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Conserved domains on  [gi|1768862262|ref|WP_152249422|]
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glucose-1-phosphate thymidylyltransferase RfbA [Xanthomonas maliensis]

Protein Classification

glucose-1-phosphate thymidylyltransferase( domain architecture ID 11492097)

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

EC:  2.7.7.24
Gene Ontology:  GO:0008879|GO:0046872|GO:0000271
PubMed:  9445404|12691742
SCOP:  4000694

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
5-290 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: 562.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQP 84
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEKP 164
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 165 LRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFIETIQ 244
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1768862262 245 MRQGLQVCCPEEIAFAQGWIDASQLERLAAPLSKNAYGQYLHSLAQ 290
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
 
Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
5-290 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: 562.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQP 84
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEKP 164
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 165 LRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFIETIQ 244
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1768862262 245 MRQGLQVCCPEEIAFAQGWIDASQLERLAAPLSKNAYGQYLHSLAQ 290
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
4-294 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 542.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   4 RKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQ 83
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEK 163
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 164 PLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFIETI 243
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1768862262 244 QMRQGLQVCCPEEIAFAQGWIDASQLERLAAPLSKNAYGQYLHSLAQRGVV 294
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRA 291
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
4-243 5.14e-163

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: 452.41  E-value: 5.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   4 RKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQ 83
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEK 163
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 164 PLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFIETI 243
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
1-285 4.26e-149

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 419.46  E-value: 4.26e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   1 MTQRKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRY 80
Cdd:PRK15480    1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  81 AVQPSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINI 160
Cdd:PRK15480   81 KVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 161 EEKPLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFI 240
Cdd:PRK15480  161 EEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1768862262 241 ETIQMRQGLQVCCPEEIAFAQGWIDASQLERLAAPLSKNAYGQYL 285
Cdd:PRK15480  241 ATIEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
5-241 5.30e-101

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: 295.70  E-value: 5.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDK-PMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQ 83
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGD-KPSCLVLGDNIFHGHGLTDVLRRASARE--HGATVFGYWVNDPERYGVAEFNSQGKVINI 160
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDeKSDVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 161 EEKPLRPR-SNYAVTGLYFYDGRACDYAAE-LMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASN 238
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLAKyLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 1768862262 239 FIE 241
Cdd:pfam00483 241 FLL 243
 
Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
5-290 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: 562.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQP 84
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEKP 164
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 165 LRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFIETIQ 244
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1768862262 245 MRQGLQVCCPEEIAFAQGWIDASQLERLAAPLSKNAYGQYLHSLAQ 290
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
4-294 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 542.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   4 RKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQ 83
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEK 163
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 164 PLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFIETI 243
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1768862262 244 QMRQGLQVCCPEEIAFAQGWIDASQLERLAAPLSKNAYGQYLHSLAQRGVV 294
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRA 291
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
4-243 5.14e-163

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: 452.41  E-value: 5.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   4 RKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQ 83
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEK 163
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 164 PLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFIETI 243
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
1-285 4.26e-149

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 419.46  E-value: 4.26e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   1 MTQRKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRY 80
Cdd:PRK15480    1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  81 AVQPSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINI 160
Cdd:PRK15480   81 KVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 161 EEKPLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASNFI 240
Cdd:PRK15480  161 EEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1768862262 241 ETIQMRQGLQVCCPEEIAFAQGWIDASQLERLAAPLSKNAYGQYL 285
Cdd:PRK15480  241 ATIEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
5-241 5.30e-101

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: 295.70  E-value: 5.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDK-PMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQ 83
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGD-KPSCLVLGDNIFHGHGLTDVLRRASARE--HGATVFGYWVNDPERYGVAEFNSQGKVINI 160
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDeKSDVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 161 EEKPLRPR-SNYAVTGLYFYDGRACDYAAE-LMPSSRGELEITDLNRRYLETGDLHLESLGRGYAWLDTGTHQSLHEASN 238
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLAKyLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 1768862262 239 FIE 241
Cdd:pfam00483 241 FLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
5-240 7.71e-70

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: 215.90  E-value: 7.71e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHeQPLFQALLGDGAQWGIDVRYAVQP 84
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGhGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFnSQGKVINIEEKP 164
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVV-DDGRIVRLVEKP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1768862262 165 LRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYaWLDTGTHQSLHEASNFI 240
Cdd:cd04189   159 KEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
6-228 1.41e-62

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: 197.03  E-value: 1.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   6 GIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVlIINTPHEQPLFQALLGDGAQWGIDVRYAVQPS 85
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEI-ILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  86 PDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGhGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEKPL 165
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1768862262 166 RPRSNYAVTGLYFYDGRACDYAAELMPssRGELEITDLNRRYLETGDLhleslgRGY----AWLDTG 228
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKV------YGYpvdgYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
5-240 3.53e-57

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: 187.61  E-value: 3.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAVQP 84
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGhGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEKP 164
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1768862262 165 LRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGYaWLDTGTHQSLHEASNFI 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
5-236 1.87e-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: 156.08  E-value: 1.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVlIINTPHEQPLFQALLGDGAQWGIDVRYAVQP 84
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SP----DGLAQAyligRDFVGDKPSCLVLGDNIFhGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINI 160
Cdd:COG1208    80 EPlgtgGALKRA----LPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRF 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1768862262 161 EEKPLRPRSNYAVTGLYFYDGRACDYAAElmpssRGELEITDLNRRYLETGDLHLESLgRGYaWLDTGTHQSLHEA 236
Cdd:COG1208   155 VEKPEEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
5-228 5.02e-44

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: 154.29  E-value: 5.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQaLLGDGAQWGIDVRYAVQP 84
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVRE-YFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAYLIGRDFVGDKpsCLVL-GDNIFHGHGLTDVLRrasarEHGATVFGYWVNDPERYGVAEFNSqGKVINIEEK 163
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDDE--FLVLnGDVLLDSDLLERLIR-----AEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1768862262 164 PLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGRGyaWLDTG 228
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
4-229 8.18e-30

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: 113.40  E-value: 8.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   4 RKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQP----------LFQALLGDG-- 71
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAiedhfdrsyeLEETLEKKGkt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  72 --------AQWGIDVRYAVQPSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHglTDVLRR--ASAREHGATVFGYWVN 141
Cdd:cd02541    81 dlleevriISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSK--EPCLKQliEAYEKTGASVIAVEEV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 142 DPE---RYGVAEFNSQG----KVINIEEKPlRPR---SNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETG 211
Cdd:cd02541   159 PPEdvsKYGIVKGEKIDgdvfKVKGLVEKP-KPEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEE 237
                         250       260
                  ....*....|....*....|.
gi 1768862262 212 DLH---LEslGRGYawlDTGT 229
Cdd:cd02541   238 PVYayvFE--GKRY---DCGN 253
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
1-229 3.44e-23

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 96.25  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   1 MTQRKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYplSV--LMLTGIREVLIINTPHEQP----------LFQALL 68
Cdd:COG1210     1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRGKRAiedhfdrsyeLEATLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  69 GDGAQ----------WGIDVRYAVQPSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGHglTDVLRR--ASAREHGATVF 136
Cdd:COG1210    79 AKGKEelleevrsisPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQmiEVYEETGGSVI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 137 GywVN--DPE---RYGVAEFNSQG----KVINIEEKPLR---PrSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLN 204
Cdd:COG1210   157 A--VQevPPEevsKYGIVDGEEIEggvyRVTGLVEKPAPeeaP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAI 233
                         250       260
                  ....*....|....*....|....*.
gi 1768862262 205 RRYLETGDLH-LESLGRGYawlDTGT 229
Cdd:COG1210   234 AALAKEEPVYaYEFEGKRY---DCGD 256
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
7-236 2.36e-22

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: 92.62  E-value: 2.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   7 IILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVlIINTPHEQPLFQALLGDGAQWGIDVRYAVQPSP 86
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  87 DGLAQAYLIGRDFVGDkPSCLVL-GDNIFHGhGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINIEEKPL 165
Cdd:cd06915    81 LGTGGAIKNALPKLPE-DQFLVLnGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1768862262 166 RPRSNYAVTGLYFYDGRACDYAAELMPSsrgeLEiTDLNRRYLETGDLhleslgRGYA----WLDTGTHQSLHEA 236
Cdd:cd06915   159 GAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
7-236 4.56e-17

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: 77.94  E-value: 4.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   7 IILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLI-INTPHEQplFQALLGDGAQWGIDVRYAVQPS 85
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYIsVNYLAEM--IEDYFGDGSKFGVNISYVREDK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  86 PDGLAQAylIGrdFVGDKPSCLVL---GDnIFHGHGLTDVLRRasAREHGA--TVFG--YWVNDPerYGVAEFNsQGKVI 158
Cdd:cd06426    80 PLGTAGA--LS--LLPEKPTDPFLvmnGD-ILTNLNYEHLLDF--HKENNAdaTVCVreYEVQVP--YGVVETE-GGRIT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 159 NIEEKplrPRSNYAV-TGLYFYDGRACDYAAElmpssrGE-LEITDLNRRYLETGdlhlESLG----RGYaWLDTGTHQS 232
Cdd:cd06426   150 SIEEK---PTHSFLVnAGIYVLEPEVLDLIPK------NEfFDMPDLIEKLIKEG----KKVGvfpiHEY-WLDIGRPED 215

                  ....
gi 1768862262 233 LHEA 236
Cdd:cd06426   216 YEKA 219
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
5-68 1.78e-16

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: 76.16  E-value: 1.78e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALL 68
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
5-236 2.10e-16

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: 76.46  E-value: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVlIINTPH--EQplFQALLGDgAQWGIDVRYav 82
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTHHlaDQ--IEAHLGD-SRFGLRITI-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  83 QPSPD-------GLAQAyligRDFVGDKPSCLVLGDNIFHGhGLTDVLRRASAREHGATVFGYWVNDPERYGVAEF--NS 153
Cdd:cd06422    75 SDEPDelletggGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 154 QGKVINIEEKPLRPrsnYAVTGLYFYDGRACDYAAElmpssrGELEITDLNRRYLETGDLHLeSLGRGYaWLDTGTHQSL 233
Cdd:cd06422   150 DGRLRRGGGGAVAP---FTFTGIQILSPELFAGIPP------GKFSLNPLWDRAIAAGRLFG-LVYDGL-WFDVGTPERL 218

                  ...
gi 1768862262 234 HEA 236
Cdd:cd06422   219 LAA 221
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
5-68 4.11e-15

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: 72.67  E-value: 4.11e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALL 68
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLL 65
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
5-194 7.95e-15

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: 72.24  E-value: 7.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREV-LIINTPHEQpLFQALLGDGAQWGIDVRYAVQ 83
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIiLAVNYRPED-MVPFLKEYEKKLGIKITFSIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGDKPSC-LVLGDNIFHGHGLTDVLrrASAREHG--ATVFGYWVNDPERYGVAEFNSQ-GKVIN 159
Cdd:cd06425    81 TEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELL--DFHKKHGaeGTILVTKVEDPSKYGVVVHDENtGRIER 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1768862262 160 IEEKPLRPRSNYAVTGLYFYDGRACDYaAELMPSS 194
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVLDR-IPLRPTS 192
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-202 4.40e-14

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 71.07  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   1 MTQRKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLII------------NTPHE-QPLFQA- 66
Cdd:PRK10122    1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthasknavenhfDTSYElESLLEQr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  67 ----LLGDGAQW---GIDVRYAVQPSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHG-------HGLTDVLRRASAREHG 132
Cdd:PRK10122   81 vkrqLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplrYNLAAMIARFNETGRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 133 ATVFGYWVNDPERYGVAE----FNSQGKVINIE---EKPLRPR---SNYAVTGLYFYDGRACDYAAELMPSSRGELEITD 202
Cdd:PRK10122  161 QVLAKRMPGDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-240 7.97e-14

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 69.50  E-value: 7.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIInTPHEQPLFQALLgdgAQWGIDVRYAVQP 84
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV-TGYKAELIEEAL---ARPGPDVTFVYNP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAY--LIGRDFVGDkpSCLVL-GDNIFHghglTDVLRRASAREHGATVF--GYWVN---DPERYgvaEFNSQGK 156
Cdd:COG1213    77 DYDETNNIYslWLAREALDE--DFLLLnGDVVFD----PAILKRLLASDGDIVLLvdRKWEKpldEEVKV---RVDEDGR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 157 VINIEEKPLRPRSNYAVTGLYFYDGRacdyAAELMPSSRGELEITDLNRRYLETGDLHLESLGR--------GYAWLDTG 228
Cdd:COG1213   148 IVEIGKKLPPEEADGEYIGIFKFSAE----GAAALREALEALIDEGGPNLYYEDALQELIDEGGpvkavdigGLPWVEID 223
                         250
                  ....*....|..
gi 1768862262 229 THQSLHEASNFI 240
Cdd:COG1213   224 TPEDLERAEELF 235
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
7-236 1.96e-13

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: 68.03  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   7 IILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIInTPHEQPLFQALLGDgaqwGIDVRYAVQPSP 86
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIV-TGYKKEQIEELLKK----YPNIKFVYNPDY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  87 D--GLAQAYLIGRDFVGDkpSCLVL-GDNIFHGHGLTDVLrrASAREHGATVFGYWVNDPERYGVAeFNSQGKVINIEEK 163
Cdd:cd02523    77 AetNNIYSLYLARDFLDE--DFLLLeGDVVFDPSILERLL--SSPADNAILVDKKTKEWEDEYVKD-LDDAGVLLGIISK 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1768862262 164 PLRPRSNYAVT-GLYFYDG----RACDYAAELMPSSRGELEITDLNRRYLETGDLHLESLGrGYAWLDTGTHQSLHEA 236
Cdd:cd02523   152 AKNLEEIQGEYvGISKFSPedadRLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
6-180 3.00e-12

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 66.25  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   6 GIILAGGSGTRLYPITKGISkqllpvydKPMIYY---------PLSVLMLTGIREVLIInTPheqplFQAL-----LGDG 71
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRA--------KPAVPFggkyriidfPLSNCVNSGIRRVGVL-TQ-----YKSHslndhIGSG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  72 AQWGIDVRY-------AVQPSPD-----GLAQAYLIGRDFVGDKPSCLVL---GDNI----------FHghgltdvlrra 126
Cdd:COG0448    70 KPWDLDRKRggvfilpPYQQREGedwyqGTADAVYQNLDFIERSDPDYVLilsGDHIykmdyrqmldFH----------- 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1768862262 127 saREHGA--TVFGYWVNDPE--RYGVAEFNSQGKVINIEEKPLRPRSNYAVTGLYFYD 180
Cdd:COG0448   139 --IESGAdiTVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
4-202 5.98e-12

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 64.93  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   4 RKGIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPL---------FQALLGDGAQW 74
Cdd:PRK13389    9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIenhfdtsfeLEAMLEKRVKR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  75 ------------GIDVRYAVQPSPDGLAQAYLIGRDFVGDKPSCLVLGDNIFHGH-------GLTDVLRRASAREHgATV 135
Cdd:PRK13389   89 qlldevqsicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYesdlsqdNLAEMIRRFDETGH-SQI 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1768862262 136 FGYWVNDPERYGVAEfnSQGKVIN---------IEEKPLRPR--SNYAVTGLYFYDGRACDYAAELMPSSRGELEITD 202
Cdd:PRK13389  168 MVEPVADVTAYGVVD--CKGVELApgesvpmvgVVEKPKADVapSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
6-216 7.39e-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: 58.42  E-value: 7.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   6 GIILAGG--SGTRLYPITKGISKQLLPVYDKPMIYYPLSVL-MLTGIREVLIINTPHEQPLFQALLGDGAQWGIDVRYAV 82
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  83 QPSPDGLAQAYLIGRDFV-GDKPSCLVL--GD-----------NIFHGHGLTDVLRRASAREHGATVFGYWVNDPerygv 148
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQIlAGNPSAFFVlnADvccdfplqellEFHKKHGASGTILGTEASREQASNYGCIVEDP----- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1768862262 149 aefnSQGKVINIEEKPLRPRSNYAVTGLYFYDGRACDYAAELMPSSRGELEITDLNRRYLETGDLHLE 216
Cdd:cd06428   156 ----STGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
7-211 2.20e-09

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 58.07  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   7 IILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGaqwgidVRYAVQPSP 86
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  87 DGLAQAYLIGRDFVGDKpsclvlGDNIFHGHGLTDVLRR-------ASAREHGA--TVFGYWVNDPERYGVAEFNSQGKV 157
Cdd:PRK14358   82 LGTGDAFLSGASALTEG------DADILVLYGDTPLLRPdtlralvADHRAQGSamTILTGELPDATGYGRIVRGADGAV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1768862262 158 INIEEKPLRPRSNYAV----TGLYFYDGRACDYAAELMPSSR-GELEITDLNRRYLETG 211
Cdd:PRK14358  156 ERIVEQKDATDAEKAIgefnSGVYVFDARAPELARRIGNDNKaGEYYLTDLLGLYRAGG 214
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
7-163 3.40e-08

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: 52.90  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   7 IILAGGSGTRLYpitKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIInTPHEQPLFQALLGDgaqwgIDVRYAVQPSP 86
Cdd:cd02540     2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALAN-----PNVEFVLQEEQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  87 DGLAQAYLIGRDFVGDKPS-CLVL-GDNIF-HGHGLTDVLRRASAREHGATVFGYWVNDPERYG-VAEfNSQGKVINI-E 161
Cdd:cd02540    73 LGTGHAVKQALPALKDFEGdVLVLyGDVPLiTPETLQRLLEAHREAGADVTVLTAELEDPTGYGrIIR-DGNGKVLRIvE 151

                  ..
gi 1768862262 162 EK 163
Cdd:cd02540   152 EK 153
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
6-237 1.52e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 52.18  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   6 GIILAGGSGTRLYPITKGISKQLLPVYDK-PMIYYPLSVLMLTGIREVLIInTPHeQPL-FQALLGDGAQWGIDVR---- 79
Cdd:PRK05293    6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVL-TQY-QPLeLNNHIGIGSPWDLDRInggv 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  80 YAVQPSPD--------GLAQAYLIGRDFVGDKPSCLVL---GDNI----------FHGHGLTDV--------LRRASare 130
Cdd:PRK05293   84 TILPPYSEseggkwykGTAHAIYQNIDYIDQYDPEYVLilsGDHIykmdydkmldYHKEKEADVtiavievpWEEAS--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262 131 hgatvfgywvndpeRYGVAEFNSQGKVINIEEKPLRPRSNYAVTGLYFYD-GRACDYaaeLMPSSRGELEITDLNR---- 205
Cdd:PRK05293  161 --------------RFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNwKRLKEY---LIEDEKNPNSSHDFGKnvip 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1768862262 206 RYLETGdlhlESLG----RGYaWLDTGTHQSLHEAS 237
Cdd:PRK05293  224 LYLEEG----EKLYaypfKGY-WKDVGTIESLWEAN 254
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
6-102 3.28e-07

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: 49.85  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   6 GIILAGGSGTRLYPITKGISKQLLPV---YDkpMIYYPLSVLMLTGIREVLIInTPHE-QPLFQAlLGDGAQWGID-VRY 80
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVL-TQYKsRSLNDH-LGSGKEWDLDrKNG 76
                          90       100
                  ....*....|....*....|..
gi 1768862262  81 AVQPSPdglAQAYLIGRDFVGD 102
Cdd:cd02508    77 GLFILP---PQQRKGGDWYRGT 95
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
7-82 4.29e-07

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: 49.74  E-value: 4.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1768862262   7 IILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLMLTG-IREVLIINTPHEQPLFQALLgdgAQWGIDVRYAV 82
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELL---AKYGIDKPVRV 71
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-203 4.40e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 50.92  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   5 KGIILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLMLTGiREVLIInTPHEQPLFQALLGDgaqwgiDVRYAVQP 84
Cdd:PRK14357    2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVV-LGHEAELVKKLLPE------WVKIFLQE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  85 SPDGLAQAYLIGRDFVGDKPSCLVL-GDNIFHGHGLTDVLRRASAREHG-ATVFGYWVNDPERYGVAEFNSqGKVINIEE 162
Cdd:PRK14357   71 EQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEHNRKGAdVTILVADLEDPTGYGRIIRDG-GKYRIVED 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1768862262 163 KPLRPRSNYAV---TGLYFYDGRacdYAAELMP-----SSRGELEITDL 203
Cdd:PRK14357  150 KDAPEEEKKIKeinTGIYVFSGD---FLLEVLPkikneNAKGEYYLTDA 195
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
7-179 1.11e-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: 48.40  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   7 IILAGGSGTRLYPITKGISKQLLPVYDKPMIYYplSVLMLTGIRE---VLIINTPHEQP--LFQALLgdgaQWGIDVRYA 81
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFICRDEHNTKfhLDESLK----LLAPNATVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  82 VQPSP-DGLAQAYLIGRDFV-GDKPSCLVLGDNIFHGhGLTDVLRRASAREHGATVFGYWVNDPeRYGVAEFNSQGKVIN 159
Cdd:cd04183    76 ELDGEtLGAACTVLLAADLIdNDDPLLIFNCDQIVES-DLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVIE 153
                         170       180
                  ....*....|....*....|
gi 1768862262 160 IEEKplRPRSNYAVTGLYFY 179
Cdd:cd04183   154 TAEK--EPISDLATAGLYYF 171
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
7-68 4.74e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.67  E-value: 4.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1768862262   7 IILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLMLTG-IREVLIINTPHEQPLFQALL 68
Cdd:PRK00155    7 IIPAAGKGSRM---GADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
7-72 4.97e-06

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: 46.36  E-value: 4.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1768862262   7 IILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLM-LTGIREVLIINTPHEQPLFQALLGDGA 72
Cdd:cd02516     4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGL 67
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
6-74 9.14e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 45.54  E-value: 9.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1768862262   6 GIILAGGSGTRLypitkGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQW 74
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRV 69
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-163 9.86e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 46.66  E-value: 9.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   1 MTQRKGIILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIInTPHEQPLFQALLGDGAqwgiDVRY 80
Cdd:PRK14355    1 MNNLAAIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLV-VGHQAEKVREHFAGDG----DVSF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  81 AVQ--------------PSPDGLAQAYLIgrdFVGDKPsclvlgdnIFHGHGLTDVLRRASAREHGATVFGYWVNDPERY 146
Cdd:PRK14355   73 ALQeeqlgtghavacaaPALDGFSGTVLI---LCGDVP--------LLRAETLQGMLAAHRATGAAVTVLTARLENPFGY 141
                         170
                  ....*....|....*...
gi 1768862262 147 GVAEFNSQGKVINI-EEK 163
Cdd:PRK14355  142 GRIVRDADGRVLRIvEEK 159
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
6-74 3.65e-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: 3.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1768862262   6 GIILAGGSGTRLypitkGISKQLLPVYDKPMIYYplSVLMLTGIREVLIINTPHEQpLFQALLGDGAQW 74
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLER--VLERLRPAGDEVVVVANDEE-VLAALAGLGVPV 61
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
6-61 3.88e-05

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: 43.75  E-value: 3.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1768862262   6 GIILAGGSGTRLYPITKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQ 61
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSD 58
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
7-163 4.34e-05

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: 44.63  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   7 IILAGGSGTRLY---PitkgisKQLLPVYDKPMIYYPLSVLMLTGIREVLIInTPHEQPLFQALLGDgaqwgIDVRYAVQ 83
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVRAALAD-----LDVEFVLQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  84 PSPDGLAQAYLIGRDFVGDKPS-CLVL-GDN-IFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQGKVINI 160
Cdd:COG1207    74 EEQLGTGHAVQQALPALPGDDGtVLVLyGDVpLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGRVLRI 153

                  ....
gi 1768862262 161 -EEK 163
Cdd:COG1207   154 vEEK 157
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
9-78 6.94e-05

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: 42.57  E-value: 6.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   9 LAGGSGTRLypitKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHeQPLFQALLGDgaqWGIDV 78
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPN-TPKTREYLKE---RGVEV 62
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
2-163 8.42e-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: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   2 TQRKGIILAGGSGTRL---YPitkgisKQLLPVYDKPMIYYPLSVLMLTGIRE-VLIINTPHEQplFQALLGDgaqwgiD 77
Cdd:PRK14354    1 MNRYAIILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKiVTVVGHGAEE--VKEVLGD------R 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  78 VRYAVQPSPDGLAQAYLIGRDFVGDKP-SCLVL-GDN-IFHGHGLTDVLRRASAREHGATVFGYWVNDPERYGVAEFNSQ 154
Cdd:PRK14354   67 SEFALQEEQLGTGHAVMQAEEFLADKEgTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN 146
                         170
                  ....*....|
gi 1768862262 155 GKVINI-EEK 163
Cdd:PRK14354  147 GEVEKIvEQK 156
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
6-104 1.11e-04

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: 42.16  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   6 GIILAGGSGTRLypitkGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALLGDGAQWGID-------- 77
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINpdweegms 77
                          90       100
                  ....*....|....*....|....*....
gi 1768862262  78 --VRYAVQPSPDGlAQAYLIgrdFVGDKP 104
Cdd:cd04182    78 ssLAAGLEALPAD-ADAVLI---LLADQP 102
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
5-37 1.21e-04

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: 42.56  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1768862262   5 KGIILAGGSGTRLYPI-TKGISKQLLPVY-DKPMI 37
Cdd:cd02509     2 YPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLL 36
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
6-55 2.52e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 42.15  E-value: 2.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1768862262   6 GIILAGGSGTRLYPITKGISKQLLPV---YDkpMIYYPLSVLMLTGIREVLII 55
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
6-55 4.18e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 41.41  E-value: 4.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1768862262   6 GIILAGGSGTRLYPITKGISKQLLPVYDK-PMIYYPLSVLMLTGIREVLII 55
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-61 6.46e-04

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: 39.79  E-value: 6.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1768862262   1 MTQR-KGIILAGGSGTRLypitkGISKQLLPVYDKPMIYYPLSVlmLTGIREVLIINTPHEQ 61
Cdd:COG0746     1 MTMPiTGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRPE 55
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-163 8.12e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.62  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262   1 MTQRKG--IILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLMLTGIREVLIINTPHEQPLFQALlgdgAQWGIDV 78
Cdd:PRK14353    1 MTDRTClaIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAA----AKIAPDA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768862262  79 RYAVQPSPDGLAQAYLIGRD----FVGDkpsCLVL-GDNIFHGHGLTDVLRRASAREHGATVFGYWVNDPERYG--VAEf 151
Cdd:PRK14353   74 EIFVQKERLGTAHAVLAAREalagGYGD---VLVLyGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrlIVK- 149
                         170
                  ....*....|...
gi 1768862262 152 nsQGKVINI-EEK 163
Cdd:PRK14353  150 --GGRLVAIvEEK 160
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
7-37 1.20e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.05  E-value: 1.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1768862262   7 IILAGGSGTRLYPI-TKGISKQLLPVY-DKPMI 37
Cdd:COG0836     6 VILAGGSGTRLWPLsRESYPKQFLPLLgEKSLL 38
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
6-67 2.92e-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: 37.94  E-value: 2.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1768862262   6 GIILAGGSGTRLypitkGISKQLLPVYDKPMIYYPLSvlMLTGIREVLIINTPHEQPLFQAL 67
Cdd:cd02503     3 GVILAGGKSRRM-----GGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
7-70 5.84e-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: 37.43  E-value: 5.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1768862262   7 IILAGGSGTRLypiTKGISKQLLPVYDKPMIYYPLSVLMLTG-IREVLIINTPHEQPLFQALLGD 70
Cdd:pfam01128   2 VIPAAGSGKRM---GAGVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAVSPDDTPEFRQLLGD 63
 
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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