLQGLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 0e+00

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 497.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  81 PSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 161 PASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTI 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-282 6.46e-148

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 416.38  E-value: 6.46e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  82 SPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 162 ASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTIE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 522170705 242 ARQGLKVACLEEIAYHQGWLSSEHLARQAEALSKTGYGQYL 282
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 8.99e-104

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 302.64  E-value: 8.99e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   81 PSPDGLAQAFLIGEDFIGDSNV-CLILGDNIFYGYGFSAMLREAASRES--GATVFGYHVSDPERFGVVEFDASGKAISI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  158 EEKPASPK-SNYAVTGLYFYDNSVVD-IARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASH 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 522170705  236 FV 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 574.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  81 PSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 161 PASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTI 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 522170705 241 EARQGLKVACLEEIAYHQGWLSSEHLARQAEALSKTGYGQYLQGLLSQE 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-286 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 557.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   82 SPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  162 ASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 522170705  242 ARQGLKVACLEEIAYHQGWLSSEHLARQAEALSKTGYGQYLQGLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 0e+00

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 497.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  81 PSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 161 PASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTI 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-282 6.46e-148

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 416.38  E-value: 6.46e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  82 SPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 162 ASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASHFVQTIE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 522170705 242 ARQGLKVACLEEIAYHQGWLSSEHLARQAEALSKTGYGQYL 282
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 8.99e-104

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 302.64  E-value: 8.99e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   81 PSPDGLAQAFLIGEDFIGDSNV-CLILGDNIFYGYGFSAMLREAASRES--GATVFGYHVSDPERFGVVEFDASGKAISI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  158 EEKPASPK-SNYAVTGLYFYDNSVVD-IARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFAWLDTGTHDSLMEASH 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 522170705  236 FV 237
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-237 9.55e-72

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 220.90  E-value: 9.55e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREV-LIISTPQDLpnFEKLLGNGVDFGIELSYAE 79
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIgIVVGPTGEE--IKEALGDGSRFGVRITYIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  80 QPSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGyGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDaSGKAISIEE 159
Cdd:cd04189   79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522170705 160 KPASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFaWLDTGTHDSLMEASHFV 237
Cdd:cd04189  157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 2.39e-64

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 201.27  E-value: 2.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDlPNFEKLLGNGVDFGIELSYAEQPS 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  83 PDGLAQAFLIGEDFIGDSNVCLILGDNIFYGyGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEKPA 162
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522170705 163 SPKSNYAVTGLYFYDNSVVDIARQVKPskRGELEITDVNNAYLQRGDLHVsmFGRGFAWLDTG 225
Cdd:cd04181  159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG--YPVDGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-233 1.51e-58

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 190.69  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   82 SPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGyGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522170705  162 ASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGFaWLDTGTHDSLMEA 233
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 3.03e-46

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 155.31  E-value: 3.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVlIISTpQDLPN-FEKLLGNGVDFGIELSYAEQ 80
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINV-GYLAEqIEEYFGDGSRFGVRITYVDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  81 PSPDGLAQAFLIGEDFIGDSNVCLILGDnIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEEK 160
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522170705 161 PASPKSNYAVTGLYFYDNSVVDIARqvkpsKRGELEITDVNNAYLQRGDLHVSMFgRGFaWLDTGTHDSLMEA 233
Cdd:COG1208  158 PEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-225 2.56e-45

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 157.37  E-value: 2.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705    1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDlPNFEKLLGNGVDFGIELSYAEQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   81 PSPDGLAQAFLIGEDFIgDSNVCLILGDNIFygygfSAMLREAASRESGATVFGYHVSDPERFGVVEFDAsGKAISIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522170705  161 PASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRGDLHVSMFGRGfaWLDTG 225
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-234 1.82e-35

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 128.42  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQ--------DlPNFE---KLLGNG- 68
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfD-RSYEleeTLEKKGk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  69 ---------VDFGIELSYAEQPSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGY--GFSAMLReaASRESGATVFGYHV 137
Cdd:cd02541   80 tdlleevriISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepCLKQLIE--AYEKTGASVIAVEE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 138 SDPE---RFGVVEFDASGKAI----SIEEKPA--SPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQRG 208
Cdd:cd02541  158 VPPEdvsKYGIVKGEKIDGDVfkvkGLVEKPKpeEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEE 237

                        250       260
                 ....*....|....*....|....*..
gi 522170705 209 DLHVSMF-GRgfaWLDTGTHDSLMEAS 234
Cdd:cd02541  238 PVYAYVFeGK---RYDCGNKLGYLKAT 261
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-226 6.18e-23

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 94.20  E-value: 6.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREV-LIIS-TPQDLPNFEKLLGNgvDFGIELSYA 78
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIiLAVNyRPEDMVPFLKEYEK--KLGIKITFS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  79 EQPSPDGLAQAFLIGEDFIGDSNVC-LILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFD-ASGKAIS 156
Cdd:cd06425   79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDeNTGRIER 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522170705 157 IEEKPASPKSNYAVTGLYFYDNSVVD-IarqvkPSKRGELEiTDVNNAYLQRGDLHVsMFGRGFaWLDTGT 226
Cdd:cd06425  159 FVEKPKVFVGNKINAGIYILNPSVLDrI-----PLRPTSIE-KEIFPKMASEGQLYA-YELPGF-WMDIGQ 221
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-233 6.37e-23

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 93.73  E-value: 6.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVlIISTpqdlpNF-----EKLLGNGVDFGIELSYA 78
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISV-----NYlaemiEDYFGDGSKFGVNISYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  79 EQPSPDGLAQAF-LIGEDFigDSNVCLILGDnIFYGYGFSAMLREAASRESGATVFG--YHVSDPerFGVVEFDAsGKAI 155
Cdd:cd06426   76 REDKPLGTAGALsLLPEKP--TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETEG-GRIT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 156 SIEEKpasPKSNYAV-TGLYFYDNSVVDiarQVKPSKRgeLEITDVNNAYLQRGDlHVSMFG-RGFaWLDTGTHDSLMEA 233
Cdd:cd06426  150 SIEEK---PTHSFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGK-KVGVFPiHEY-WLDIGRPEDYEKA 219
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 1.02e-21

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 92.02  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYplSV--LMLAGIREVLIISTPQ--------DlPNFE--------- 62
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRGkraiedhfD-RSYEleatleakg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  63 --KLLG--NGVDFGIELSYAEQPSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGY--GFSAMLreAASRESGATVFG-Y 135
Cdd:COG1210   82 keELLEevRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkpCLKQMI--EVYEETGGSVIAvQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 136 HVSDPE--RFGVVEF-DASGKAISIE---EKPASPK--SNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNNAYLQR 207
Cdd:COG1210  160 EVPPEEvsKYGIVDGeEIEGGVYRVTglvEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                        250       260
                 ....*....|....*....|....*..
gi 522170705 208 GDLHVSMF-GRgfaWLDTGTHDSLMEA 233
Cdd:COG1210  240 EPVYAYEFeGK---RYDCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 1.63e-21

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 90.30  E-value: 1.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLI--------IstpqdlpnfEKLLGNGVDFGIEL 75
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLsvgylaeqI---------EEYFGDGYRGGIRI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  76 SYAEQPSPDGLAQAFLIGEDFIGDSNVCLILGDNiFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAI 155
Cdd:cd06915   73 YYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 156 SIEEKPASPKSNYAVTGLYFYDNSVVDIARQVKPSkrgeLEiTDVNNAYLQRGDLhvsmfgRGFA----WLDTGTHDSLM 231
Cdd:cd06915  152 AFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYA 220


                 ..
gi 522170705 232 EA 233
Cdd:cd06915  221 RA 222
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-177 5.34e-17

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 80.12  E-value: 5.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLHPITRGVSKqllpiydkPMIYY---------PLSVLMLAGIREVLIIsTPQdlpNFEKL---LGNGV- 69
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVL-TQY---KSHSLndhIGSGKp 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  70 -DFGIELSY-----AEQPSPD-----GLAQAFLIGEDFIGDSNV--CLIL-GDNIfYGYGFSAMLREAasRESGA--TVF 133
Cdd:COG0448   72 wDLDRKRGGvfilpPYQQREGedwyqGTADAVYQNLDFIERSDPdyVLILsGDHI-YKMDYRQMLDFH--IESGAdiTVA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 522170705 134 GYHVSDPE--RFGVVEFDASGKAISIEEKPASPKSNYAVTGLYFYD 177
Cdd:COG0448  149 CIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-57 5.55e-15

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 72.31  E-value: 5.55e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQD 57
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-233 2.88e-14

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 70.29  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIistpqdlpN-------FEKLLGN-GVDFGI 73
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV--------NthhladqIEAHLGDsRFGLRI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  74 ELSYaEQPSP----DGLAQAfligEDFIGDSNVCLILGDnIFYGYGFSAMLREAASRESG--ATVFGYHVSDPERFGVVE 147
Cdd:cd06422   73 TISD-EPDELletgGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDAllLLLPLVRNPGHNGVGDFS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 148 FDASGKAISIEEKPASPksnYAVTGLYFYDNSVVDIArqvkpsKRGELEITDVNNAYLQRGDLHVSMFgRGFaWLDTGTH 227
Cdd:cd06422  147 LDADGRLRRGGGGAVAP---FTFTGIQILSPELFAGI------PPGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTP 215


                 ....*.
gi 522170705 228 DSLMEA 233
Cdd:cd06422  216 ERLLAA 221
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-199 4.36e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 67.99  E-value: 4.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLII--STPQDLPN-------FEKLLGNGVDF 71
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthASKNAVENhfdtsyeLESLLEQRVKR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  72 ------------GIELSYAEQPSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYG-------YGFSAMLreAASRESG-AT 131
Cdd:PRK10122  84 qllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplrYNLAAMI--ARFNETGrSQ 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522170705 132 VFGYHVS-DPERFGVVE----FDASGKAISIE---EKPASPK---SNYAVTGLYFYDNSVVDIARQVKPSKRGELEITD 199
Cdd:PRK10122 162 VLAKRMPgDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-199 8.92e-13

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 67.24  E-value: 8.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLII--STPQDLPN-------FEKLLGNGVDF- 71
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthSSKNSIENhfdtsfeLEAMLEKRVKRq 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  72 -----------GIELSYAEQPSPDGLAQAFLIGEDFIGDSNVCLILGDNIFYGY-------GFSAMLREAAsrESGAT-V 132
Cdd:PRK13389  90 lldevqsicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYesdlsqdNLAEMIRRFD--ETGHSqI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522170705 133 FGYHVSDPERFGVVEFDA-------SGKAISIEEKPASPK--SNYAVTGLYFYDNSVVDIARQVKPSKRGELEITD 199
Cdd:PRK13389 168 MVEPVADVTAYGVVDCKGvelapgeSVPMVGVVEKPKADVapSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-52 2.34e-12

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 64.97  E-value: 2.34e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLII 52
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-212 3.39e-12

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 64.56  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDlPNFEKLLGNGVDfgIELSYAEQPSP 83
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKKYPN--IKFVYNPDYAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  84 DGLAQAFLIGEDFIGDsNVCLILGDNIFYgygfSAMLRE--AASRESGATVFGYHVSDPERFGVVEFDASGKAISIeEKP 161
Cdd:cd02523   79 TNNIYSLYLARDFLDE-DFLLLEGDVVFD----PSILERllSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGII-SKA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 522170705 162 ASPKSNYAVT-GLYFYDNS----VVDIARQVKPSKRGELEITDVNNAYLQRGDLHV 212
Cdd:cd02523  153 KNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKV 208
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-208 5.62e-12

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 65.77  E-value: 5.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIIsTPQDLPNFEKLL-GNGVDFgielsyAEQPS 82
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVV-TGHGAEQVEAALqGSGVAF------ARQEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  83 PDGLAQAFLIGEDFI--GDSNVCLILGDN-IFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISIEE 159
Cdd:PRK14358  81 QLGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 522170705 160 KPASPKSNYAV----TGLYFYDNSVVDIARQV-KPSKRGELEITDVNNAYLQRG 208
Cdd:PRK14358 161 QKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-234 6.55e-12

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 65.27  E-value: 6.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREVLIISTPQDLpNFEKLLGNGVDFGIE----- 74
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPL-ELNNHIGIGSPWDLDringg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  75 ---LS-YAEQPSPD---GLAQAFLIGEDFIGDSN--VCLIL-GDNIfYGYGFSAMLREAASRESGATVFGYHVSDPE--R 142
Cdd:PRK05293  83 vtiLPpYSESEGGKwykGTAHAIYQNIDYIDQYDpeYVLILsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEVPWEEasR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705 143 FGVVEFDASGKAISIEEKPASPKSNYAVTGLYFY---------------DNSVVDIARQVKPSkrgeleitdvnnaYLQR 207
Cdd:PRK05293 162 FGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL-------------YLEE 228

                        250       260
                 ....*....|....*....|....*....
gi 522170705 208 GDlhvSMFGRGFA--WLDTGTHDSLMEAS 234
Cdd:PRK05293 229 GE---KLYAYPFKgyWKDVGTIESLWEAN 254
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-200 1.30e-10

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 60.22  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLH---PitrgvsKQLLPIYDKPMIYYPL-SVLMLAGIREVLIISTPQDLpnFEKLLGNgvdfgIELSYAE 79
Cdd:cd02540    2 VILAAGKGTRMKsdlP------KVLHPLAGKPMLEHVLdAARALGPDRIVVVVGHGAEQ--VKKALAN-----PNVEFVL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  80 QPSPDGLAQAFLIGEDFIGDSN-VCLILgdnifygYG---------FSAMLREAASRESGATVFGYHVSDPERFGVVEFD 149
Cdd:cd02540   69 QEEQLGTGHAVKQALPALKDFEgDVLVL-------YGdvplitpetLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRD 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 522170705 150 ASGKAISI-EEKPASP--KSNYAV-TGLYFYDNSVVDIA-RQVKPS-KRGELEITDV 200
Cdd:cd02540  142 GNGKVLRIvEEKDATEeeKAIREVnAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI 198
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-202 1.39e-10

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 60.35  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGG--SGTRLHPITRGVSKQLLPIYDKPMIYYPLSVL-MLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAE 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  80 QPSPDGLAQAFLIGEDFI--GDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPE--RFG-VVEFDASGKA 154
Cdd:cd06428   81 EYKPLGTAGGLYHFRDQIlaGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQasNYGcIVEDPSTGEV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 522170705 155 ISIEEKPASPKSNYAVTGLYFYDNSVVDIARQVKPSKRGELEITDVNN 202
Cdd:cd06428  161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNN 208
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-166 1.44e-10

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 61.38  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLHPITRGVSKQLLP---IYDkpMIYYPLSVLMLAGIRE--VLIISTPQDLP-------NFEKLLGNGVD 70
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRiyVLTQYKSHSLDrhisqtwRLSGLLGNYIT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  71 fgielsyaeqPSP----------DGLAQAFLIGEDFIGDSN---VCLILGDNIfYGYGFSAMLREAASRESGATVFGYHV 137
Cdd:PRK00844  86 ----------PVPaqqrlgkrwyLGSADAIYQSLNLIEDEDpdyVVVFGADHV-YRMDPRQMVDFHIESGAGVTVAAIRV 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 522170705 138 --SDPERFGVVEFDASGKAISIEEKPASPKS 166
Cdd:PRK00844 155 prEEASAFGVIEVDPDGRIRGFLEKPADPPG 185
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-52 4.74e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.33  E-value: 4.74e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 522170705   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLII 52
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-65 4.15e-09

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 55.52  E-value: 4.15e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522170705   4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLMLAG-IREVLIISTPQDLPNFEKLL 65
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELL 60
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-166 4.39e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 56.77  E-value: 4.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREVLII------STPQDLPN----FEKLLGngvDFg 72
Cdd:PRK00725  19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLtqykahSLIRHIQRgwsfFREELG---EF- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  73 IELSYAEQPSPD-----GLAQAFLIGEDFIGDSNV--CLIL-GDNIfYGYGFSAMLREaaSRESGA--TVFGYHVSDPE- 141
Cdd:PRK00725  95 VDLLPAQQRVDEenwyrGTADAVYQNLDIIRRYDPkyVVILaGDHI-YKMDYSRMLAD--HVESGAdcTVACLEVPREEa 171

                        170       180
                 ....*....|....*....|....*.
gi 522170705 142 -RFGVVEFDASGKAISIEEKPASPKS 166
Cdd:PRK00725 172 sAFGVMAVDENDRITAFVEKPANPPA 197
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-200 7.41e-09

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 56.31  E-value: 7.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   1 MKGIILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLpnFEKLLGNGVDFgielsyAEQ 80
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPEWVKI------FLQ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  81 PSPDGLAQAFLIGEDFIGDSNVCLIL-GDNIFYGYG-FSAMLREAASRESGATVFGYHVSDPERFGVVEFDaSGKAISIE 158
Cdd:PRK14357  70 EEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENtLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRD-GGKYRIVE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 522170705 159 EKPASPKSNYAV---TGLYFYD-NSVVDIARQVKP-SKRGELEITDV 200
Cdd:PRK14357 149 DKDAPEEEKKIKeinTGIYVFSgDFLLEVLPKIKNeNAKGEYYLTDA 195
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-138 1.65e-08

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 53.70  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLHPITRGVSKQLLPI---YDkpMIYYPLSVLMLAGIREVLIIsTPQdlpNFEKL---LGNGVDF----- 71
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVL-TQY---KSRSLndhLGSGKEWdldrk 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522170705  72 --GIELSYAEQ-PSPD---GLAQAFLIGEDFIGDSNV--CLILGDNIFYGYGFSAMLREAasRESGATV-FGYHVS 138
Cdd:cd02508   75 ngGLFILPPQQrKGGDwyrGTADAIYQNLDYIERSDPeyVLILSGDHIYNMDYREMLDFH--IESGADItVVYKAS 148
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 2.95e-08

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 53.21  E-value: 2.95e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522170705   4 IILAGGSGTRLHPitrGVSKQLLPIYDKPMIYYPLSVLMLAG-IREVLIISTPQDLPNFEKLL 65
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-68 3.25e-08

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 52.91  E-value: 3.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522170705   4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLM-LAGIREVLIISTPQDLPNFEKLLGNG 68
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-208 4.81e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 53.59  E-value: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLhpiTRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGvdfgiELSYAEQPSP 83
Cdd:PRK14355   7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG-----DVSFALQEEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  84 DGLAQAFLIG-EDFIGDSNVCLIL-GDN-IFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAISI-EE 159
Cdd:PRK14355  79 LGTGHAVACAaPALDGFSGTVLILcGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 522170705 160 KPASPKS---NYAVTGLYFYDNSVV--DIARQVKPSKRGELEITDVNNAYLQRG 208
Cdd:PRK14355 159 KDATPEErsiREVNSGIYCVEAAFLfdAIGRLGNDNAQGEYYLTDIVAMAAAEG 212
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-200 3.58e-07

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 50.80  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLH---PitrgvsKQLLPIYDKPMIYYPLSVLMLAGIREVLIIstpqdlpnfeklLGNGVD------FGIE 74
Cdd:COG1207    6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEqvraalADLD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  75 LSYAEQPSPDGLAQAFLIGEDFI-GDSNVCLILgdnifygYG---------FSAMLREAASRESGATVFGYHVSDPERFG 144
Cdd:COG1207   68 VEFVLQEEQLGTGHAVQQALPALpGDDGTVLVL-------YGdvpliraetLKALLAAHRAAGAAATVLTAELDDPTGYG 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522170705 145 VVEFDASGKAISI-EEKPASP--KSNYAV-TGLYFYDNSVVDIA-RQVKPS-KRGELEITDV 200
Cdd:COG1207  141 RIVRDEDGRVLRIvEEKDATEeqRAIREInTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-104 2.81e-06

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 46.81  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   6 LAGGSGTRLhpitRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPqDLPNFEKLL-GNGVDFgIELSyaeqpspd 84
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREYLkERGVEV-IETP-------- 66

                         90       100
                 ....*....|....*....|
gi 522170705  85 glaqafliGEDFIGDSNVCL 104
Cdd:COG2266   67 --------GEGYVEDLNEAL 78
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-208 2.85e-06

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 47.25  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYplSVLMLAGIRE---VLIIS----TPQDLPNFEKLLGNGVDFgIELs 76
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFICRdehnTKFHLDESLKLLAPNATV-VEL- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  77 yaeQPSPDGLAQAFLIGEDFIgDSNVCLILGD-NIFYGYGFSAMLREAASRESGATVFGYHVSDPeRFGVVEFDASGKAI 155
Cdd:cd04183   78 ---DGETLGAACTVLLAADLI-DNDDPLLIFNcDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVI 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 522170705 156 SIEEKpaSPKSNYAVTGLYFYDNS--VVDIARQV-KPSKR--GELEITDVNNAYLQRG 208
Cdd:cd04183  153 ETAEK--EPISDLATAGLYYFKSGslFVEAAKKMiRKDDSvnGEFYISPLYNELILDG 208
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-57 2.19e-05

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 44.03  E-value: 2.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 522170705   1 MKGIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVlmLAGIREVLIISTPQD 57
Cdd:COG0746    5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP 54
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-161 2.50e-05

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 45.23  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLHPITRGVSKQLLPI---YDkpMIYYPLSVLMLAGIREVLII------STPQDLP---NFekllGNGVD 70
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLtqfnsaSLNRHLSrayNF----GNGGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  71 FG---IELSYAEQpSPD------GLAQA---FL-IGEDF--IGDSNVcLIL-GDNIfYGYGFSAMLReaASRESGA--TV 132
Cdd:PLN02241  80 FGdgfVEVLAATQ-TPGekgwfqGTADAvrqFLwLFEDAknKNVEEV-LILsGDHL-YRMDYMDFVQ--KHRESGAdiTI 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 522170705 133 fGYHVSDPER---FGVVEFDASGKAISIEEKP 161
Cdd:PLN02241 155 -ACLPVDESRasdFGLMKIDDTGRIIEFSEKP 185
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-164 3.12e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.85  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPqDLPNFEKLLGngvDFGIELSYAEQPSP 83
Cdd:PRK14353   9 IILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAAA---KIAPDAEIFVQKER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  84 DGLAQAFLIGEDFI--GDSNVCLILGDNIFYGYGFSAMLREAASRESGATVFGYHVSDPERFG-VVEFDASGKAIsIEEK 160
Cdd:PRK14353  82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrLIVKGGRLVAI-VEEK 160


                 ....
gi 522170705 161 PASP 164
Cdd:PRK14353 161 DASD 164
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-52 3.47e-05

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 43.61  E-value: 3.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLII 52
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV 50
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-34 4.14e-05

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 44.10  E-value: 4.14e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 522170705   1 MKGIILAGGSGTRLHPITR-GVSKQLLPIY-DKPMI 34
Cdd:cd02509    1 IYPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLL 36
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-66 4.52e-05

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 42.95  E-value: 4.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522170705    3 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAGiREVLIISTPQDLPNFEKLLG 66
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG 58
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-161 5.38e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 44.11  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREVLI------------ISTPQDLPNFekllGNGv 69
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVltqfnsaslnrhISQTYNFDGF----SGG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  70 dFgIELSYAEQP--SPD---GLAQA-----FLIGEDfigDSNVCLIL-GDNIfYGYGFSAMLreAASRESGA--TVFGYH 136
Cdd:PRK02862  81 -F-VEVLAAQQTpeNPSwfqGTADAvrkylWHFQEW---DVDEYLILsGDQL-YRMDYRLFV--QHHRETGAdiTLAVLP 152

                        170       180
                 ....*....|....*....|....*..
gi 522170705 137 VS--DPERFGVVEFDASGKAISIEEKP 161
Cdd:PRK02862 153 VDekDASGFGLMKTDDDGRITEFSEKP 179
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-136 5.43e-05

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 42.93  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTPQDLPNFEKLLGNGVDFGIELSYAEqps 82
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE--- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 522170705  83 pdGLAQAFLIG-EDFIGDSNVCLI-LGDNIFYGYGFSAMLREAASRESGATVFGYH 136
Cdd:cd04182   75 --GMSSSLAAGlEALPADADAVLIlLADQPLVTAETLRALIDAFREDGAGIVAPVY 128
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-200 9.17e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 43.67  E-value: 9.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705   4 IILAGGSGTRL---HPitrgvsKQLLPIYDKPMIYYPLSVLMLAGIRE-VLIISTPQDLpnFEKLLGNGVDFGIElsyAE 79
Cdd:PRK14354   6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKiVTVVGHGAEE--VKEVLGDRSEFALQ---EE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705  80 QPspdGLAQAFLIGEDFIGDS--NVCLILGDN-IFYGYGFSAMLREAASRESGATVFGYHVSDPERFGVVEFDASGKAIS 156
Cdd:PRK14354  75 QL---GTGHAVMQAEEFLADKegTTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEK 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 522170705 157 I-EEKPASPKS------NyavTGLYFYDN-SVVDIARQVKPSK-RGELEITDV 200
Cdd:PRK14354 152 IvEQKDATEEEkqikeiN---TGTYCFDNkALFEALKKISNDNaQGEYYLTDV 201
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-34 3.77e-04

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 41.59  E-value: 3.77e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 522170705   1 MKGIILAGGSGTRLHPITRGVS-KQLLPIY-DKPMI 34
Cdd:COG0836    3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLL 38
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-52 8.35e-04

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 39.90  E-value: 8.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 522170705   3 GIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREVLII 52
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-64 2.25e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 38.24  E-value: 2.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522170705   1 MKGIILAGGSGTRLHpitrGVSKQLLPIYDKPMIYYPLSVL--MLAGIrevlIISTPQDLPNFEKL 64
Cdd:PRK00317   4 ITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERLapQVDEI----VINANRNLARYAAF 61
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 4-66 2.69e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 38.20  E-value: 2.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522170705    4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLMLAG-IREVLIISTPQDLPNFEKLLG 66
Cdd:pfam01128   2 VIPAAGSGKRMG---AGVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAVSPDDTPEFRQLLG 62
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 3-111 3.21e-03

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 38.09  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522170705    3 GIILAGGSGTRLhpitrgVSKQLLPIYDKPMIYYPLSVLMLAGIREVLIISTpqDLPNFEKLLgngVDFGIELSYAEQPS 82
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT--DSEEIADVA---KEFGAGVVMTSGSL 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 522170705   83 PDGLAQAFLIGEDFIGDSN--VCLILGDNIF 111
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNDHDdiIVNIQGDNPL 101
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-67 6.10e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 37.90  E-value: 6.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522170705   4 IILAGGSGTRLhpiTRGVSKQLLPIYDKPMIYYPLSVLMLAG-IREVLIISTPQDLPNFEKLLGN 67
Cdd:PRK09382   9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-64 9.94e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 36.40  E-value: 9.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522170705   1 MKGIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSvlMLAGIREVLIISTPQDLPNFEKL 64
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH