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Conserved domains on  [gi|1330549855|ref|WP_102475756|]
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glucose-1-phosphate thymidylyltransferase RfbA [Shewanella sp. 10N.286.52.C2]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

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

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

Graphical summary

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List of domain hits

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

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 570.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 161 PEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1330549855 241 ENVQGLKVACLEEIAWRNGWLSDEQVLTLAKPMMKNEYGQYLTRLVNEK 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 570.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 161 PEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1330549855 241 ENVQGLKVACLEEIAWRNGWLSDEQVLTLAKPMMKNEYGQYLTRLVNEK 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-285 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: 570.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 162 EAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1330549855 242 NVQGLKVACLEEIAWRNGWLSDEQVLTLAKPMMKNEYGQYLTRL 285
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 6.76e-178

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: 490.16  E-value: 6.76e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 161 PEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-286 8.49e-149

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 418.69  E-value: 8.49e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 162 EAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1330549855 242 NVQGLKVACLEEIAWRNGWLSDEQVLTLAKPMMKNEYGQYLTRLV 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 3.66e-100

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: 293.39  E-value: 3.66e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDK-PMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSV-CLVLGDNIFYGQSFSSTLKNAASRES--GATVFGYQVKDPERFGVVEFDEDMKAVSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 158 EEKPEAPK-SNYAVTGLYFYDNRVVEM-AKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASS 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1330549855 236 FV 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 570.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 161 PEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1330549855 241 ENVQGLKVACLEEIAWRNGWLSDEQVLTLAKPMMKNEYGQYLTRLVNEK 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-285 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: 570.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 162 EAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1330549855 242 NVQGLKVACLEEIAWRNGWLSDEQVLTLAKPMMKNEYGQYLTRL 285
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 6.76e-178

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: 490.16  E-value: 6.76e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 161 PEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-286 8.49e-149

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 418.69  E-value: 8.49e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 162 EAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASSFVQTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1330549855 242 NVQGLKVACLEEIAWRNGWLSDEQVLTLAKPMMKNEYGQYLTRLV 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 3.66e-100

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: 293.39  E-value: 3.66e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDK-PMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSV-CLVLGDNIFYGQSFSSTLKNAASRES--GATVFGYQVKDPERFGVVEFDEDMKAVSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 158 EEKPEAPK-SNYAVTGLYFYDNRVVEM-AKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFAWLDTGTHESLHEASS 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1330549855 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 2.75e-72

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 222.44  E-value: 2.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEdNAGFKRLLGDGSDFGINLEYAIQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGqSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDmKAVSIEEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330549855 161 PEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFaWLDTGTHESLHEASSFV 237
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 1.13e-64

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 202.04  E-value: 1.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   3 GIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAgFKRLLGDGSDFGINLEYAIQPS 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQ-IEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  83 PDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGqSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEKPE 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330549855 163 APKSNYAVTGLYFYDNRVVEMAKQVKPshRGELEITTLNEMYLNDGLLNVELLgrGFAWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-249 7.53e-62

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: 199.55  E-value: 7.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAIQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGqSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 162 EAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGFaWLDTGTHESLHEASSFV--QT 239
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIldEV 238

                         250
                  ....*....|
gi 1330549855 240 IENVQGLKVA 249
Cdd:TIGR01208 239 EREVQGVDDE 248
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-225 6.95e-48

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: 164.30  E-value: 6.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAgFKRLLGDGSDFGINLEYAIQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEK-VREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  81 PSPDGLAQAFIIGEEFIgDDSVCLVLGDNIFYGQSfsstLKNAASREsGATVFGYQVKDPERFGVVEFDEDmKAVSIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDL----LERLIRAE-APAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330549855 161 PEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGRGfaWLDTG 225
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 2.01e-45

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: 153.38  E-value: 2.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITT--PEDnagFKRLLGDGSDFGINLEYAI 79
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQ---IEEYFGDGSRFGVRITYVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  80 QPSP----DGLAQAfiigEEFIGDDSVCLVLGDnIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAV 155
Cdd:COG1208    78 EGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVT 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330549855 156 SIEEKPEAPKSNYAVTGLYFYDNRVVEMAKQvkpshRGELEITTLNEMYLNDGLLNVELLgRGFaWLDTGTHESLHEA 233
Cdd:COG1208   153 RFVEKPEEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-234 2.27e-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: 2.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEdnagfKRLLGDGSDFGINLE---- 76
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRG-----KRAIEDHFDRSYELEetle 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  77 ---------------------YAIQPSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQsfSSTLKN--AASRESGATVF 133
Cdd:cd02541    76 kkgktdlleevriisdlanihYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSK--EPCLKQliEAYEKTGASVI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 134 GYQVKDPE---RFGVV---EFDEDM-KAVSIEEKP---EAPkSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEIT-TLNE 202
Cdd:cd02541   154 AVEEVPPEdvsKYGIVkgeKIDGDVfKVKGLVEKPkpeEAP-SNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTdAIAK 232

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1330549855 203 MYLNDGLLNVELLGRgfaWLDTGTHESLHEAS 234
Cdd:cd02541   233 LLEEEPVYAYVFEGK---RYDCGNKLGYLKAT 261
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-226 9.43e-23

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 95.10  E-value: 9.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTP-----ED-------------NAGFKR 63
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiEDhfdrsyeleatleAKGKEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  64 LLG---DGSDfGINLEYAIQPSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQsfSSTLKN--AASRESGATVFGYQVK 138
Cdd:COG1210    85 LLEevrSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQmiEVYEETGGSVIAVQEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 139 DPE---RFGVVEFDED----MKAVSIEEKP---EAPkSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITT-LNEMYLND 207
Cdd:COG1210   162 PPEevsKYGIVDGEEIeggvYRVTGLVEKPapeEAP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDaIAALAKEE 240

                         250
                  ....*....|....*....
gi 1330549855 208 GLLNVELLGRgfaWLDTGT 226
Cdd:COG1210   241 PVYAYEFEGK---RYDCGD 256
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-233 7.45e-21

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: 88.34  E-value: 7.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITtpednaGFKR-----LLGDGSDFGINLEYA 78
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISV------NYLAemiedYFGDGSKFGVNISYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  79 IQPSPDGLAQAFIIGEEFIgDDSVCLVLGD---NIFYGQSFSSTLKNAASRESGATVFGYQVkdPerFGVVEFDEDmKAV 155
Cdd:cd06426    76 REDKPLGTAGALSLLPEKP-TDPFLVMNGDiltNLNYEHLLDFHKENNADATVCVREYEVQV--P--YGVVETEGG-RIT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 156 SIEEKPEapkSNYAV-TGLYFYDNRVVEmakQVKPSHRgeLEITTLNEMYLNDGL-LNVELLgRGFaWLDTGTHESLHEA 233
Cdd:cd06426   150 SIEEKPT---HSFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGKkVGVFPI-HEY-WLDIGRPEDYEKA 219
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 2.32e-20

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: 87.22  E-value: 2.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITtpednaGFKR-----LLGDGSDFGINLEYA 78
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSV------GYLAeqieeYFGDGYRGGIRIYYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  79 IQPSPDGLAQAFIIGEEFIGDDSVcLVLgdnifYGQSF-----SSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMK 153
Cdd:cd06915    76 IEPEPLGTGGAIKNALPKLPEDQF-LVL-----NGDTYfdvdlLALLAALRASGADATMALRRVPDASRYGNVTVDGDGR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 154 AVSIEEKPEAPKSNYAVTGLYFYDNRVVEMAKQVKPShrgeLEITTLNEMYLNDGLLNVELLGRgFawLDTGTHESLHEA 233
Cdd:cd06915   150 VIAFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LEADVLPALVKRGRLYGFEVDGY-F--IDIGIPEDYARA 222
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-181 3.50e-20

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: 86.88  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITT--PEDNAGFKRLLGDgsDFGINLEYA 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEYEK--KLGIKITFS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  79 IQPSPDGLAQAFIIGEEFIGDDSVC-LVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAV-S 156
Cdd:cd06425    79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIeR 158

                         170       180
                  ....*....|....*....|....*
gi 1330549855 157 IEEKPEAPKSNYAVTGLYFYDNRVV 181
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVL 183
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-59 1.99e-17

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: 78.85  E-value: 1.99e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNA 59
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQA 59
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-177 1.45e-16

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 78.96  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   3 GIVLAGGSGTRLYPLTRGVSKqllpiydkPMV-F---Y-----PISTLMLAGIKDILIITtpednaGFK-----RLLGDG 68
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVpFggkYriidfPLSNCVNSGIRRVGVLT------QYKshslnDHIGSG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  69 SDFGINLE---------YAIQPSPD---GLAQAFIIGEEFIGD---DSVCLVLGDNIF---YGQSFsstlknAASRESGA 130
Cdd:COG0448    70 KPWDLDRKrggvfilppYQQREGEDwyqGTADAVYQNLDFIERsdpDYVLILSGDHIYkmdYRQML------DFHIESGA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1330549855 131 --TVFGYQV--KDPERFGVVEFDEDMKAVSIEEKPEAPKSNYAVTGLYFYD 177
Cdd:COG0448   144 diTVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-59 5.81e-14

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: 69.20  E-value: 5.81e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNA 59
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQA 59
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 2.50e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 68.76  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNA-----------------GFKR 63
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAvenhfdtsyeleslleqRVKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  64 -LLGDGSDF---GINLEYAIQPSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAAS-----RESG-ATVF 133
Cdd:PRK10122   84 qLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAmiarfNETGrSQVL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330549855 134 GYQVK-DPERFGVVEFDEDMKA-------VSIEEKPEAPK---SNYAVTGLYFYDNRVVEMAKQVKPSHRGELEIT 198
Cdd:PRK10122  164 AKRMPgDLSEYSVIQTKEPLDRegkvsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-205 4.59e-12

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 65.31  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNA-------GF-----------KR 63
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSienhfdtSFeleamlekrvkRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  64 LLGDGSDF---GINLEYAIQPSPDGLAQAFIIGEEFIGDDSVCLVLGDNIFygQSFSSTLK--NAAS-----RESGAT-V 132
Cdd:PRK13389   90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIL--DEYESDLSqdNLAEmirrfDETGHSqI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 133 FGYQVKDPERFGVVEFD-------EDMKAVSIEEKP---EAPkSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNE 202
Cdd:PRK13389  168 MVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPkadVAP-SNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAID 246


                  ...
gi 1330549855 203 MYL 205
Cdd:PRK13389  247 MLI 249
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-208 2.73e-11

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 63.84  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLyplTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFginleyAIQPSP 83
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAF------ARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  84 DGLAQAFIIGEEFI--GDDSVCLVLGDN-IFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSIEEK 160
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1330549855 161 PEAPKSNYAV----TGLYFYDNRVVEMAKQVKPSHR-GELEITTLNEMYLNDG 208
Cdd:PRK14358  162 KDATDAEKAIgefnSGVYVFDARAPELARRIGNDNKaGEYYLTDLLGLYRAGG 214
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-233 9.10e-11

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: 60.71  E-value: 9.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAgFKRLLGDGSDFGI--NLEYAIQp 81
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQ-IEELLKKYPNIKFvyNPDYAET- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  82 spdGLAQAFIIGEEFIGDDsvCLVL-GDNIFYgqsfSSTLKNAASRESGATVFGYQVKDPERFGVVEFDED-MKAVSIEE 159
Cdd:cd02523    80 ---NNIYSLYLARDFLDED--FLLLeGDVVFD----PSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDaGVLLGIIS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330549855 160 KPEAPKSNYAVT-GLYFYD----NRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVELLGrGFAWLDTGTHESLHEA 233
Cdd:cd02523   151 KAKNLEEIQGEYvGISKFSpedaDRLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-191 2.29e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 59.48  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITtpednaGFKRLLGDG--SDFGINLEYAI 79
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT------GYKAELIEEalARPGPDVTFVY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  80 QPSPDG------LAQAFiigeEFIGDDsvCLVL-GDnIFYGQSFSSTLknAASRESGATVFGYQVKDPErfgvvefDEDM 152
Cdd:COG1213    75 NPDYDEtnniysLWLAR----EALDED--FLLLnGD-VVFDPAILKRL--LASDGDIVLLVDRKWEKPL-------DEEV 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1330549855 153 KaVSIEEkpeapksnyavtglyfyDNRVVEMAKQVKPSH 191
Cdd:COG1213   139 K-VRVDE-----------------DGRIVEIGKKLPPEE 159
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-233 1.17e-09

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: 57.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   2 KGIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIittpedNAG-----FKRLLGDgSDFGINLE 76
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV------NTHhladqIEAHLGD-SRFGLRIT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  77 yaIQPSPD-------GLAQAfiigEEFIGDDSVCLVLGDnIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFD 149
Cdd:cd06422    74 --ISDEPDelletggGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 150 EDmKAVSIEEKPEAPKSNYAVTGLYFYDNRVVEMAKQVKPShrgeleittLNEMYlNDGLLNVELLG---RGFaWLDTGT 226
Cdd:cd06422   147 LD-ADGRLRRGGGGAVAPFTFTGIQILSPELFAGIPPGKFS---------LNPLW-DRAIAAGRLFGlvyDGL-WFDVGT 214


                  ....*..
gi 1330549855 227 HESLHEA 233
Cdd:cd06422   215 PERLLAA 221
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-209 6.45e-09

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: 55.21  E-value: 6.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLY-PLtrgvSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAgFKRLLGDgsdfgINLEYAIQPS 82
Cdd:cd02540     2 VILAAGKGTRMKsDL----PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQ-VKKALAN-----PNVEFVLQEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  83 PDGLAQAFIIGEEFI-GDDSVCLVLgdnifYG-------QSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKA 154
Cdd:cd02540    72 QLGTGHAVKQALPALkDFEGDVLVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330549855 155 VSI-EEK---PEAPKSNYAVTGLYFYDNRVVEMA-KQVKPSH-RGELEITTLNEMYLNDGL 209
Cdd:cd02540   147 LRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDIIALAVADGL 207
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-234 9.58e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 52.56  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVSKQLLP------IYDkpmvfYPISTLMLAGIKDILIITTPEDNAgFKRLLGDGSDFGIN 74
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPfggkyrIID-----FTLSNCANSGIDTVGVLTQYQPLE-LNNHIGIGSPWDLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  75 LE----YAIQPSPD--------GLAQAFIIGEEFIG--DDSVCLVL-GDNIF---YGQSFSSTLKNAASresgATVFGYQ 136
Cdd:PRK05293   78 RInggvTILPPYSEseggkwykGTAHAIYQNIDYIDqyDPEYVLILsGDHIYkmdYDKMLDYHKEKEAD----VTIAVIE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855 137 V--KDPERFGVVEFDEDMKAVSIEEKPEAPKSNYAVTGLYFYDNRV-----VEMAKQVKPSHR-GELEITtlneMYLNDG 208
Cdd:PRK05293  154 VpwEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRlkeylIEDEKNPNSSHDfGKNVIP----LYLEEG 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1330549855 209 llnvellGRGFA------WLDTGTHESLHEAS 234
Cdd:PRK05293  230 -------EKLYAypfkgyWKDVGTIESLWEAN 254
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-213 1.14e-07

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: 51.87  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   3 GIVLAGG--SGTRLYPLTRGVSKQLLPIYDKPMVFYPISTL-MLAGIKDILIITTPEDNAgFKRLLGDGS-DFGINLEYA 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQqEFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  79 IQPSPDGLAQAF-----IIGEefiGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQV--KDPERFGVVEFDED 151
Cdd:cd06428    80 QEYKPLGTAGGLyhfrdQILA---GNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGCIVEDPS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330549855 152 MKAVS-IEEKPEAPKSNYAVTGLYFYDNRVVEMAKQVKPSHRGELEITTLNEMYLNDGLLNVE 213
Cdd:cd06428   157 TGEVLhYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-108 1.63e-07

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: 50.25  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   3 GIVLAGGSGTRLypltrGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAiqps 82
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWE---- 73

                          90       100
                  ....*....|....*....|....*...
gi 1330549855  83 pDGLAQAFIIGEEFIGDD-SVCLV-LGD 108
Cdd:cd04182    74 -EGMSSSLAAGLEALPADaDAVLIlLAD 100
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-53 2.79e-07

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: 50.65  E-value: 2.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330549855   1 MKGIVLAGGSGTRLYPLTR-GVSKQLLPIY-DKPMVFYPISTLM-LAGIKDILIIT 53
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVVT 56
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-209 3.73e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.99  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRL---YPltrgvsKQLLPIYDKPMVFYPISTLMLAGIKDILIIttpednAGF-----KRLLGDGSdfginl 75
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------VGHgaeevKEVLGDRS------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  76 EYAIQPSPDGLAQAFIIGEEFIGD-DSVCLVL-GDN-IFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDM 152
Cdd:PRK14354   68 EFALQEEQLGTGHAVMQAEEFLADkEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330549855 153 KAVSI-EEK---PEAPKSNYAVTGLYFYDNRV-VEMAKQVKPSH-RGELEITTLNEMYLNDGL 209
Cdd:PRK14354  148 EVEKIvEQKdatEEEKQIKEINTGTYCFDNKAlFEALKKISNDNaQGEYYLTDVIEILKNEGE 210
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 1.13e-06

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: 48.59  E-value: 1.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330549855   4 IVLAGGSGTRLyplTRGVSKQLLPIYDKPMVFYPISTLMLAG-IKDILIITTPEDNAGFKRLLGD 67
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-55 1.68e-06

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 47.58  E-value: 1.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1330549855   6 LAGGSGTRLypltRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTP 55
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-166 1.94e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 48.67  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   3 GIVLAGGSGTRLYPLTRGVSKQLLP---IYDkpMVFYPISTLMLAGIKDILIITTpednagFK------------RLlgd 67
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLTQ------YKshsldrhisqtwRL--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  68 gsdFGINLEYaIQPSP----------DGLAQAFIIGEEFIGD---DSVCLVLGDNIfYGQSFSSTLknAASRESGA--TV 132
Cdd:PRK00844   77 ---SGLLGNY-ITPVPaqqrlgkrwyLGSADAIYQSLNLIEDedpDYVVVFGADHV-YRMDPRQMV--DFHIESGAgvTV 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1330549855 133 FGYQV--KDPERFGVVEFDEDMKAVSIEEKPEAPKS 166
Cdd:PRK00844  150 AAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPG 185
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-53 2.34e-06

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: 47.15  E-value: 2.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330549855   3 GIVLAGGSGTRLYPLTRGVSKQLLP------IYDkpmvfYPISTLMLAGIKDILIIT 53
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPfggryrLID-----FPLSNMVNSGIRNVGVLT 52
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 3.49e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 47.05  E-value: 3.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330549855   4 IVLAGGSGTRLYPltrGVSKQLLPIYDKPMVFYPISTLMLAG-IKDILIITTPEDNAGFKRLL 65
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-108 4.87e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 46.31  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   3 GIVLAGGSGTRLypltrGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGSDFGINLEYAiqps 82
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWE---- 76

                          90       100
                  ....*....|....*....|....*...
gi 1330549855  83 pDGLAQAFIIGEEFIGD--DSVCLVLGD 108
Cdd:COG2068    77 -EGMSSSLRAGLAALPAdaDAVLVLLGD 103
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-166 7.19e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 47.14  E-value: 7.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLYPLTRGVSKQLLP------IYDkpmvfYPISTLMLAGIKDILIITTpednagFK-----RLLGDGSDF- 71
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYfggkfrIID-----FALSNCINSGIRRIGVLTQ------YKahsliRHIQRGWSFf 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  72 --GINlEY-----AIQPSPD-----GLAQAF-----IIGEEfigDDSVCLVL-GDNIfYGQSFSSTLknAASRESGA--T 131
Cdd:PRK00725   88 reELG-EFvdllpAQQRVDEenwyrGTADAVyqnldIIRRY---DPKYVVILaGDHI-YKMDYSRML--ADHVESGAdcT 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1330549855 132 VFGYQV--KDPERFGVVEFDEDMKAVSIEEKPEAPKS 166
Cdd:PRK00725  161 VACLEVprEEASAFGVMAVDENDRITAFVEKPANPPA 197
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-209 8.27e-06

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: 46.94  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLY---PltrgvsKQLLPIYDKPMVFYPISTLMLAGIKDILIITtpednaGFKR-----LLGDgsdfgINL 75
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVV------GHGAeqvraALAD-----LDV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  76 EYAIQPSPDGLAQAFIIGEEFI-GDDSVCLVLgdnifYG-------QSFSSTLKNAASRESGATVFGYQVKDPERFGVVE 147
Cdd:COG1207    69 EFVLQEEQLGTGHAVQQALPALpGDDGTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTGYGRIV 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330549855 148 FDEDMKAVSI-EEKpEAPKSNYAV----TGLYFYDNRVVEMA-KQVKPSH-RGELEITTLNEMYLNDGL 209
Cdd:COG1207   144 RDEDGRVLRIvEEK-DATEEQRAIreinTGIYAFDAAALREAlPKLSNDNaQGEYYLTDVIAIARADGL 211
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-203 9.52e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 46.68  E-value: 9.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   1 MKGIVLAGGSGTRL---YPltrgvsKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAgfKRLLGDgsdfgiNLEY 77
Cdd:PRK14357    1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAELV--KKLLPE------WVKI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  78 AIQPSPDGLAQAFIIGEEFIGDDSVCLVL-GDNIFYGQSFSSTLKNAASRE-SGATVFGYQVKDPERFGVVEFDEDmKAV 155
Cdd:PRK14357   67 FLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEHNRKgADVTILVADLEDPTGYGRIIRDGG-KYR 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1330549855 156 SIEEKpEAPKSNYAV----TGLYFYDNR-VVEMAKQVKPSH-RGELEITTLNEM 203
Cdd:PRK14357  146 IVEDK-DAPEEEKKIkeinTGIYVFSGDfLLEVLPKIKNENaKGEYYLTDAVNF 198
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-53 9.71e-06

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 46.77  E-value: 9.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330549855   3 GIVLAGGSGTRLYPLTRGVSKQLLPI---Y---DKPMvfypiSTLMLAGIKDILIIT 53
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYrliDIPM-----SNCINSGINKIYVLT 57
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-132 1.34e-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: 44.49  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   3 GIVLAGGSGTRLypltrGVSKQLLPIYDKPMVFYPISTLMLAGiKDILIITTPEDNAGFKRLLGdgsdfginLEYAIQPS 82
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330549855  83 PD-----GLAQAFiigEEFIGDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATV 132
Cdd:pfam12804  67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-53 1.42e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 46.03  E-value: 1.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330549855   1 MK---GIVLAGGSGTRLYPLTRGVSKQLLPIYDK-PMVFYPISTLMLAGIKDILIIT 53
Cdd:PRK02862    1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 1.55e-05

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 45.83  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330549855   1 MKGIVLAGGSGTRLYPLTRGVS-KQLLPIY-DKPMVfypISTLM----LAGIKDILIIT 53
Cdd:COG0836     3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLL---QQTVErlagLVPPENILVVT 58
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-70 2.33e-05

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: 44.44  E-value: 2.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330549855   4 IVLAGGSGTRlypLTRGVSKQLLPIYDKPMVFYPISTLM-LAGIKDILIITTPEDNAGFKRLLGDGSD 70
Cdd:cd02516     4 IILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-165 4.04e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.65  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRLyplTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPEDNAGFKRLLGDGsdfgiNLEYAIQPSP 83
Cdd:PRK14355    7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG-----DVSFALQEEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  84 DGLAQAFIIGEEFI--GDDSVCLVLGDN-IFYGQSFSSTLKNAASRESGATVFGYQVKDPERFGVVEFDEDMKAVSI-EE 159
Cdd:PRK14355   79 LGTGHAVACAAPALdgFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158


                  ....*.
gi 1330549855 160 KPEAPK 165
Cdd:PRK14355  159 KDATPE 164
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-171 1.12e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.23  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855   4 IVLAGGSGTRL-YPLtrgvSKQLLPIYDKPMVFYPISTLMLAGIKDILIITTPednaGFKRLLGDGSDFGINLEYAIQPS 82
Cdd:PRK14353    9 IILAAGEGTRMkSSL----PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP----GAEAVAAAAAKIAPDAEIFVQKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330549855  83 PDGLAQAFIIGEEFI--GDDSVCLVLGDNIFYGQSFSSTLKNAASRESGATVFGYQVKDPERFG-VVEfdEDMKAVSIEE 159
Cdd:PRK14353   81 RLGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrLIV--KGGRLVAIVE 158

                         170
                  ....*....|..
gi 1330549855 160 KPEAPKSNYAVT 171
Cdd:PRK14353  159 EKDASDEERAIT 170
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-34 2.23e-03

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: 38.25  E-value: 2.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1330549855   1 MKGIVLAGGSGTRLypltrGVSKQLLPIYDKPMV 34
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLL 33
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-67 2.44e-03

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


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 39.06  E-value: 2.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330549855   4 IVLAGGSGTRLyplTRGVSKQLLPIYDKPMVFYPISTLMLAG-IKDILIITTPEDNAGFKRLLGD 67
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-54 6.70e-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: 37.20  E-value: 6.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1330549855   3 GIVLAGGSGTRLYPLTRGVSKQLLPIYDKPMVFYPISTLMLAGIKDILIITT 54
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCC 54
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-64 7.50e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 36.70  E-value: 7.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330549855   1 MKGIVLAGGSGTRLypltRGVSKQLLPIYDKPMVFYPISTlmLAGIKDILIITTPEDNAGFKRL 64
Cdd:PRK00317    4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIER--LAPQVDEIVINANRNLARYAAF 61
 
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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