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Conserved domains on  [gi|489280071|ref|WP_003187717|]
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MULTISPECIES: glucose-1-phosphate thymidylyltransferase RfbA [Pseudomonas]

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];
2-289 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 559.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 PSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEK 161
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 162 PAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTI 241
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489280071 242 EHRQGLKVACLEEIAYENGWIDRDYLLERAKYFGKTGYGQYLYSLAGE 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
2-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 559.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 PSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEK 161
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 162 PAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTI 241
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489280071 242 EHRQGLKVACLEEIAYENGWIDRDYLLERAKYFGKTGYGQYLYSLAGE 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
3-287 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: 541.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQP 82
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   83 SPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEKP 162
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  163 AKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTIE 242
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 489280071  243 HRQGLKVACLEEIAYENGWIDRDYLLERAKYFGKTGYGQYLYSLA 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
2-241 2.08e-173

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: 478.61  E-value: 2.08e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 PSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEK 161
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 162 PAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTI 241
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
3-286 4.08e-138

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 391.34  E-value: 4.08e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQP 82
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  83 SPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEKP 162
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 163 AKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTIE 242
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489280071 243 HRQGLKVACLEEIAYENGWIDRDYLLERAKYFGKTGYGQYLYSL 286
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
3-235 1.19e-97

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 286.84  E-value: 1.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDK-PMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   82 PSPDGLAQAFIIGEEFIGDDAV-CLILGDNIFHGQHFGDQLRTAAERSS--GATVFGYWVKDPERFGVIDFDKEGRALSI 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489280071  159 EEKPAKPKSP-YAVTGLYFYDNDVI-KIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEAS 235
Cdd:pfam00483 161 VEKPKLPKASnYASMGIYIFNSGVLdFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEAN 239
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
2-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 559.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 PSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEK 161
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 162 PAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTI 241
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489280071 242 EHRQGLKVACLEEIAYENGWIDRDYLLERAKYFGKTGYGQYLYSLAGE 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
3-287 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: 541.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQP 82
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   83 SPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEKP 162
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  163 AKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTIE 242
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 489280071  243 HRQGLKVACLEEIAYENGWIDRDYLLERAKYFGKTGYGQYLYSLA 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
2-241 2.08e-173

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: 478.61  E-value: 2.08e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 PSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEK 161
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 162 PAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTI 241
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
3-286 4.08e-138

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 391.34  E-value: 4.08e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQP 82
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  83 SPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEKP 162
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 163 AKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEASTYVQTIE 242
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489280071 243 HRQGLKVACLEEIAYENGWIDRDYLLERAKYFGKTGYGQYLYSL 286
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
3-235 1.19e-97

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 286.84  E-value: 1.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDK-PMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   82 PSPDGLAQAFIIGEEFIGDDAV-CLILGDNIFHGQHFGDQLRTAAERSS--GATVFGYWVKDPERFGVIDFDKEGRALSI 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489280071  159 EEKPAKPKSP-YAVTGLYFYDNDVI-KIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFAWLDTGTHDSLLEAS 235
Cdd:pfam00483 161 VEKPKLPKASnYASMGIYIFNSGVLdFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEAN 239
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
2-238 4.82e-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: 213.97  E-value: 4.82e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVI--STPVDLPQYrnlLGDGSQFGVRFTYA 79
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgPTGEEIKEA---LGDGSRFGVRITYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  80 EQPSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQhFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDkEGRALSIE 159
Cdd:cd04189   78 LQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG-ISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 160 EKPAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGdLHVE-RFGRGFaWLDTGTHDSLLEASTYV 238
Cdd:cd04189  156 EKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRG-RRVGySIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
4-226 1.82e-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: 1.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   4 GIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPvDLPQYRNLLGDGSQFGVRFTYAEQPS 83
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGY-LGEQIEEYFGDGSKFGVNIEYVVQEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  84 PDGLAQAFIIGEEFIGDDAVCLILGDNIFHGqHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEKPA 163
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489280071 164 KPKSPYAVTGLYFYDNDVIKIAKAVKpsPRGELEITDVNNAYLQRGDLHVERFgrGFAWLDTG 226
Cdd:cd04181  159 LPESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
3-234 7.49e-57

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


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 186.45  E-value: 7.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAEQP 82
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   83 SPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGqHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEKP 162
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489280071  163 AKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGFaWLDTGTHDSLLEA 234
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
2-238 1.06e-47

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: 163.53  E-value: 1.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDlPQYRNLLGDGSQFGVRFTYAEQ 81
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   82 PSPDGLAQAFIIGEEFIgDDAVCLILGDNIFHGQHFGDQLRTaaersSGATVFGYWVKDPERFGVIDFDkEGRALSIEEK 161
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLIRA-----EAPAIAVVEVDDPSDYGVVETD-GGRVTGIVEK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489280071  162 PAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVERFGRGfaWLDTGTHDSLLEASTYV 238
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
3-234 1.93e-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: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDIlVISTPvDLP-QYRNLLGDGSQFGVRFTYAEQ 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVG-YLAeQIEEYFGDGSRFGVRITYVDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 PSP----DGLAQAfiigEEFIGDDAVCLILGDNIFhGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALS 157
Cdd:COG1208   79 GEPlgtgGALKRA----LPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489280071 158 IEEKPAKPKSPYAVTGLYFYDNDVIKIAkavkpsPRGE-LEITDVNNAYLQRGDLHVERFgRGFaWLDTGTHDSLLEA 234
Cdd:COG1208  154 FVEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
2-235 1.44e-29

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: 112.63  E-value: 1.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTP------------------------V 57
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdrsyeleetlekkgkT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  58 DLPQYRNLLGDGsqfgVRFTYAEQPSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFG-DQLRTAAERSsGATVFGY 136
Cdd:cd02541   81 DLLEEVRIISDL----ANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPClKQLIEAYEKT-GASVIAV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 137 WVKDPE---RFGVID-FDKEGRALSIE---EKPaKPK---SPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYL 206
Cdd:cd02541  156 EEVPPEdvsKYGIVKgEKIDGDVFKVKglvEKP-KPEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLL 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 489280071 207 QRGDLHVERF-GRgfaWLDTGTHDSLLEAS 235
Cdd:cd02541  235 EEEPVYAYVFeGK---RYDCGNKLGYLKAT 261
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
5-234 2.12e-22

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


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 92.62  E-value: 2.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDIlVISTPVDLPQYRNLLGDGSQFGVRFTYAEQPSP 84
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  85 DGLAQAFIIGEEFIGDDAVCLILGDNIFHGQhFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEGRALSIEEKPAK 164
Cdd:cd06915   81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489280071 165 PKSPYAVTGLYFYDNDVIKIAKAVKPSprgeLEiTDVNNAYLQRGDL----HVERFgrgfawLDTGTHDSLLEA 234
Cdd:cd06915  160 AAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRLygfeVDGYF------IDIGIPEDYARA 222
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
5-234 2.75e-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: 89.49  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDIlVISTPVDLPQYRNLLGDGSQFGVRFTYAEQPSP 84
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  85 DGLAQAFIIGEEFIgDDAVCLILGDnIFHGQHFGDQLRTAAERSSGATVFG--YWVKDPerFGVIDFDkEGRALSIEEkp 162
Cdd:cd06426   81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETE-GGRITSIEE-- 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489280071 163 aKPKSPYAV-TGLYFYDNDVIKIAkavkpsPRGE-LEITDVNNAYLQRGDlHVERFG-RGFaWLDTGTHDSLLEA 234
Cdd:cd06426  154 -KPTHSFLVnAGIYVLEPEVLDLI------PKNEfFDMPDLIEKLIKEGK-KVGVFPiHEY-WLDIGRPEDYEKA 219
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-234 4.78e-20

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 87.40  E-value: 4.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTP------------VDLpqYRNLLGDG- 69
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfdrsYEL--EATLEAKGk 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  70 ---------SQFGVRFTYAEQPSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHFG-DQLRTAAERsSGATVFGywVK 139
Cdd:COG1210   83 eelleevrsISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPClKQMIEVYEE-TGGSVIA--VQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 140 --DPE---RFGVIDFDK-EGRALSIE---EKPAKPKSP--YAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNNAYLQR 208
Cdd:COG1210  160 evPPEevsKYGIVDGEEiEGGVYRVTglvEKPAPEEAPsnLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239
                        250       260
                 ....*....|....*....|....*..
gi 489280071 209 GDLHVERF-GRgfaWLDTGTHDSLLEA 234
Cdd:COG1210  240 EPVYAYEFeGK---RYDCGDKLGYLKA 263
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
2-182 2.02e-18

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: 81.87  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKD-ILVIS-TPVDLPQYRNLLGDgsQFGVRFTYA 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  80 EQPSPDGLAQAFIIGEEFIGDDAVCLIL--GDNI----------FHGQHFGDqlrtaaerssgATVFGYWVKDPERFGVI 147
Cdd:cd06425   79 IETEPLGTAGPLALARDLLGDDDEPFFVlnSDVIcdfplaelldFHKKHGAE-----------GTILVTKVEDPSKYGVV 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489280071 148 DFDKE-GRALSIEEKPAKPKSPYAVTGLYFYDNDVI 182
Cdd:cd06425  148 VHDENtGRIERFVEKPKVFVGNKINAGIYILNPSVL 183
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-234 4.04e-17

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: 78.00  E-value: 4.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDIlVISTPvDLP-QYRNLLGDgSQFGVRFTYAEQ 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTH-HLAdQIEAHLGD-SRFGLRITISDE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 P-----SPDGLAQAfiigEEFIGDDAVCLILGDNIFHGqHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDF--DKEGR 154
Cdd:cd06422   78 PdelleTGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDADGR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 155 alsIEEKPAKPKSPYAVTGLYFYDNDVIKIAkavkpsPRGELEITDVNNAYLQRGDLHVERFgRGFaWLDTGTHDSLLEA 234
Cdd:cd06422  153 ---LRRGGGGAVAPFTFTGIQILSPELFAGI------PPGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
2-58 7.05e-14

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: 69.22  E-value: 7.05e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVD 58
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
2-200 7.80e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 67.22  E-value: 7.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVIS------------TPVDLPQY------R 63
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  64 NLLGDGSQF---GVRFTYAEQPSPDGLAQAFIIGEEFIGDDAVCLILGDNIFHGQHfGDQLR--TAA-----ERSSGATV 133
Cdd:PRK10122  84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAS-ADPLRynLAAmiarfNETGRSQV 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489280071 134 FGYWVK-DPERFGVID----FDKEGRALSIE---EKPAKPK---SPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITD 200
Cdd:PRK10122 163 LAKRMPgDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
2-53 3.13e-12

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 64.58  E-value: 3.13e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVI 53
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
4-235 8.41e-12

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 64.71  E-value: 8.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   4 GIVLAGGSGTRLHPITLGVSKqllpvydkPMIYY---------PISVLMLAGIKDILVistpvdLPQYRNL-----LGDG 69
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKSHslndhIGSG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  70 SQF-------GVRFTYAEQPSPD-----GLAQAFIIGEEFIGD---DAVcLIL-GDNIFHgQHFGDQLRTAAERSSGATV 133
Cdd:COG0448   70 KPWdldrkrgGVFILPPYQQREGedwyqGTADAVYQNLDFIERsdpDYV-LILsGDHIYK-MDYRQMLDFHIESGADITV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 134 FGYWV--KDPERFGVIDFDKEGRALSIEEKPAKPKSPYAVTGLYFYDNDVIKiaKAVKPS-PRGELE-ITDVNNAYLQRG 209
Cdd:COG0448  148 ACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVLI--ELLEEDaPNSSHDfGKDIIPRLLDRG 225
                        250       260
                 ....*....|....*....|....*.
gi 489280071 210 DLHVERFgRGFaWLDTGTHDSLLEAS 235
Cdd:COG0448  226 KVYAYEF-DGY-WRDVGTIDSYYEAN 249
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
5-215 3.97e-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: 61.48  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVI----STpvdlpQYRNLLGDgsQFGVRFTYAE 80
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVtgykKE-----QIEELLKK--YPNIKFVYNP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  81 QPSPDGLAQAFIIGEEFIGDDavCLIL-GDNIFHGQHFgDQLRtAAERSSGATVFGYWVKDPERFGVIDFDKEGRaLSIE 159
Cdd:cd02523   75 DYAETNNIYSLYLARDFLDED--FLLLeGDVVFDPSIL-ERLL-SSPADNAILVDKKTKEWEDEYVKDLDDAGVL-LGII 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489280071 160 EKPAKPKSPYAVT-GLYFYDND----VIKIAKAVKPSPRGELEITDVNNAYLQRGDLHVER 215
Cdd:cd02523  150 SKAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKD 210
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-200 1.42e-10

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 60.69  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVIS------------TPVDLPQY------RN 64
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEAMlekrvkRQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  65 LLGDGSQF---GVRFTYAEQPSPDGLAQAFIIGEEFIGDDAVCLILGDNI---FHGQHFGDQLRTAAER--SSGAT-VFG 135
Cdd:PRK13389  90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeYESDLSQDNLAEMIRRfdETGHSqIMV 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489280071 136 YWVKDPERFGVIDFD----KEGRA---LSIEEKPAKPKSP--YAVTGLYFYDNDVIKIAKAVKPSPRGELEITD 200
Cdd:PRK13389 170 EPVADVTAYGVVDCKgvelAPGESvpmVGVVEKPKADVAPsnLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
3-53 7.75e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 54.86  E-value: 7.75e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489280071   3 KGIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVI 53
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
5-209 2.97e-08

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 54.21  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTRLHPitlGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVIsTPVDLPQYRNLLgdgSQFGVRFtyAEQPSP 84
Cdd:PRK14358  11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVV-TGHGAEQVEAAL---QGSGVAF--ARQEQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  85 DGLAQAFIIGEEFIGD-DAVCLILgdnifhgqhFGDQ--LRTAA---------ERSSGATVFGYWVKDPERFGVIDFDKE 152
Cdd:PRK14358  82 LGTGDAFLSGASALTEgDADILVL---------YGDTplLRPDTlralvadhrAQGSAMTILTGELPDATGYGRIVRGAD 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489280071 153 GRALSIEEKPAKPKSPYAV----TGLYFYDNDVIKIAKAV-KPSPRGELEITDVNNAYLQRG 209
Cdd:PRK14358 153 GAVERIVEQKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
5-68 3.35e-08

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: 52.82  E-value: 3.35e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489280071   5 IVLAGGSGTRLHpitLGVSKQLLPVYDKPMIYYPISVLMLAG-IKDILVISTPVDLPQYRNLLGD 68
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
4-133 2.29e-07

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: 49.50  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    4 GIVLAGGSGTRlhpitLGVSKQLLPVYDKPMIYYpiSVLMLAGIKDILVISTPvdlpqYRNLLGDGSQFGVRFTYAEQPS 83
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLER--VLERLRPAGDEVVVVAN-----DEEVLAALAGLGVPVVPDPDPG 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489280071   84 P---DGLAQAFiigEEFIGDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATV 133
Cdd:pfam12804  69 QgplAGLLAAL---RAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-109 2.32e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 50.16  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   1 MMK--GIVLAGGSGTRLhpitlGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVIsTPVDLPQYRNLLgdgSQFGVRFTY 78
Cdd:COG2068    1 MSKvaAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LGADAEEVAAAL---AGLGVRVVV 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489280071  79 AEQPSpDGLAQAFIIGEEFIGD--DAVCLILGD 109
Cdd:COG2068   72 NPDWE-EGMSSSLRAGLAALPAdaDAVLVLLGD 103
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
4-203 5.30e-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: 49.56  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   4 GIVLAGG--SGTRLHPITLGVSKQLLPVYDKPMIYYPISVL-MLAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFTYAE 80
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  81 QPSPDGLAQAF-----IIGEEfiGDDAVCLILGDNI----------FHGQHFGDQ--LRTAAERSSgATVFGYWVKDPer 143
Cdd:cd06428   81 EYKPLGTAGGLyhfrdQILAG--NPSAFFVLNADVCcdfplqelleFHKKHGASGtiLGTEASREQ-ASNYGCIVEDP-- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 144 fgvidfdKEGRALSIEEKPAKPKSPYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDVNN 203
Cdd:cd06428  156 -------STGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNN 208
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
5-201 7.17e-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: 7.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTR--------LHPItLGvskqllpvydKPMIYYPISVLMLAGIKDILVIsTPVDLPQYRNLLGDGSqfgvrF 76
Cdd:cd02540    2 VILAAGKGTRmksdlpkvLHPL-AG----------KPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALANPN-----V 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  77 TYAEQPSPDGLAQAFIIGEEFIGDDA-VCLILgdnifhgqhFGDQ-----------LRTAAERSSGATVFGYWVKDPERF 144
Cdd:cd02540   65 EFVLQEEQLGTGHAVKQALPALKDFEgDVLVL---------YGDVplitpetlqrlLEAHREAGADVTVLTAELEDPTGY 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489280071 145 GVIDFDKEGRALSI-EEKPAKP--KSPYAV-TGLYFYDNDVIKIA-KAVKPSP-RGELEITDV 201
Cdd:cd02540  136 GRIIRDGNGKVLRIvEEKDATEeeKAIREVnAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDI 198
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-66 1.50e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 48.21  E-value: 1.50e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489280071   5 IVLAGGSGTRLHPitlGVSKQLLPVYDKPMIYYPISVLMLAG-IKDILVISTPVDLPQYRNLL 66
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
5-77 2.11e-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: 47.52  E-value: 2.11e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489280071   5 IVLAGGSGTRLHpitLGVSKQLLPVYDKPMIYYPISVLM-LAGIKDILVISTPVDLPQYRNLLGDGSQFGVRFT 77
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIV 74
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-201 6.78e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.13  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTRL---HPitlgvsKQLLPVYDKPMIYYPISVLMLAGIKDILVIstpvdlpqyrnlLGDGS-----QFGVRF 76
Cdd:PRK14354   6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGAeevkeVLGDRS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  77 TYAEQPSPDGLAQAFIIGEEFIGD-DAVCLIL-GDN-IFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIDFDKEG 153
Cdd:PRK14354  68 EFALQEEQLGTGHAVMQAEEFLADkEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489280071 154 RALSI-EEKPAKPKSpYAV----TGLYFYDNDVIKIA-KAVKP-SPRGELEITDV 201
Cdd:PRK14354 148 EVEKIvEQKDATEEE-KQIkeinTGTYCFDNKALFEAlKKISNdNAQGEYYLTDV 201
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
2-201 9.56e-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: 9.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPitlGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLpqYRNLLGDGSQFgvrFTYAEQ 81
Cdd:PRK14357   1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPEWVKI---FLQEEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  82 PspdGLAQAFIIGEEFIGDDAVCLIL-GDNIFHGQHFGDQLRTAAERS-SGATVFGYWVKDPERFGVIDFDkEGRALSIE 159
Cdd:PRK14357  73 L---GTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEHNRKgADVTILVADLEDPTGYGRIIRD-GGKYRIVE 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489280071 160 EKPAKPKSPYAV---TGLYFYDND-VIKIAKAVKP-SPRGELEITDV 201
Cdd:PRK14357 149 DKDAPEEEKKIKeinTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
2-235 1.46e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 46.01  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   2 MKGIVLAGGSGTRLHPITLGVSKQLLPVYDK-PMIYYPISVLMLAGIKDILVIStpvdlpQYRNLL-----GDGSQFG-- 73
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT------QYQPLElnnhiGIGSPWDld 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  74 -------VRFTYAEQPSPD---GLAQAFIIGEEFIGD---DAVcLIL-GDNIFHgQHFGDQLRTAAERSSGAT--VFGYW 137
Cdd:PRK05293  78 ringgvtILPPYSESEGGKwykGTAHAIYQNIDYIDQydpEYV-LILsGDHIYK-MDYDKMLDYHKEKEADVTiaVIEVP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 138 VKDPERFGVIDFDKEGRALSIEEKPAKPKSPYAVTGLYFYDNDVIK---IAKAVKPSPR---GEleitDVNNAYLQRGD- 210
Cdd:PRK05293 156 WEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKeylIEDEKNPNSShdfGK----NVIPLYLEEGEk 231
                        250       260
                 ....*....|....*....|....*
gi 489280071 211 LHVERFgRGFaWLDTGTHDSLLEAS 235
Cdd:PRK05293 232 LYAYPF-KGY-WKDVGTIESLWEAN 254
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
4-234 1.89e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.59  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   4 GIVLAGGSGTRLHPITLGVSKQLLP---VYDkpMIYYPISVLMLAGIKDILVistpvdLPQYR---------------NL 65
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYV------LTQYKshsldrhisqtwrlsGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  66 LGdgsQF----------GVRFtYaeQPSPDGLAQAFiigeEFIGD---DAVCLILGDNIFHgQHFGDQLRTAAERSSGAT 132
Cdd:PRK00844  80 LG---NYitpvpaqqrlGKRW-Y--LGSADAIYQSL----NLIEDedpDYVVVFGADHVYR-MDPRQMVDFHIESGAGVT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071 133 VFGYWV--KDPERFGVIDFDKEGRALSIEEKPAKPK----SP---YAVTGLYFYDNDVikIAKAVKPSPRGELEITDVNN 203
Cdd:PRK00844 149 VAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPglpdDPdeaLASMGNYVFTTDA--LVDALRRDAADEDSSHDMGG 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 489280071 204 ----AYLQRGDLHVERF-----------GRGFaWLDTGTHDSLLEA 234
Cdd:PRK00844 227 diipRLVERGRAYVYDFstnevpgaterDRGY-WRDVGTIDAYYDA 271
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
4-109 2.36e-05

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 44.09  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   4 GIVLAGGSGTRLhpitlGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPVDLPQYRNLLGdgsqFGVRFTYAEQPS 83
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAG----LPVVVVINPDWE 73
                         90       100
                 ....*....|....*....|....*...
gi 489280071  84 pDGLAQAFIIGEEFIGDDA-VCLI-LGD 109
Cdd:cd04182   74 -EGMSSSLAAGLEALPADAdAVLIlLAD 100
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-166 3.26e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTRLHPitlGVSKQLLPVYDKPMIYYPISVLMLAGIKDI-LVISTPVDlpQYRNLLGDgsQFGVRFTYAEQPS 83
Cdd:PRK14355   7 IILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIvLVVGHQAE--KVREHFAG--DGDVSFALQEEQL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  84 PDGLAQAFIIGEEFIGDDAVCLILGDN-IFHGQHFGDQLrtAAERSSGA--TVFGYWVKDPERFGVIDFDKEGRALSI-E 159
Cdd:PRK14355  80 GTGHAVACAAPALDGFSGTVLILCGDVpLLRAETLQGML--AAHRATGAavTVLTARLENPFGYGRIVRDADGRVLRIvE 157

                 ....*..
gi 489280071 160 EKPAKPK 166
Cdd:PRK14355 158 EKDATPE 164
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
2-77 4.38e-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: 43.26  E-value: 4.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489280071   2 MKGIVLAGGSGTRlhpitLGVSKQLLPVYDKPMIYYPISVlmLAGIKDILVISTPVDlPQYRnllgdgsQFGVRFT 77
Cdd:COG0746    5 ITGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP-ERYA-------ALGVPVV 65
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
7-56 7.60e-05

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 42.57  E-value: 7.60e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489280071   7 LAGGSGTRLHpitlGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTP 56
Cdd:COG2266    1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
4-63 2.35e-04

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: 41.37  E-value: 2.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489280071   4 GIVLAGGSGTRLHPITLGVSKQLLPV---YDkpMIYYPISVLMLAGIKDILVistpvdLPQYR 63
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGV------LTQYK 55
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 7.15e-04

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.43  E-value: 7.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   1 MMKGIVLAGGSGTRLHPitlgVS-----KQLLPVY-DKPMIYYPIS-VLMLAGIKDILVI 53
Cdd:COG0836    2 MIYPVILAGGSGTRLWP----LSresypKQFLPLLgEKSLLQQTVErLAGLVPPENILVV 57
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
4-53 8.86e-04

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 39.90  E-value: 8.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489280071   4 GIVLAGGSGTRLHPITLGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVI 53
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
2-65 1.09e-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: 39.10  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489280071   2 MKGIVLAGGSGTRlhpitLGVSKQLLPVYDKPMIYYPISvlMLAGIKDILVISTPVDLPQYRNL 65
Cdd:cd02503    1 ITGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
5-201 1.75e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 39.62  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTR--------LHPItLGvskqllpvydKPMIYYPISVLMLAGIKDILVIstpvdlpqyrnlLGDGSQ----- 71
Cdd:COG1207    6 VILAAGKGTRmksklpkvLHPL-AG----------KPMLEHVLDAARALGPDRIVVV------------VGHGAEqvraa 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  72 -FGVRFTYAEQPSPDGLAQAFIIGEEFI-GDDAVCLILgdnifhgqhFGDQ-----------LRTAAERSSGATVFGYWV 138
Cdd:COG1207   63 lADLDVEFVLQEEQLGTGHAVQQALPALpGDDGTVLVL---------YGDVpliraetlkalLAAHRAAGAAATVLTAEL 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489280071 139 KDPERFGVIDFDKEGRALSI-EEKPAKP--KspyAV----TGLYFYDNDVIKIA-KAVKPS-PRGELEITDV 201
Cdd:COG1207  134 DDPTGYGRIVRDEDGRVLRIvEEKDATEeqR---AIreinTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
4-112 2.17e-03

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


Pssm-ID: 396773  Cd Length: 217  Bit Score: 38.47  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071    4 GIVLAGGSGTRLhpitlgVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTpvDLPQYRNLLgdgSQFGVRFTYAEQPS 83
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT--DSEEIADVA---KEFGAGVVMTSGSL 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 489280071   84 PDGLAQAFIIGEEFIG--DDAVCLILGDNIF 112
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNdhDDIIVNIQGDNPL 101
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
5-68 2.30e-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: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489280071   5 IVLAGGSGTRLhpiTLGVSKQLLPVYDKPMIYYPISVLMLAG-IKDILVISTPVDLPQYRNLLGD 68
Cdd:PRK09382   9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
2-53 2.53e-03

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: 38.71  E-value: 2.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489280071   2 MKGIVLAGGSGTRLHPitlgVS-----KQLLPVY-DKPMIYYPIS-VLMLAGIKDILVI 53
Cdd:cd02509    1 IYPVILAGGSGTRLWP----LSresypKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVV 55
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-63 4.80e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 37.47  E-value: 4.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489280071   1 MMKGIVLAGGSGTRLHpitlGVSKQLLPVYDKPMIYYPISVlmLAGIKDILVISTPVDLPQYR 63
Cdd:PRK00317   3 PITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIER--LAPQVDEIVINANRNLARYA 59
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-165 8.56e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.53  E-value: 8.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071   5 IVLAGGSGTRLHPitlGVSKQLLPVYDKPMIYYPISVLMLAGIKDILVISTPvDLPQYRNLLgdgSQFGVRFTYAEQPSP 84
Cdd:PRK14353   9 IILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAA---AKIAPDAEIFVQKER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489280071  85 DGLAQAFIIGEEFI--GDDAVCLILGDNIFHGQHFGDQLRTAAERSSGATVFGYWVKDPERFGVIdFDKEGRALSI-EEK 161
Cdd:PRK14353  82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGRL-IVKGGRLVAIvEEK 160

                 ....
gi 489280071 162 PAKP 165
Cdd:PRK14353 161 DASD 164
 
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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