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Conserved domains on  [gi|1792550357|gb|QHD51883|]
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glucose-1-phosphate thymidylyltransferase RfbA [Shewanella algae]

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];
1-287 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 540.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 161 PNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1792550357 241 EHRQSLKVACLEEIALRNGWLSNDKVLDIAEQLSKTGYGQYLLSLIR 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 540.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 161 PNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1792550357 241 EHRQSLKVACLEEIALRNGWLSNDKVLDIAEQLSKTGYGQYLLSLIR 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-287 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: 526.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQH 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  82 KPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 162 NKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1792550357 242 HRQSLKVACLEEIALRNGWLSNDKVLDIAEQLSKTGYGQYLLSLIR 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 7.66e-172

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: 474.76  E-value: 7.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 161 PNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-287 3.19e-137

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 389.03  E-value: 3.19e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQH 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  82 KPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 162 NKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1792550357 242 HRQSLKVACLEEIALRNGWLSNDKVLDIAEQLSKTGYGQYLLSLIR 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 5.81e-98

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: 287.61  E-value: 5.81e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDK-PMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNV-CLVLGDNIFYGQGFSHMLKEIV--NNNIGATVFGYQVRDPHRFGVVEFDENYQVKSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIekAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 158 EEKPNKPR-SNWAVTGLYFYDNQVVDF-AKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1792550357 236 FV 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 540.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 161 PNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1792550357 241 EHRQSLKVACLEEIALRNGWLSNDKVLDIAEQLSKTGYGQYLLSLIR 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-287 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: 526.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQH 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  82 KPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 162 NKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1792550357 242 HRQSLKVACLEEIALRNGWLSNDKVLDIAEQLSKTGYGQYLLSLIR 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 7.66e-172

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: 474.76  E-value: 7.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 161 PNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-287 3.19e-137

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 389.03  E-value: 3.19e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQH 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  82 KPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 162 NKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQFVQTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1792550357 242 HRQSLKVACLEEIALRNGWLSNDKVLDIAEQLSKTGYGQYLLSLIR 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 5.81e-98

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: 287.61  E-value: 5.81e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDK-PMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNV-CLVLGDNIFYGQGFSHMLKEIV--NNNIGATVFGYQVRDPHRFGVVEFDENYQVKSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIekAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 158 EEKPNKPR-SNWAVTGLYFYDNQVVDF-AKKVKPSARGELEITAINQLYLERDALRVQLLGRGFAWLDTGTHDSLIEAGQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1792550357 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 1.62e-69

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 215.13  E-value: 1.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDlDGFKRLLGDGSELGISLSYAVQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGqGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENyQVKSIEEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1792550357 161 PNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEIT-AInQLYLERdALRVQL-LGRGFaWLDTGTHDSLIEAGQFV 237
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITdAI-QWLIDR-GRRVGYsIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 2.05e-60

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: 191.25  E-value: 2.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   3 GIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDlDGFKRLLGDGSELGISLSYAVQHK 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  83 PNGLAEAFIIGESFIDKDNVCLVLGDNIFYGqGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEKPN 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1792550357 163 KPRSNWAVTGLYFYDNQVVDFAKKVKPsaRGELEITAINQLYLERDALRVQLLgrGFAWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-237 3.29e-59

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: 192.62  E-value: 3.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSELGISLSYAVQH 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  82 KPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGqGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1792550357 162 NKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGFaWLDTGTHDSLIEAGQFV 237
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-225 9.08e-46

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: 158.53  E-value: 9.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDlDGFKRLLGDGSELGISLSYAVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  81 HKPNGLAEAFIIGESFIDkDNVCLVLGDNIFYGQGFSHMLKEIvnnniGATVFGYQVRDPHRFGVVEFDENYqVKSIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD-DEFLVLNGDVLLDSDLLERLIRAE-----APAIAVVEVDDPSDYGVVETDGGR-VTGIVEK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1792550357 161 PNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGRGfaWLDTG 225
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 1.19e-42

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: 146.07  E-value: 1.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITT--PEDldgFKRLLGDGSELGISLSYAV 79
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQ---IEEYFGDGSRFGVRITYVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  80 QHKPNGLAEAFIIGESFIDKDNVCLVLGDnIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIEE 159
Cdd:COG1208    78 EGEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1792550357 160 KPNKPRSNWAVTGLYFYDNQVVDFakkVKPSARGELEiTAINQLyLERDALRVQLLgRGFaWLDTGTHDSLIEA 233
Cdd:COG1208   157 KPEEPPSNLINAGIYVLEPEIFDY---IPEGEPFDLE-DLLPRL-IAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-233 7.46e-34

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: 124.18  E-value: 7.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTP-----ED-------LDGFKRLLGDG 68
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiEDhfdrsyeLEETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  69 SEL--------GISLSYAVQHKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQ--GFSHMLKeiVNNNIGATVFGYQVR 138
Cdd:cd02541    81 DLLeevriisdLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepCLKQLIE--AYEKTGASVIAVEEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 139 DP---HRFGVVEF----DENYQVKSIEEKPnKPR---SNWAVTGLYFYDNQVVDFAKKVKPSARGELEIT-AINQLYLER 207
Cdd:cd02541   159 PPedvSKYGIVKGekidGDVFKVKGLVEKP-KPEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTdAIAKLLEEE 237

                         250       260
                  ....*....|....*....|....*.
gi 1792550357 208 DALRVQLLGRgfaWLDTGTHDSLIEA 233
Cdd:cd02541   238 PVYAYVFEGK---RYDCGNKLGYLKA 260
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-226 7.92e-24

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: 96.51  E-value: 7.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITT--PEDLDGFKRLLGDgsELGISLSYA 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEYEK--KLGIKITFS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  79 VQHKPNGLAEAFIIGESFIDKDNVC-LVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDEN-YQVKS 156
Cdd:cd06425    79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIER 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1792550357 157 IEEKPNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGEL--EITAINQLYlerdALRVQllgrGFaWLDTGT 226
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIfpKMASEGQLY----AYELP----GF-WMDIGQ 221
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 1.62e-23

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 97.03  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYplSV--LMLAGINDILIITTP-----ED-------LDGFKRLLGD 67
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiEDhfdrsyeLEATLEAKGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  68 GSEL--------GISLSYAVQHKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQgfSHMLKEIVN--NNIGATVFGYQ- 136
Cdd:COG1210    83 EELLeevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQMIEvyEETGGSVIAVQe 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 137 VR--DPHRFGVVEFDEN----YQVKSIEEKPNK---PrSNWAVTGLYFYDNQVVDFAKKVKPSARGELEIT-AINQLYLE 206
Cdd:COG1210   161 VPpeEVSKYGIVDGEEIeggvYRVTGLVEKPAPeeaP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTdAIAALAKE 239

                         250       260
                  ....*....|....*....|....*..
gi 1792550357 207 RDALRVQLLGRgfaWLDTGTHDSLIEA 233
Cdd:COG1210   240 EPVYAYEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-182 4.48e-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: 83.33  E-value: 4.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITT--PEDLdgfKRLLGDGSELGISLSYAVQH 81
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNylAEMI---EDYFGDGSKFGVNISYVRED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  82 KPNGLAEAFiigeSFIDK--DNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATV----FGYQVrdPhrFGVVEFDENyQVK 155
Cdd:cd06426    79 KPLGTAGAL----SLLPEkpTDPFLVMNGDILTNLNYEHLLDFHKENNADATVcvreYEVQV--P--YGVVETEGG-RIT 149

                         170       180
                  ....*....|....*....|....*...
gi 1792550357 156 SIEEKPNKprsNWAV-TGLYFYDNQVVD 182
Cdd:cd06426   150 SIEEKPTH---SFLVnAGIYVLEPEVLD 174
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 1.26e-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: 82.22  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITtpedldGFKR-----LLGDGSELGISLSYA 78
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSV------GYLAeqieeYFGDGYRGGIRIYYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  79 VQHKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGqGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSIE 158
Cdd:cd06915    76 IEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 159 EKPNKPRSNWAVTGLYFYDNQVVDFAKKVKPSargeleitainqlyLERDALRVQLLG---RGFA----WLDTGTHDSLI 231
Cdd:cd06915   155 EKGPGAAPGLINGGVYLLRKEILAEIPADAFS--------------LEADVLPALVKRgrlYGFEvdgyFIDIGIPEDYA 220


                  ..
gi 1792550357 232 EA 233
Cdd:cd06915   221 RA 222
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-177 1.15e-17

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 82.05  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   3 GIVLAGGAGTRLYPLTRGVSKqllpvydkPMIYY---------PLSVLMLAGINDILIITtpedldGFK-----RLLGDG 68
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT------QYKshslnDHIGSG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  69 SE--LGISLSY-----AVQHKPN-----GLAEAFIIGESFIDK---DNVCLVLGDNIfYGQGFSHMLKEIVNNNIGATVF 133
Cdd:COG0448    70 KPwdLDRKRGGvfilpPYQQREGedwyqGTADAVYQNLDFIERsdpDYVLILSGDHI-YKMDYRQMLDFHIESGADITVA 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1792550357 134 GYQV--RDPHRFGVVEFDENYQVKSIEEKPNKPRSNWAVTGLYFYD 177
Cdd:COG0448   149 CIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-57 4.48e-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: 77.70  E-value: 4.48e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPED 57
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-57 5.14e-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: 66.51  E-value: 5.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPED 57
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHS 57
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-210 7.22e-12

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 64.54  E-value: 7.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIIT------------TPEDLDGF------KR 63
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEAMlekrvkRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  64 LLGDGSEL---GISLSYAVQHKPNGLAEAFIIGESFIDKDNVCLVLGDNI-------------------FYGQGFSHMLK 121
Cdd:PRK13389   90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeyesdlsqdnlaemirrFDETGHSQIMV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 122 EIVNNnigatVFGYQVRDPHRFGVVEFDENYQVKSIEE-KPNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAI 200
Cdd:PRK13389  170 EPVAD-----VTAYGVVDCKGVELAPGESVPMVGVVEKpKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244

                         250
                  ....*....|
gi 1792550357 201 NQLYLERDAL 210
Cdd:PRK13389  245 IDMLIEKETV 254
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-233 7.74e-12

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 64.89  E-value: 7.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDK-PMIYYPLSVLMLAGINDILIIT--------------TPEDLDGFkrll 65
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTqyqplelnnhigigSPWDLDRI---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  66 gDGselGISL--SYAVQHKPN---GLAEAFIIGESFIDKDNVCLVL---GDNIfYGQGFSHMLKEIVNNNIGATVFGYQV 137
Cdd:PRK05293   80 -NG---GVTIlpPYSESEGGKwykGTAHAIYQNIDYIDQYDPEYVLilsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 138 --RDPHRFGVVEFDENYQVKSIEEKPNKPRSNWAVTGLYFY---------------DNQVVDFAKKVKPSargeleitai 200
Cdd:PRK05293  155 pwEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL---------- 224

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1792550357 201 nqlYLERDalrvqllGRGFA------WLDTGTHDSLIEA 233
Cdd:PRK05293  225 ---YLEEG-------EKLYAypfkgyWKDVGTIESLWEA 253
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-223 1.05e-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: 63.02  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITtpedldGFKR-----LLGDgsELGISLSYA 78
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT------GYKKeqieeLLKK--YPNIKFVYN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  79 VQHKPNGLAEAFIIGESFIDKDnvCLVL-GDNIFYGQgfshMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSI 157
Cdd:cd02523    74 PDYAETNNIYSLYLARDFLDED--FLLLeGDVVFDPS----ILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLG 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1792550357 158 EEKPNKPRSN--WAVTGLYFYDNQ----VVDFAKKVKPSARGELEITAINQLYLERDALRVQLLGrGFAWLD 223
Cdd:cd02523   148 IISKAKNLEEiqGEYVGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 1.09e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 60.25  E-value: 1.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIIT 53
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-233 3.06e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 57.16  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLYPLTRGVSKQLLPVYDK-PMIYYPLSVLMLAGINDILIITTpedldgFK-----RLLGDG-----SELG 72
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQ------YKahsliRHIQRGwsffrEELG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  73 --ISLSYAVQ--HKPN---GLAEAF-----IIGESfiDKDNVCLVLGDNIfYGQGFSHMLKEIVNNNIGATVFGYQVR-- 138
Cdd:PRK00725   93 efVDLLPAQQrvDEENwyrGTADAVyqnldIIRRY--DPKYVVILAGDHI-YKMDYSRMLADHVESGADCTVACLEVPre 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 139 DPHRFGVVEFDENYQVKSIEEKP-------NKPRSNWAVTGLYFYDNQVV---------------DFAKKVKPSARGELE 196
Cdd:PRK00725  170 EASAFGVMAVDENDRITAFVEKPanppampGDPDKSLASMGIYVFNADYLyelleedaedpnsshDFGKDIIPKIVEEGK 249

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1792550357 197 ITAinqlYLERDALRVQLLGRGFAWLDTGTHDSLIEA 233
Cdd:PRK00725  250 VYA----HPFSDSCVRSDPEEEPYWRDVGTLDAYWQA 282
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-194 3.64e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 57.15  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRL---YPltrgvsKQLLPVYDKPMIYYPLSVLMLAGINDILII--TTPEDLdgfKRLLGDGSElgislsYA 78
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVvgHGAEEV---KEVLGDRSE------FA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  79 VQHKPNGLAEAFIIGESFI-DKDNVCLVL-GDN-IFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVK 155
Cdd:PRK14354   71 LQEEQLGTGHAVMQAEEFLaDKEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVE 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1792550357 156 SI-EEK---PNKPRSNWAVTGLYFYDNQVVdFA--KKVKP-SARGE 194
Cdd:PRK14354  151 KIvEQKdatEEEKQIKEINTGTYCFDNKAL-FEalKKISNdNAQGE 195
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-203 6.41e-09

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 55.66  E-value: 6.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIIT------------TPEDLDGF------K 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  63 RLLGDGSEL---GISLSYAVQHKPNGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHM---LKEIV---NNNIGATVF 133
Cdd:PRK10122   84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLrynLAAMIarfNETGRSQVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 134 GYQVR-DPHRFGVVE----FDENYQVKSIE---EKPNKPR---SNWAVTGLYFYDNQVVDFAKKVKPSARGELEIT-AIN 201
Cdd:PRK10122  164 AKRMPgDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTdAIA 243


                  ..
gi 1792550357 202 QL 203
Cdd:PRK10122  244 EL 245
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-51 3.80e-08

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: 52.57  E-value: 3.80e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1792550357   2 KGIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILI 51
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV 50
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-132 4.76e-08

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 52.16  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   3 GIVLAGGAGTRLYPLTRGVSKQLLPV---YDkpMIYYPLSVLMLAGINDILIIT------TPEDLDGFKRLLGDGSELGI 73
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLTqyksrsLNDHLGSGKEWDLDRKNGGL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1792550357  74 SLSYAVQHKPN----GLAEAFIIGESFI---DKDNVCLVLGDNIfYGQGFSHMLKEIVNNNIGATV 132
Cdd:cd02508    79 FILPPQQRKGGdwyrGTADAIYQNLDYIersDPEYVLILSGDHI-YNMDYREMLDFHIESGADITV 143
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-219 9.38e-08

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: 9.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   3 GIVLAGGA--GTRLYPLTRGVSKQLLPVYDKPMIYYPLSVL-MLAGINDILIITTPEDLDgFKRLLGDGS-ELGISLSYA 78
Cdd:cd06428     1 AVILVGGPqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQqEFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  79 VQHKPNGLAEAF-----IIGES-----FIDKDNVC--LVLGDNI-FY---GQGFSHMLKEIvnNNIGATVFGYQVRDPHR 142
Cdd:cd06428    80 QEYKPLGTAGGLyhfrdQILAGnpsafFVLNADVCcdFPLQELLeFHkkhGASGTILGTEA--SREQASNYGCIVEDPST 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357 143 FGVVEFdenyqvksiEEKPNKPRSNWAVTGLYFYDNQVVDFAKKVKPSARGELEITAINQ-------LYLERDALrVQLL 215
Cdd:cd06428   158 GEVLHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNregraevIRLEQDVL-TPLA 227


                  ....
gi 1792550357 216 GRGF 219
Cdd:cd06428   228 GSGK 231
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-166 1.31e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 52.14  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   3 GIVLAGGAGTRLYPLTRGVSKQLLP---VYDkpMIYYPLSVLMLAGINDILIITT--PEDLDgfkRLLGDGSEL-GISLS 76
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLTQykSHSLD---RHISQTWRLsGLLGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  77 Y-----AVQHK-PN---GLAEAFIIGESFIDKDN---VCLVLGDNIfYGQGFSHMLKEIVNNNIGATVFGyqVRDP---- 140
Cdd:PRK00844   83 YitpvpAQQRLgKRwylGSADAIYQSLNLIEDEDpdyVVVFGADHV-YRMDPRQMVDFHIESGAGVTVAA--IRVPreea 159

                         170       180
                  ....*....|....*....|....*.
gi 1792550357 141 HRFGVVEFDENYQVKSIEEKPNKPRS 166
Cdd:PRK00844  160 SAFGVIEVDPDGRIRGFLEKPADPPG 185
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-200 1.42e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 52.07  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   1 MKGIVLAGGAGTRL---YPltrgvsKQLLPVYDKPMIYYplsVLMLAG-INDILIITTPEDLDGFKRLLGDGSELgisls 76
Cdd:PRK14357    1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINW---VIDTAKkVAQKVGVVLGHEAELVKKLLPEWVKI----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  77 yAVQHKPNGLAEAFIIGESFIDKDNVCLVL-GDNIFYGQG-FSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENyQV 154
Cdd:PRK14357   67 -FLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENtLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGG-KY 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1792550357 155 KSIEEK--PNKPRSNWAV-TGLYFYD-NQVVDFAKKVKP-SARGELEITAI 200
Cdd:PRK14357  145 RIVEDKdaPEEEKKIKEInTGIYVFSgDFLLEVLPKIKNeNAKGEYYLTDA 195
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 1.70e-07

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 50.90  E-value: 1.70e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1792550357   4 IVLAGGAGTRLyplTRGVSKQLLPVYDKPMIYYPLSVLMLAG-INDILIITTPEDLDGFKRLLGD 67
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-160 7.21e-07

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: 49.05  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLY-PLtrgvSKQLLPVYDKPMIYYPLSVLMLAGINDILIIttpedldgfkrlLGDGSEL------GISLS 76
Cdd:cd02540     2 VILAAGKGTRMKsDL----PKVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEQvkkalaNPNVE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  77 YAVQHKPNGLAEAFIIGESFIDKDN-VCLVLgdnifYG-------QGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEF 148
Cdd:cd02540    66 FVLQEEQLGTGHAVKQALPALKDFEgDVLVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIR 140

                         170
                  ....*....|...
gi 1792550357 149 DENYQVKSI-EEK 160
Cdd:cd02540   141 DGNGKVLRIvEEK 153
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-160 8.84e-07

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 49.64  E-value: 8.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLY---PltrgvsKQLLPVYDKPMIYYPLSVLMLAGINDILIITtpedldgfkrllGDGSEL------GIS 74
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVV------------GHGAEQvraalaDLD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  75 LSYAVQHKPNGLAEAFIIGESFI-DKDNVCLVLgdnifYG-------QGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVV 146
Cdd:COG1207    68 VEFVLQEEQLGTGHAVQQALPALpGDDGTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTGYGRI 142

                         170
                  ....*....|....*
gi 1792550357 147 EFDENYQVKSI-EEK 160
Cdd:COG1207   143 VRDEDGRVLRIvEEK 157
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-53 9.56e-07

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 49.47  E-value: 9.56e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1792550357   3 GIVLAGGAGTRLYPLTRGVSKQLLPV---YDkpMIYYPLSVLMLAGINDILIIT 53
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLT 57
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 1.04e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 48.59  E-value: 1.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1792550357   4 IVLAGGAGTRLYPltrGVSKQLLPVYDKPMIYYPLSVLMLAG-INDILIITTPEDLDGFKRLL 65
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-53 1.06e-06

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: 49.11  E-value: 1.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1792550357   1 MKGIVLAGGAGTRLYPLTR-GVSKQLLPVY-DKPMIYYPLS-VLMLAGINDILIIT 53
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVT 56
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-75 3.93e-06

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 46.75  E-value: 3.93e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1792550357   4 IVLAGGAGTRLyplTRGVSKQLLPVYDKPMIYYPLSVLM-LAGINDILIITTPEDLDGFKRLLGDGSELGISL 75
Cdd:cd02516     4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-53 4.66e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 47.57  E-value: 4.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1792550357   3 GIVLAGGAGTRLYPLTRGVSKQLLPVYDK-PMIYYPLSVLMLAGINDILIIT 53
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-55 1.35e-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: 44.88  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1792550357   6 LAGGAGTRLypltRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTP 55
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-204 1.46e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 46.13  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLyplTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITtpedldgfkrllGDGSE------LGISLSY 77
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVT------------GHGAEqveaalQGSGVAF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  78 AVQHKPNGLAEAFIIG-ESFIDKDNVCLVL-GDN-IFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQV 154
Cdd:PRK14358   76 ARQEQQLGTGDAFLSGaSALTEGDADILVLyGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1792550357 155 KSIEEKPNKPRSNWAV----TGLYFYDNQVVDFAKKV-KPSARGELEITAINQLY 204
Cdd:PRK14358  156 ERIVEQKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLY 210
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-66 1.52e-05

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 44.11  E-value: 1.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1792550357   3 GIVLAGGAGTRLypltrGVSKQLLPVYDKPMIYYPLSVLMLAGiNDILIITTPEDLDGFKRLLG 66
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG 58
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-53 2.26e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 44.38  E-value: 2.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1792550357   3 GIVLAGGAGTRLypltrGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIIT 53
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVL 51
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 2.65e-05

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 45.06  E-value: 2.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1792550357   1 MKGIVLAGGAGTRLYPLTRGVS-KQLLPVY-DKPMIYypLSVLMLAGI---NDILIIT 53
Cdd:COG0836     3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ--QTVERLAGLvppENILVVT 58
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-57 3.55e-05

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 43.64  E-value: 3.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1792550357   1 MKGIVLAGGAGTRLypltrGVSKQLLPVYDKPMIYYPLSVlmLAGINDILIITTPED 57
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP 54
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-92 4.14e-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: 43.32  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   3 GIVLAGGAGTRLypltrGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGSE----------LG 72
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVvvinpdweegMS 77

                          90       100
                  ....*....|....*....|
gi 1792550357  73 ISLSYAVQHKPNGlAEAFII 92
Cdd:cd04182    78 SSLAAGLEALPAD-ADAVLI 96
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-214 5.62e-05

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 43.40  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYplSVLMLAGIND--ILIITTPEDLDGFKrlLGDGSELGISLSYAVQH 81
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrFIFICRDEHNTKFH--LDESLKLLAPNATVVEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  82 KP--NGLAEAFIIGESFIDKDNVCLVLGDNIFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHrFGVVEFDENYQVKSIEE 159
Cdd:cd04183    78 DGetLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPR-WSYVKLDENGRVIETAE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1792550357 160 KpnKPRSNWAVTGLYFYDN--QVVDFAKKV-KPSAR--GELEIT-AINqlYLERDALRVQL 214
Cdd:cd04183   157 K--EPISDLATAGLYYFKSgsLFVEAAKKMiRKDDSvnGEFYISpLYN--ELILDGKKVGI 213
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-160 1.23e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357   4 IVLAGGAGTRLyplTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITTPEDLDGFKRLLGDGselgiSLSYAVQHKP 83
Cdd:PRK14355    7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG-----DVSFALQEEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1792550357  84 NGLAEAFIIGESFID--KDNVCLVLGDN-IFYGQGFSHMLKEIVNNNIGATVFGYQVRDPHRFGVVEFDENYQVKSI-EE 159
Cdd:PRK14355   79 LGTGHAVACAAPALDgfSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158


                  .
gi 1792550357 160 K 160
Cdd:PRK14355  159 K 159
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-54 4.89e-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: 37.59  E-value: 4.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1792550357   3 GIVLAGGAGTRLYPLTRGVSKQLLPVYDKPMIYYPLSVLMLAGINDILIITT 54
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCC 54
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-64 7.91e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 36.70  E-value: 7.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1792550357   1 MKGIVLAGGAGTRLypltRGVSKQLLPVYDKPMIYYplsVLM-LAGINDILIITTPEDLDGFKRL 64
Cdd:PRK00317    4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQH---VIErLAPQVDEIVINANRNLARYAAF 61
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-64 8.44e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 36.40  E-value: 8.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1792550357   1 MKGIVLAGGAGTRLypltrGVSKQLLPVYDKPMIYYPLSvlMLAGINDILIITTPEDLDGFKRL 64
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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