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Conserved domains on  [gi|501908721|ref|WP_012666571|]
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glucose-1-phosphate thymidylyltransferase RfbA [Erwinia pyrifoliae]

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 ...
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: 562.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721    2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQA 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   82 SPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  162 SQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 501908721  242 KRQGFKIACLEEIGWRNGWLSDDEVRRSAAALTKTGYGQYLSDLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
 
Name Accession Description Interval E-value
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: 562.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721    2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQA 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   82 SPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  162 SQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 501908721  242 KRQGFKIACLEEIGWRNGWLSDDEVRRSAAALTKTGYGQYLSDLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 551.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  81 ASPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 161 PSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTV 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501908721 241 EKRQGFKIACLEEIGWRNGWLSDDEVRRSAAALTKTGYGQYLSDLLHVRPRQY 293
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRARV 293
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-240 3.82e-174

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: 480.53  E-value: 3.82e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  81 ASPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 161 PSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTV 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-282 5.00e-142

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 401.36  E-value: 5.00e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQA 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  82 SPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 162 SQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTVE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 501908721 242 KRQGFKIACLEEIGWRNGWLSDDEVRRSAAALTKTGYGQYL 282
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 1.46e-97

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: 286.84  E-value: 1.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721    2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDK-PMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   81 ASPDGLAQAFIIGEAFIGGDSC-CLVLGDNIFFGQGFSPKLKQAVE--NPSGATVFGYQVMDPERFGVVEFDDNFRALSL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  158 EEKPSQPK-SRWAVTGLYFYDNRVVEF-AKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEAST 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 501908721  236 FV 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
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: 562.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721    2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQA 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   82 SPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  162 SQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 501908721  242 KRQGFKIACLEEIGWRNGWLSDDEVRRSAAALTKTGYGQYLSDLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 551.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  81 ASPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 161 PSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTV 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501908721 241 EKRQGFKIACLEEIGWRNGWLSDDEVRRSAAALTKTGYGQYLSDLLHVRPRQY 293
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRARV 293
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-240 3.82e-174

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: 480.53  E-value: 3.82e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  81 ASPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 161 PSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTV 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-282 5.00e-142

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 401.36  E-value: 5.00e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQA 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  82 SPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 162 SQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEASTFVQTVE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 501908721 242 KRQGFKIACLEEIGWRNGWLSDDEVRRSAAALTKTGYGQYL 282
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 1.46e-97

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: 286.84  E-value: 1.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721    2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDK-PMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   81 ASPDGLAQAFIIGEAFIGGDSC-CLVLGDNIFFGQGFSPKLKQAVE--NPSGATVFGYQVMDPERFGVVEFDDNFRALSL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  158 EEKPSQPK-SRWAVTGLYFYDNRVVEF-AKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFAWLDTGTHDSLIEAST 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 501908721  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 4.92e-67

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: 208.96  E-value: 4.92e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIIT--TPEDKPHYqrlLGEGDEFGIRLTYA 78
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVgpTGEEIKEA---LGDGSRFGVRITYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  79 EQASPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGqGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNfRALSLE 158
Cdd:cd04189   78 LQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLV 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501908721 159 EKPSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFaWLDTGTHDSLIEASTFV 237
Cdd:cd04189  156 EKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-249 6.56e-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: 189.15  E-value: 6.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721    2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAEQA 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   82 SPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGqGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  162 SQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGFaWLDTGTHDSLIEAS-TFVQTV 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANrLILDEV 238
                         250
                  ....*....|
gi 501908721  241 EKR-QGFKIA 249
Cdd:TIGR01208 239 EREvQGVDDE 248
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-225 8.70e-58

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: 184.71  E-value: 8.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   3 GIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPedKPHY-QRLLGEGDEFGIRLTYAEQA 81
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGY--LGEQiEEYFGDGSKFGVNIEYVVQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  82 SPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGqGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:cd04181   79 EPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501908721 162 SQPKSRWAVTGLYFYDNRVVEFAKQVRPsvRGELEITSINQMYLERGELNVQLLgrGFAWLDTG 225
Cdd:cd04181  158 TLPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-234 2.06e-42

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: 149.67  E-value: 2.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721    1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKpHYQRLLGEGDEFGIRLTYAEQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKE-KVREYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   81 ASPDGLAQAFIIGEAFIGGDscCLVL-GDNIFFgqgfSPKLKQAVENPsGATVFGYQVMDPERFGVVEFDDNfRALSLEE 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDDE--FLVLnGDVLLD----SDLLERLIRAE-APAIAVVEVDDPSDYGVVETDGG-RVTGIVE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501908721  160 KPSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGRGfaWLDTGTHDSLIEAS 234
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDAN 224
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-233 2.14e-39

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: 137.98  E-value: 2.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedkpHY-----QRLLGEGDEFGIRLT 76
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV------GYlaeqiEEYFGDGSRFGVRIT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  77 YAEQASP----DGLAQAfiigEAFIGGDSCCLVLGDnIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNF 152
Cdd:COG1208   75 YVDEGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 153 RALSLEEKPSQPKSRWAVTGLYFYDNRVVEFAKQVRPsvrgeLEITSINQMYLERGELNVQLLgRGFaWLDTGTHDSLIE 232
Cdd:COG1208  150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFDYIPEGEP-----FDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLE 222

                 .
gi 501908721 233 A 233
Cdd:COG1208  223 A 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-234 2.00e-32

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: 120.33  E-value: 2.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTP-----EDkpHYQR-------LLGEG 68
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiED--HFDRsyeleetLEKKG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  69 DE----------FGIRLTYAEQASPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQgfSPKLKQAVE--NPSGATVFGYQ 136
Cdd:cd02541   79 KTdlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSK--EPCLKQLIEayEKTGASVIAVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 137 VMDPE---RFGVVEF----DDNFRALSLEEKPSQ--PKSRWAVTGLYFYDNRVVEFAKQVRPSVRGELEIT-SINQMyLE 206
Cdd:cd02541  157 EVPPEdvsKYGIVKGekidGDVFKVKGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTdAIAKL-LE 235
                        250       260
                 ....*....|....*....|....*....
gi 501908721 207 RGELN-VQLLGRgfaWLDTGTHDSLIEAS 234
Cdd:cd02541  236 EEPVYaYVFEGK---RYDCGNKLGYLKAT 261
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-233 7.65e-19

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: 82.94  E-value: 7.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedkpHYQR-----LLGEGDEFGIRLTYA 78
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISV------NYLAemiedYFGDGSKFGVNISYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  79 EQASPDGLAQAFIIGEAFIggDSCCLVLGDNIFFGQGFSPKLKQAVENPSGATV----FGYQVmdPerFGVVEFDDNfRA 154
Cdd:cd06426   76 REDKPLGTAGALSLLPEKP--TDPFLVMNGDILTNLNYEHLLDFHKENNADATVcvreYEVQV--P--YGVVETEGG-RI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 155 LSLEEKPSQpksRWAV-TGLYFYDNRVVEfakQVRPSVRgeLEITSINQMYLERGE-LNVQLLgRGFaWLDTGTHDSLIE 232
Cdd:cd06426  149 TSIEEKPTH---SFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGKkVGVFPI-HEY-WLDIGRPEDYEK 218

                 .
gi 501908721 233 A 233
Cdd:cd06426  219 A 219
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 1.27e-18

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 83.54  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYplSV--LMLAGIRDVLIITTP-----EDkpHY-------QRLLGE 67
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiED--HFdrsyeleATLEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  68 GDE----------FGIRLTYAEQASPDGLAQAFIIGEAFIGGDSCCLVLGDNIFFGQgfSPKLKQAVE--NPSGATVFGY 135
Cdd:COG1210   81 GKEelleevrsisPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQMIEvyEETGGSVIAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 136 QVMDPE---RFGVVE----FDDNFRALSLEEKPSQPK--SRWAVTGLYFYDNRVVEFAKQVRPSVRGELEIT-SINQMYL 205
Cdd:COG1210  159 QEVPPEevsKYGIVDgeeiEGGVYRVTGLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTdAIAALAK 238
                        250       260
                 ....*....|....*....|....*...
gi 501908721 206 ERGELNVQLLGRgfaWLDTGTHDSLIEA 233
Cdd:COG1210  239 EEPVYAYEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-233 2.83e-18

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: 81.45  E-value: 2.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVL---------IITtpedkpHYqrllGEGDEFGIR 74
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVlsvgylaeqIEE------YF----GDGYRGGIR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  75 LTYAEQASPDGLAQAFIIGEAFIGGDSCCLVLGDNiFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRA 154
Cdd:cd06915   72 IYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 155 LSLEEKPSQPKSRWAVTGLYFYDNRVVEFAKQVRPSvrgeLEiTSINQMYLERGELnvqllgRGFA----WLDTGTHDSL 230
Cdd:cd06915  151 IAFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDY 219

                 ...
gi 501908721 231 IEA 233
Cdd:cd06915  220 ARA 222
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-226 5.86e-17

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: 78.02  E-value: 5.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLI-------ITTPEDKPHYQRLlgegdefGI 73
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILavnyrpeDMVPFLKEYEKKL-------GI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  74 RLTYAEQASPDGLAQAFIIGEAFIGGDS-CCLVLGDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFD-DN 151
Cdd:cd06425   74 KITFSIETEPLGTAGPLALARDLLGDDDePFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDeNT 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501908721 152 FRALSLEEKPSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGEL--EITSINQMYLErgELNvqllgrGFaWLDTGT 226
Cdd:cd06425  154 GRIERFVEKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIfpKMASEGQLYAY--ELP------GF-WMDIGQ 221
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-65 1.71e-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: 76.54  E-value: 1.71e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLL 65
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-62 4.33e-13

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: 66.89  E-value: 4.33e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQ 62
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIE 62
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-177 2.14e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 63.56  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   3 GIVLAGGSGTRLHPITRGLSKqllpvydkPMIYY---------PLSVLMLAGIRDVLIITtpEDKPH-YQRLLGEGDEF- 71
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT--QYKSHsLNDHIGSGKPWd 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  72 ------GIRLTYAEQASPD-----GLAQAF-----IIGEA---FIggdsccLVL-GDNIF---FGQgfspKLKQAVENPS 128
Cdd:COG0448   74 ldrkrgGVFILPPYQQREGedwyqGTADAVyqnldFIERSdpdYV------LILsGDHIYkmdYRQ----MLDFHIESGA 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501908721 129 GATVFGYQV--MDPERFGVVEFDDNFRALSLEEKPSQPKSRWAVTGLYFYD 177
Cdd:COG0448  144 DITVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-233 7.37e-11

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: 60.66  E-value: 7.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedkpHYQ-----RLLGEgDEFGIRLT 76
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNT------HHLadqieAHLGD-SRFGLRIT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  77 YAEQasPD-------GLAQAfiigEAFIGGDSCCLVLGDNIFFGqGFSPKLKQAVENPSGATVFGYQVMDPERFGVVEFD 149
Cdd:cd06422   74 ISDE--PDelletggGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 150 DNfRALSLEEKPSQPKSRWAVTGLYFYDNRVVEFAKQvrpsvrgelEITSINQMY---LERGELnVQLLGRGFaWLDTGT 226
Cdd:cd06422  147 LD-ADGRLRRGGGGAVAPFTFTGIQILSPELFAGIPP---------GKFSLNPLWdraIAAGRL-FGLVYDGL-WFDVGT 214

                 ....*..
gi 501908721 227 HDSLIEA 233
Cdd:cd06422  215 PERLLAA 221
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 3.24e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 59.10  E-value: 3.24e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501908721   2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIIT 53
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
4-208 1.72e-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: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHpitRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKPHYQRLLGEGdefgirLTYAEQASP 83
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  84 DGLAQAFIIG-EAFIGGDSCCLVL-GDNIFfgqgFSPKLKQAV-----ENPSGATVFGYQVMDPERFG-VVEFDDNFRAL 155
Cdd:PRK14358  82 LGTGDAFLSGaSALTEGDADILVLyGDTPL----LRPDTLRALvadhrAQGSAMTILTGELPDATGYGrIVRGADGAVER 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501908721 156 SLEEKPSQPKSRwAV----TGLYFYDNRVVEFAKQV-RPSVRGELEITSINQMYLERG 208
Cdd:PRK14358 158 IVEQKDATDAEK-AIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-223 1.80e-09

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: 56.86  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEdKPHYQRLLGEgdEFGIRLTYAEQASP 83
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYK-KEQIEELLKK--YPNIKFVYNPDYAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  84 DGLAQAFIIGEAFIGGDscCLVL-GDNIFFGQGfspkLKQAVENPSGATVFGYQVMDPERFGVVEFDDNFRALSLEEKPS 162
Cdd:cd02523   79 TNNIYSLYLARDFLDED--FLLLeGDVVFDPSI----LERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGIISKA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501908721 163 QPKSR--WAVTGLYFYD----NRVVEFAKQVRPSVRGELEITSINQMYLERGELNVQLLGrGFAWLD 223
Cdd:cd02523  153 KNLEEiqGEYVGISKFSpedaDRLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-67 8.06e-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: 54.75  E-value: 8.06e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501908721   4 IVLAGGSGTRLHpitRGLSKQLLPVYDKPMIYYPLSVLMLAG-IRDVLIITTPEDKPHYQRLLGE 67
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
4-166 2.24e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 54.46  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHPITRGLSKQLLPVYDK-PMIYYPLSVLMLAGIRDVLIITtpEDKP-----HYQR----LLGEGDEFgI 73
Cdd:PRK00725  19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLT--QYKAhslirHIQRgwsfFREELGEF-V 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  74 RLTYAEQASPD-----GLAQAF-----II---GEAFIggdsccLVL-GDNIFfGQGFSPKLKQAVENPSGATVFGYQV-- 137
Cdd:PRK00725  96 DLLPAQQRVDEenwyrGTADAVyqnldIIrryDPKYV------VILaGDHIY-KMDYSRMLADHVESGADCTVACLEVpr 168
                        170       180
                 ....*....|....*....|....*....
gi 501908721 138 MDPERFGVVEFDDNFRALSLEEKPSQPKS 166
Cdd:PRK00725 169 EEASAFGVMAVDENDRITAFVEKPANPPA 197
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-207 3.57e-08

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 53.76  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   2 KGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPE------------------DKPHYQR 63
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSknsienhfdtsfeleamlEKRVKRQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  64 LLGEGDEF---GIRLTYAEQASPDGLAQAFIIGEAFIGGDSCCLVLGDNI-------------------FFGQGFSPKLK 121
Cdd:PRK13389  90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeyesdlsqdnlaemirrFDETGHSQIMV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 122 QAVENPSGATVF---GYQVMDPER---FGVVEfddnfralslEEKPSQPKSRWAVTGLYFYDNRVVEFAKQVRPSVRGEL 195
Cdd:PRK13389 170 EPVADVTAYGVVdckGVELAPGESvpmVGVVE----------KPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEI 239
                        250
                 ....*....|..
gi 501908721 196 EITSINQMYLER 207
Cdd:PRK13389 240 QLTDAIDMLIEK 251
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-110 4.61e-08

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 53.35  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTPEDKP---HY---------------Q 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAvenHFdtsyeleslleqrvkR 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501908721  63 RLLGEGDEF---GIRLTYAEQASPDGLAQAFIIGEAFIGGDSCCLVLGDNI 110
Cdd:PRK10122  84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVV 134
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 7.57e-08

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 52.06  E-value: 7.57e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501908721   4 IVLAGGSGTRLHPitrGLSKQLLPVYDKPMIYYPLSVLMLAG-IRDVLIITTPEDKPHYQRLL 65
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-70 9.54e-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: 51.37  E-value: 9.54e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501908721   4 IVLAGGSGTRLHpitRGLSKQLLPVYDKPMIYYPLSVLM-LAGIRDVLIITTPEDKPHYQRLLGEGDE 70
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-73 4.14e-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: 49.46  E-value: 4.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501908721   3 GIVLAGGSGTRLHPITRGLSKQLLPV---YDkpMIYYPLSVLMLAGIRDVLIITtpEDKPH-YQRLLGEGDEFGI 73
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT--QYKSRsLNDHLGSGKEWDL 71
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-108 1.05e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 48.23  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   3 GIVLAGGSGTRLhpitrGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedKPHYQRLLGEGDEFGIRLTYAEQAS 82
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVL----GADAEEVAAALAGLGVRVVVNPDWE 76
                         90       100
                 ....*....|....*....|....*...
gi 501908721  83 pDGLAQAFIIGEAFIGG--DSCCLVLGD 108
Cdd:COG2068   77 -EGMSSSLRAGLAALPAdaDAVLVLLGD 103
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-234 1.79e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 48.71  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLSKQLLPVYDK-PMIYYPLSVLMLAGIRDVLIITtpedkpHYQRLL-----GEGDEFGI- 73
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT------QYQPLElnnhiGIGSPWDLd 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  74 RLT--------YAEQASPD---GLAQAFIIGEAFIggDSC----CLVL-GDNIFfGQGFSPKLKQAVENPSGATVfgyQV 137
Cdd:PRK05293  78 RINggvtilppYSESEGGKwykGTAHAIYQNIDYI--DQYdpeyVLILsGDHIY-KMDYDKMLDYHKEKEADVTI---AV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 138 MD-P----ERFGVVEFDDNFRALSLEEKPSQPKSRWAVTGLYFY---------------DNRVVEFAKQVRPSvrgelei 197
Cdd:PRK05293 152 IEvPweeaSRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL------- 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 501908721 198 tsinqmYLERGElnvqllgRGFA------WLDTGTHDSLIEAS 234
Cdd:PRK05293 225 ------YLEEGE-------KLYAypfkgyWKDVGTIESLWEAN 254
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-108 1.46e-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: 44.86  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   3 GIVLAGGSGTRLhpitrGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedKPHYQRLLGEGDEFGIRLTYAEQAS 82
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVL----GAEADAVRAALAGLPVVVVINPDWE 73
                         90       100
                 ....*....|....*....|....*...
gi 501908721  83 pDGLAQAFIIG-EAFIGGDSCCLV-LGD 108
Cdd:cd04182   74 -EGMSSSLAAGlEALPADADAVLIlLAD 100
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-55 2.12e-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: 44.11  E-value: 2.12e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 501908721   6 LAGGSGTRLhpitRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITTP 55
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-53 2.52e-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: 44.87  E-value: 2.52e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501908721   1 MKGIVLAGGSGTRLHPITR-GLSKQLLPVY-DKPMIYYPLS-VLMLAGIRDVLIIT 53
Cdd:cd02509    1 IYPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVT 56
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-103 3.17e-05

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: 44.55  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   3 GIVLAGG--SGTRLHPITRGLSKQLLPVYDKPMIYYPLSVL-MLAGIRDVLIITTPEDKPHYQRLLGEGDEFGIRLTYAE 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501908721  80 QASPDGLA---------------QAFIIgeafIGGDSCC 103
Cdd:cd06428   81 EYKPLGTAgglyhfrdqilagnpSAFFV----LNADVCC 115
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-66 4.21e-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: 4.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501908721    3 GIVLAGGSGTRLhpitrGLSKQLLPVYDKPMIYYPLSVLMLAGiRDVLIITTPEDKPHYQRLLG 66
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG 58
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-166 9.75e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 43.28  E-value: 9.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   3 GIVLAGGSGTRLHPITRGLSKQLLP---VYDkpMIYYPLSVLMLAGIRDVLIITtpEDKPH--YQ------RLLGEGDEF 71
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLT--QYKSHslDRhisqtwRLSGLLGNY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  72 gIRLTYAEQ--------ASPDGLAQA--FIIGEAfigGDSCCLVLGDNIF---FGQgfspKLKQAVENPSGATVFGYQV- 137
Cdd:PRK00844  84 -ITPVPAQQrlgkrwylGSADAIYQSlnLIEDED---PDYVVVFGADHVYrmdPRQ----MVDFHIESGAGVTVAAIRVp 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 501908721 138 -MDPERFGVVEFDDNFRALSLEEKPSQPKS 166
Cdd:PRK00844 156 rEEASAFGVIEVDPDGRIRGFLEKPADPPG 185
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-209 1.21e-04

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: 42.50  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHpitRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedkpHYQR-----LLGEGDefgirLTYA 78
Cdd:cd02540    2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVV------GHGAeqvkkALANPN-----VEFV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  79 EQASPDGLAQAFIIGEAFIGGDS-CCLVL-GDN--IffgqgfSPK-LKQAVE----NPSGATVFGYQVMDPERFG--VVE 147
Cdd:cd02540   68 LQEEQLGTGHAVKQALPALKDFEgDVLVLyGDVplI------TPEtLQRLLEahreAGADVTVLTAELEDPTGYGriIRD 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501908721 148 FDDNFRALsLEEK---PSQPKSRWAVTGLYFYDNRVVEFA-KQVRPS-VRGELEITSINQMYLERGE 209
Cdd:cd02540  142 GNGKVLRI-VEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDIIALAVADGL 207
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 2.06e-04

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 42.36  E-value: 2.06e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501908721   1 MKGIVLAGGSGTRLHPITRGLS-KQLLPVY-DKPMIYypLSVLMLAGI---RDVLIIT 53
Cdd:COG0836    3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ--QTVERLAGLvppENILVVT 58
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-238 2.58e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.06  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   1 MKGIVLAGGSGTRLHpitRGLSKQLLPVYDKPMIYYplsVLMLAG-IRDVLIITTPEDKPHYQRLLGEGDEFgirltyAE 79
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINW---VIDTAKkVAQKVGVVLGHEAELVKKLLPEWVKI------FL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  80 QASPDGLAQAFIIGEAFIGGDSCCLVL-GDNIFFGQGFSPKL-KQAVENPSGATVFGYQVMDPERFG-VVEFDDNFRALS 156
Cdd:PRK14357  69 QEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLiEEHNRKGADVTILVADLEDPTGYGrIIRDGGKYRIVE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721 157 LEEKPSQPKSRWAV-TGLYFYDNR----------------------VVEFAKQVRpSVRGE--LEITSINQ----MYLE- 206
Cdd:PRK14357 149 DKDAPEEEKKIKEInTGIYVFSGDfllevlpkiknenakgeyyltdAVNFAEKVR-VVKTEdlLEITGVNTriqlAWLEk 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 501908721 207 --RGELNVQLLGRGFAWLDTGT----------HDSLIEASTFVQ 238
Cdd:PRK14357 228 qlRMRILEELMENGVTILDPNTtyihydveigMDTIIYPMTFIE 271
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
3-53 5.30e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.99  E-value: 5.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501908721   3 GIVLAGGSGTRLHPITRGLSKQLLPV---YDkpMIYYPLSVLMLAGIRDVLIIT 53
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLT 57
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-64 8.07e-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: 39.41  E-value: 8.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501908721   1 MKGIVLAGGSGTRLhpitrGLSKQLLPVYDKPMIYYPLSVLMLAgIRDVLIITTPEDKphYQRL 64
Cdd:COG0746    5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPER--YAAL 60
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-54 3.62e-03

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: 37.97  E-value: 3.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501908721   3 GIVLAGGSGTRLHPITRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITT 54
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCC 54
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-171 4.41e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.30  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHpitRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedKPHYQRLLGEGDEFGIRLTYAEQASP 83
Cdd:PRK14353   9 IILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVV----GPGAEAVAAAAAKIAPDAEIFVQKER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721  84 DGLAQAFIIG-EAFIGGDSCCLVL-GDNIFFGQGFSPKLKQAVENPSGATVFGYQVMDPERFG-VVEFDDNFRALsLEEK 160
Cdd:PRK14353  82 LGTAHAVLAArEALAGGYGDVLVLyGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrLIVKGGRLVAI-VEEK 160
                        170
                 ....*....|.
gi 501908721 161 PSQPKSRwAVT 171
Cdd:PRK14353 161 DASDEER-AIT 170
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
1-53 7.75e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 37.56  E-value: 7.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501908721   1 MK---GIVLAGGSGTRLHPITRGLSKQLLPVYDK-PMIYYPLSVLMLAGIRDVLIIT 53
Cdd:PRK02862   1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-108 9.32e-03

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: 37.31  E-value: 9.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501908721   4 IVLAGGSGTRLHpitRGLSKQLLPVYDKPMIYYPLSVLMLAGIRDVLIITtpedkpHYQR-----LLGEgdefgIRLTYA 78
Cdd:COG1207    6 VILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVV------GHGAeqvraALAD-----LDVEFV 71
                         90       100       110
                 ....*....|....*....|....*....|..
gi 501908721  79 EQASPDGLAQAFIIGEAFIGGDS-CCLVL-GD 108
Cdd:COG1207   72 LQEEQLGTGHAVQQALPALPGDDgTVLVLyGD 103
 
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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