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Conserved domains on  [gi|651324434|ref|WP_026448742|]
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glucose-1-phosphate thymidylyltransferase RfbA [Actinopolyspora mortivallis]

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: 517.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 161 PSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVL 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 651324434 241 ENRQGVRIACLEEIALRMGYISAEQCYELGRGLAKSGYGHYVMEVAR 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: 517.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 161 PSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVL 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 651324434 241 ENRQGVRIACLEEIALRMGYISAEQCYELGRGLAKSGYGHYVMEVAR 287
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-287 9.62e-178

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: 491.52  E-value: 9.62e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434    2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   82 EPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  162 SHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVLE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 651324434  242 NRQGVRIACLEEIALRMGYISAEQCYELGRGLAKSGYGHYVMEVAR 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 8.83e-160

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: 444.33  E-value: 8.83e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 161 PSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVL 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-289 1.50e-134

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 382.87  E-value: 1.50e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  82 EPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 162 SHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVLE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 651324434 242 NRQGVRIACLEEIALRMGYISAEQCYELGRGLAKSGYGHYVMEVARGF 289
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 4.38e-91

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: 270.66  E-value: 4.38e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434    2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDK-PMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   81 PEPNGLAEAFVLGADFVGEDSV-ALVLGDNIFYGQGFSKLLQRSV--AELEGCTLFGYAVRDPQRYGVGETDSEGRLVSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIekAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  158 EEKPSHPR-SNKAVTGLYLYDNEVVE-IARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 651324434  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: 517.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 161 PSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVL 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 651324434 241 ENRQGVRIACLEEIALRMGYISAEQCYELGRGLAKSGYGHYVMEVAR 287
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-287 9.62e-178

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: 491.52  E-value: 9.62e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434    2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   82 EPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  162 SHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVLE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 651324434  242 NRQGVRIACLEEIALRMGYISAEQCYELGRGLAKSGYGHYVMEVAR 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 8.83e-160

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: 444.33  E-value: 8.83e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 161 PSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVL 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-289 1.50e-134

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 382.87  E-value: 1.50e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  82 EPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 162 SHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQFVQVLE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 651324434 242 NRQGVRIACLEEIALRMGYISAEQCYELGRGLAKSGYGHYVMEVARGF 289
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 4.38e-91

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: 270.66  E-value: 4.38e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434    2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDK-PMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   81 PEPNGLAEAFVLGADFVGEDSV-ALVLGDNIFYGQGFSKLLQRSV--AELEGCTLFGYAVRDPQRYGVGETDSEGRLVSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIekAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  158 EEKPSHPR-SNKAVTGLYLYDNEVVE-IARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYAWLDTGTHESLLEAGQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 651324434  236 FV 237
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-237 2.07e-68

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: 212.43  E-value: 2.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDlPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGqGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDsEGRLVSIEEK 160
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVEK 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 651324434 161 PSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGYaWLDTGTHESLLEAGQFV 237
Cdd:cd04189  158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-225 5.61e-59

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: 187.79  E-value: 5.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   3 GIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDlPLFRRLFGDGSHLGLRMEYTVQPE 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  83 PNGLAEAFVLGADFVGEDSVALVLGDNIFYGqGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEKPS 162
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651324434 163 HPRSNKAVTGLYLYDNEVVEIARSLRPsaRGELEITDVNAEYLRAGRARMTELgRGYaWLDTG 225
Cdd:cd04181  159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV-DGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-249 9.15e-56

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: 183.76  E-value: 9.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434    2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTVQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   82 EPNGLAEAFVLGADFVGEDSVALVLGDNIFYGqGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  162 SHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVnAEYL-----RAGRARMTelgrGYaWLDTGTHESLLEAGQF 236
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDA-IQWLiekgyKVGGSKVT----GW-WKDTGKPEDLLDANRL 233
                         250
                  ....*....|....*
gi 651324434  237 V--QVLENRQGVRIA 249
Cdd:TIGR01208 234 IldEVEREVQGVDDE 248
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-233 6.49e-45

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: 156.60  E-value: 6.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434    1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDlPLFRRLFGDGSHLGLRMEYTVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   81 PEPNGLAEAFVLGADFVgEDSVALVLGDNIFYgqgfSKLLQRsVAELEGCTLFGYAVRDPQRYGVGETDsEGRLVSIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLD----SDLLER-LIRAEAPAIAVVEVDDPSDYGVVETD-GGRVTGIVEK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651324434  161 PSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARMTELGRGyaWLDTGTHESLLEA 233
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDA 223
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-233 4.89e-41

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: 142.21  E-value: 4.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLIStpGDLP-LFRRLFGDGSHLGLRMEYTVQ 80
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV--GYLAeQIEEYFGDGSRFGVRITYVDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVLGDnIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEK 160
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651324434 161 PSHPRSNKAVTGLYLYDNEVVEIARslrpsARGELEITDVNAEYLRAGRARMTELgRGYaWLDTGTHESLLEA 233
Cdd:COG1208  158 PEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-233 6.59e-31

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: 116.48  E-value: 6.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPG----------DLPLFRRLFGDGSH 70
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfdrSYELEETLEKKGKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  71 LGLR----------MEYTVQPEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQ--GFSKLLQrsVAELEGCTLFGY--- 135
Cdd:cd02541   81 DLLEevriisdlanIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepCLKQLIE--AYEKTGASVIAVeev 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 136 AVRDPQRYGVGET-DSEGRLVSIE---EKPS--HPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDvnaeylraGR 209
Cdd:cd02541  159 PPEDVSKYGIVKGeKIDGDVFKVKglvEKPKpeEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTD--------AI 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 651324434 210 ARMTELGRGYA------WLDTGTHESLLEA 233
Cdd:cd02541  231 AKLLEEEPVYAyvfegkRYDCGNKLGYLKA 260
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 1.82e-20

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 88.94  E-value: 1.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYplSV--LMLAGIRDVLLISTP----------------------GD 57
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiedhfdrsyeleatleakGK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  58 LPLFRRLfgDGSHLGLRMEYTVQPEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQgfSKLLQR--SVAELEGCTLFG- 134
Cdd:COG1210   83 EELLEEV--RSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQmiEVYEETGGSVIAv 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 135 YAVRDPQ--RYG-VGETDSEGRLVSIE---EKPSH---PrSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYL 205
Cdd:COG1210  159 QEVPPEEvsKYGiVDGEEIEGGVYRVTglvEKPAPeeaP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALA 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 651324434 206 RAGR--ARMTElGRGYawlDTGTHESLLEA 233
Cdd:COG1210  238 KEEPvyAYEFE-GKRY---DCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-233 9.28e-20

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


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 85.68  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRD-VLLISTPGDlpLFRRLFGDGSHLGLRMEYTVQPE 82
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRiVLSVGYLAE--QIEEYFGDGYRGGIRIYYVIEPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  83 PNGLAEAFVLGADFVGEDSVALVLGDNIFYGqGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEKPS 162
Cdd:cd06915   80 PLGTGGAIKNALPKLPEDQFLVLNGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 651324434 163 HPRSNKAVTGLYLYDNEVVEIARSLRPSargeLEiTDVNAEYLRAGRARMTElGRGYaWLDTGTHESLLEA 233
Cdd:cd06915  159 GAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRLYGFE-VDGY-FIDIGIPEDYARA 222
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-181 3.69e-19

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: 84.18  E-value: 3.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLL-IS-TPGDLPLFRRLFGDgsHLGLRMEYT 78
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNyRPEDMVPFLKEYEK--KLGIKITFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  79 VQPEPNGLAEAFVLGADFVGEDSVA-LVLGDNIFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETD-SEGRLVS 156
Cdd:cd06425   79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDeNTGRIER 158
                        170       180
                 ....*....|....*....|....*
gi 651324434 157 IEEKPSHPRSNKAVTGLYLYDNEVV 181
Cdd:cd06425  159 FVEKPKVFVGNKINAGIYILNPSVL 183
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-233 1.21e-17

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 79.86  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVlLISTpGDLP-LFRRLFGDGSHLGLRMEYTVQPE 82
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISV-NYLAeMIEDYFGDGSKFGVNISYVREDK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  83 PNGLAEAFVLGADFVgEDSVALVLGDnIFYGQGFSKLL---QRSVAELEGCT-LFGYAVrdPqrYGVGETDsEGRLVSIE 158
Cdd:cd06426   80 PLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLdfhKENNADATVCVrEYEVQV--P--YGVVETE-GGRITSIE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 159 EKPSHprSNKAVTGLYLYDNEVVE-IARSLRpsargeLEITDVnaeyLRAGRARMTELG----RGYaWLDTGTHESLLEA 233
Cdd:cd06426  153 EKPTH--SFLVNAGIYVLEPEVLDlIPKNEF------FDMPDL----IEKLIKEGKKVGvfpiHEY-WLDIGRPEDYEKA 219
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-106 3.85e-15

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: 72.69  E-value: 3.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFR---RLFGDGSHLGLRMEY 77
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEIStylRSFPLNLKQKLDEVT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 651324434  78 TVQPEPNGLAEA------------FVLGADFVGEDSVALVL 106
Cdd:cd04198   81 IVLDEDMGTADSlrhirkkikkdfLVLSCDLITDLPLIELV 121
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-233 3.63e-13

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 68.95  E-value: 3.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   3 GIVLAGGSGTRLHPITQVVSkqllpvydKPMVYY---------PLSVLMLAGIRDVLLI------StpgdlpLFRRLfGD 67
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRA--------KPAVPFggkyriidfPLSNCVNSGIRRVGVLtqykshS------LNDHI-GS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  68 GSHLGLRME----YTVQPEPNGLAEAFVLG-ADFV----------GEDSVaLVL-GDNIfYGQGFSKLLQRSV---AEle 128
Cdd:COG0448   69 GKPWDLDRKrggvFILPPYQQREGEDWYQGtADAVyqnldfiersDPDYV-LILsGDHI-YKMDYRQMLDFHIesgAD-- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 129 gCTLFGYAV--RDPQRYGVGETDSEGRLVSIEEKPSHPRSNKAVTGLYLYDNEV-VEIarsLRPSARGELE--ITDVNAE 203
Cdd:COG0448  145 -ITVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVlIEL---LEEDAPNSSHdfGKDIIPR 220
                        250       260       270
                 ....*....|....*....|....*....|
gi 651324434 204 YLRAGRARMTELgRGYaWLDTGTHESLLEA 233
Cdd:COG0448  221 LLDRGKVYAYEF-DGY-WRDVGTIDSYYEA 248
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-233 3.88e-13

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: 67.21  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLL-ISTPGDlpLFRRLFGDgSHLGLRMEYtvQ 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVnTHHLAD--QIEAHLGD-SRFGLRITI--S 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAE---AFVLGADFVGEDSVALVLGDnIFYGQGFSKLLQRSVAELEGCTLFGYAVRDP--QRYGVGETDSEGRLV 155
Cdd:cd06422   76 DEPDELLEtggGIKKALPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPghNGVGDFSLDADGRLR 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651324434 156 SIEEKPSHPRsnkAVTGLYLYDNEVveiarsLRPSARGELEITDVNAEYLRAGRARmTELGRGYaWLDTGTHESLLEA 233
Cdd:cd06422  155 RGGGGAVAPF---TFTGIQILSPEL------FAGIPPGKFSLNPLWDRAIAAGRLF-GLVYDGL-WFDVGTPERLLAA 221
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-203 4.70e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 65.29  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLIS------------TPGDLPLF------R 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  63 RLFGDGSHL---GLRMEYTVQPEPNGLAEAFVLGADFVGEDSVALVLGDNIFYGQGFSKL---LQRSVAELEGC----TL 132
Cdd:PRK10122  84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLrynLAAMIARFNETgrsqVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 133 FGYAVRDPQRYGVGET----DSEG---RLVSIEEKPSHPR---SNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNA 202
Cdd:PRK10122 164 AKRMPGDLSEYSVIQTkeplDREGkvsRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243

                 .
gi 651324434 203 E 203
Cdd:PRK10122 244 E 244
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-52 2.75e-11

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: 61.89  E-value: 2.75e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLI 52
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-199 1.37e-10

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 61.08  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLIsTPGDLPLFRRLFGDGSHLGLRMEYTVQ- 80
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKNSIENHFDTSFELEAMLEKRVKr 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 ----------PE-----------PNGLAEAFVLGADFVGEDSVALVLGDNI-------------------FYGQGFSKLL 120
Cdd:PRK13389  89 qlldevqsicPPhvtimqvrqglAKGLGHAVLCAHPVVGDEPVAVILPDVIldeyesdlsqdnlaemirrFDETGHSQIM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 121 QRSVAELEgctlfGYAVRDPQRYGVGETDSeGRLVSIEEKP--SHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEIT 198
Cdd:PRK13389 169 VEPVADVT-----AYGVVDCKGVELAPGES-VPMVGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242

                 .
gi 651324434 199 D 199
Cdd:PRK13389 243 D 243
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-233 5.79e-10

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 59.50  E-value: 5.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHPITQVVSKqllpvydkPMVYY---------PLSVLMLAGIRDV---------LL-----ISTPGD 57
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAK--------PAVPFggkyriidfTLSNCANSGIDTVgvltqyqplELnnhigIGSPWD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  58 LplfrrlfgDGSHLGLrmeyTVQPeP----------NGLAEAFVLGADFVGEDSVALVL---GDNIfYGQGFSKLLQRSV 124
Cdd:PRK05293  76 L--------DRINGGV----TILP-PyseseggkwyKGTAHAIYQNIDYIDQYDPEYVLilsGDHI-YKMDYDKMLDYHK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 125 AELEGCTLfgyAVRD-P----QRYGVGETDSEGRLVSIEEKPSHPRSNKAVTGLYLYDNEVVEiaRSLRPSARGELEITD 199
Cdd:PRK05293 142 EKEADVTI---AVIEvPweeaSRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLK--EYLIEDEKNPNSSHD 216
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 651324434 200 ----VNAEYLRAGRARMTELGRGYaWLDTGTHESLLEA 233
Cdd:PRK05293 217 fgknVIPLYLEEGEKLYAYPFKGY-WKDVGTIESLWEA 253
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
4-212 5.27e-08

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 53.83  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRLHpitQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGshlglrMEYTVQPEP 83
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  84 NGLAEAFVLGADFVGE-DSVALVL-GDN-IFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSIEEK 160
Cdd:PRK14358  82 LGTGDAFLSGASALTEgDADILVLyGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 651324434 161 PSHPRSNKAV----TGLYLYDNEVVEIARSL-RPSARGELEITDVNAEYlRAGRARM 212
Cdd:PRK14358 162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLY-RAGGAQV 217
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-67 5.46e-07

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 49.36  E-value: 5.46e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651324434   4 IVLAGGSGTRLHpitQVVSKQLLPVYDKPMVYYPLSVLMLAG-IRDVLLISTPGDLPLFRRLFGD 67
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-52 1.12e-06

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 48.70  E-value: 1.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 651324434   2 KGIVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLI 52
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-212 1.30e-06

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: 48.79  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   3 GIVLAGG--SGTRLHPITQVVSKQLLPVYDKPMVYYPLSVL-MLAGIRDVLLISTPGDLPLFRRLFGDGSHLGLRMEYTV 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  80 QPEPNGLA----------------EAFVLGADFVGEDSVALVLGdniFYGQ-GFSKLLQRSVAELEGCTLFGYAVRDPqr 142
Cdd:cd06428   81 EYKPLGTAgglyhfrdqilagnpsAFFVLNADVCCDFPLQELLE---FHKKhGASGTILGTEASREQASNYGCIVEDP-- 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 143 ygvgetdSEGRLVSIEEKPSHPRSNKAVTGLYLYDNEVVEIARSLRPSARGELEITDVNAEYLRAGRARM 212
Cdd:cd06428  156 -------STGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRL 218
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-120 1.33e-06

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: 48.38  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRLHPITQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLIStpGDLP-LFRRLFGDGSHLglrmEYTVQPE 82
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT--GYKKeQIEELLKKYPNI----KFVYNPD 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 651324434  83 PN--GLAEAFVLGADFVGEDSvaLVL-GDNIFYGQGFSKLL 120
Cdd:cd02523   76 YAetNNIYSLYLARDFLDEDF--LLLeGDVVFDPSILERLL 114
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-208 1.49e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.06  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRL---HPitqvvsKQLLPVYDKPMVYYPLSVLMLAGIRDVLLIstpgdlplfrrlFGDGS-----HLGLRM 75
Cdd:PRK14354   6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGAeevkeVLGDRS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  76 EYTVQPEPNGLAEAFVLGADFV-GEDSVALVL-GDN-IFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEG 152
Cdd:PRK14354  68 EFALQEEQLGTGHAVMQAEEFLaDKEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651324434 153 RLVSI-EEKPSHPrSNKAV----TGLYLYDNEV-VEIARSLRP-SARGELEITDVNAEYLRAG 208
Cdd:PRK14354 148 EVEKIvEQKDATE-EEKQIkeinTGTYCFDNKAlFEALKKISNdNAQGEYYLTDVIEILKNEG 209
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-70 3.02e-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: 47.13  E-value: 3.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651324434   4 IVLAGGSGTRLHpitQVVSKQLLPVYDKPMVYYPLSVLM-LAGIRDVLLISTPGDLPLFRRLFGDGSH 70
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-200 2.66e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 45.14  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   1 MKGIVLAGGSGTRLHpitQVVSKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPlfrrlfgdGSHLGLRMEYTVQ 80
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAELV--------KKLLPEWVKIFLQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  81 PEPNGLAEAFVLGADFVGEDSVALVL-GDNIFYGQG-FSKLLQRSVAELEGCTLFGYAVRDPQRYG--VGEtdsEGRLVS 156
Cdd:PRK14357  70 EEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENtLKRLIEEHNRKGADVTILVADLEDPTGYGriIRD---GGKYRI 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 651324434 157 IEEKPSHPRSNKAV---TGLYLYDNE-VVEIARSLRP-SARGELEITDV 200
Cdd:PRK14357 147 VEDKDAPEEEKKIKeinTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-209 4.09e-05

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: 44.04  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRLH---PitqvvsKQLLPVYDKPMVYYPL-SVLMLAGIRDVLLISTPGDlpLFRRLFGDGSHlglrmEYTV 79
Cdd:cd02540    2 VILAAGKGTRMKsdlP------KVLHPLAGKPMLEHVLdAARALGPDRIVVVVGHGAE--QVKKALANPNV-----EFVL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  80 QPEPNGLAEAfVLGADFVGEDSVALVLgdnIFYG-------QGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEG 152
Cdd:cd02540   69 QEEQLGTGHA-VKQALPALKDFEGDVL---VLYGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNG 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651324434 153 RLVSI-EEKPSHP--RSNKAV-TGLYLYDNEVVEIA-RSLRPS-ARGELEITDVNAEYLRAGR 209
Cdd:cd02540  145 KVLRIvEEKDATEeeKAIREVnAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDIIALAVADGL 207
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-64 5.45e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 43.58  E-value: 5.45e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651324434   4 IVLAGGSGTRL---HPitqvvsKQLLPVYDKPMVYYPLSVLMLAG-IRDVLLISTPGDLPLFRRL 64
Cdd:PRK00155   7 IIPAAGKGSRMgadRP------KQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAEL 65
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-53 7.61e-05

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: 42.91  E-value: 7.61e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 651324434   3 GIVLAGGSGTRLHPITQVVSKQLLPVYDKpmvY----YPLSVLMLAGIRDVLLIS 53
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR---YrlidFPLSNMVNSGIRNVGVLT 52
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-200 1.11e-04

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: 43.48  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRLH---PitqvvsKQLLPVYDKPMVYYPLSVLMLAGIRDVLLIstpgdlplfrrlFGDG-----SHLG-LR 74
Cdd:COG1207    6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGaeqvrAALAdLD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  75 MEYTVQPEPNGLAEAFVLGADFVGEDS-VALVLgdnifYG-------QGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVG 146
Cdd:COG1207   68 VEFVLQEEQLGTGHAVQQALPALPGDDgTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTGYGRI 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 147 ETDSEGRLVSI-EEKPSHP--RSNKAV-TGLYLYDNEVVEIA-RSLRPS-ARGELEITDV 200
Cdd:COG1207  143 VRDEDGRVLRIvEEKDATEeqRAIREInTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-209 4.57e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.27  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   4 IVLAGGSGTRLHpiTQVVsKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLFGDGShlglrMEYTVQPEP 83
Cdd:PRK14355   7 IILAAGKGTRMK--SDLV-KVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEEQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  84 NGLAEAFVLGADFV--GEDSVALVLGDN-IFYGQGFSKLLQRSVAELEGCTLFGYAVRDPQRYGVGETDSEGRLVSI-EE 159
Cdd:PRK14355  79 LGTGHAVACAAPALdgFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 651324434 160 KPSHP--RSNKAV-TGLYLYDNEVVE--IARSLRPSARGELEITDVNAEYLRAGR 209
Cdd:PRK14355 159 KDATPeeRSIREVnSGIYCVEAAFLFdaIGRLGNDNAQGEYYLTDIVAMAAAEGL 213
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-233 9.19e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 40.58  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   3 GIVLAGGSGTRLHPITQVVSKQLLP---VYDkpMVYYPLSVLMLAGIRDVLLISTPGDLPLFRrlfgdgsHL--GLRM-- 75
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLTQYKSHSLDR-------HIsqTWRLsg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434  76 ---EYtVQPEP----------NGLAEAFVLGADFVGE---DSVALVLGDNIfYGQGFSKLLQRSVAELEGCTLfgYAVRD 139
Cdd:PRK00844  79 llgNY-ITPVPaqqrlgkrwyLGSADAIYQSLNLIEDedpDYVVVFGADHV-YRMDPRQMVDFHIESGAGVTV--AAIRV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434 140 P----QRYGVGETDSEGRLVSIEEKPSHP-----RSNKAVT--GLYLYDNEVveIARSLRPSARGELEITD----VNAEY 204
Cdd:PRK00844 155 PreeaSAFGVIEVDPDGRIRGFLEKPADPpglpdDPDEALAsmGNYVFTTDA--LVDALRRDAADEDSSHDmggdIIPRL 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 651324434 205 LRAGRARM-----------TELGRGYaWLDTGTHESLLEA 233
Cdd:PRK00844 233 VERGRAYVydfstnevpgaTERDRGY-WRDVGTIDAYYDA 271
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-108 4.51e-03

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 37.45  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   3 GIVLAGGSGTRL-HPitqvvsKQLLPVYDKPMVYYPLSVLMLAGIRDVLLISTPGDLPLFRRLfgdgSHLGLRMEYTVQP 81
Cdd:COG2068    6 AIILAAGASSRMgRP------KLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAL----AGLGVRVVVNPDW 75
                         90       100
                 ....*....|....*....|....*....
gi 651324434  82 EpNGLAEAFVLGADFVGE--DSVALVLGD 108
Cdd:COG2068   76 E-EGMSSSLRAGLAALPAdaDAVLVLLGD 103
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-34 4.89e-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: 37.94  E-value: 4.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 651324434   1 MKGIVLAGGSGTRLHPI-TQVVSKQLLPVY-DKPMV 34
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLL 36
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-108 9.28e-03

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: 36.38  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651324434   3 GIVLAGGSGTRLHPItqvvsKQLLPVYDKPMVYYPLSVLMLAGIRDVLLIsTPGDLPLFRRLFGDGSHLGLrmeytVQPE 82
Cdd:cd04182    3 AIILAAGRSSRMGGN-----KLLLPLDGKPLLRHALDAALAAGLSRVIVV-LGAEADAVRAALAGLPVVVV-----INPD 71
                         90       100
                 ....*....|....*....|....*....
gi 651324434  83 P-NGLAEAFVLGADFVGEDSVALV--LGD 108
Cdd:cd04182   72 WeEGMSSSLAAGLEALPADADAVLilLAD 100
 
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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