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Conserved domains on  [gi|2044928587|ref|WP_213570227|]
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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];
3-287 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 561.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2044928587 243 HRQGLKVACLEEIAYQQGWIDQAHLLKRGEMFGKTGYGQYLFGLV 287
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 561.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2044928587 243 HRQGLKVACLEEIAYQQGWIDQAHLLKRGEMFGKTGYGQYLFGLV 287
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 3-286 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 548.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2044928587 243 HRQGLKVACLEEIAYQQGWIDQAHLLKRGEMFGKTGYGQYLFGL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 3-241 6.83e-176

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: 484.77  E-value: 6.83e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTI 241
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-287 2.72e-142

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 402.13  E-value: 2.72e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2044928587 243 HRQGLKVACLEEIAYQQGWIDQAHLLKRGEMFGKTGYGQYLFGLV 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-238 7.56e-100

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 292.62  E-value: 7.56e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDK-PMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQ 81
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  82 PSPDGLAQAFLIGEEFIGDDSV-CLILGDNIFHGQGFTPQLRKAAQ--QGKGATVFGYWVKDPERFGVVEFDDKGHALSI 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 159 EEKPTQPK-SSYAVTGLYFYDNDVI-KIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQ 236
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLdFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2044928587 237 YV 238
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 561.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2044928587 243 HRQGLKVACLEEIAYQQGWIDQAHLLKRGEMFGKTGYGQYLFGLV 287
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 3-286 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 548.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2044928587 243 HRQGLKVACLEEIAYQQGWIDQAHLLKRGEMFGKTGYGQYLFGL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 3-241 6.83e-176

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: 484.77  E-value: 6.83e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTI 241
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-287 2.72e-142

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 402.13  E-value: 2.72e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2044928587 243 HRQGLKVACLEEIAYQQGWIDQAHLLKRGEMFGKTGYGQYLFGLV 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-238 7.56e-100

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 292.62  E-value: 7.56e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDK-PMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQ 81
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  82 PSPDGLAQAFLIGEEFIGDDSV-CLILGDNIFHGQGFTPQLRKAAQ--QGKGATVFGYWVKDPERFGVVEFDDKGHALSI 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 159 EEKPTQPK-SSYAVTGLYFYDNDVI-KIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFAWLDTGTHDSLLEASQ 236
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLdFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2044928587 237 YV 238
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 3-238 4.09e-70

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: 216.67  E-value: 4.09e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI--STPQDLPQYkqlLGDGSQFGIELSYAE 80
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgPTGEEIKEA---LGDGSRFGVRITYIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  81 QPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDkGHALSIEE 160
Cdd:cd04189    79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD-GRIVRLVE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044928587 161 KPTQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRG-SLNVQLLgRGFaWLDTGTHDSLLEASQYV 238
Cdd:cd04189   157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGrRVGYSIV-TGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 4-226 9.12e-62

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: 194.72  E-value: 9.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDlPQYKQLLGDGSQFGIELSYAEQPS 83
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  84 PDGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKPT 163
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044928587 164 QPKSSYAVTGLYFYDNDVIKIAKAVKpsPRGELEITDINNAYLNRGSLNVQLLgrGFAWLDTG 226
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 3-238 2.86e-59

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


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 192.62  E-value: 2.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEQP 82
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKP 162
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044928587 163 TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGFaWLDTGTHDSLLEASQYV 238
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 2-238 1.75e-46

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 160.45  E-value: 1.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   2 TKGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDlPQYKQLLGDGSQFGIELSYAEQ 81
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  82 PSPDGLAQAFLIGEEFIgDDSVCLILGDNIFHGqgftPQLRKAAQqGKGATVFGYWVKDPERFGVVEFDDkGHALSIEEK 161
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDS----DLLERLIR-AEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044928587 162 PTQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGRGfaWLDTGTHDSLLEASQYV 238
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 3-238 6.95e-44

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: 149.15  E-value: 6.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLIStpQDLP-QYKQLLGDGSQFGIELSYAEQ 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV--GYLAeQIEEYFGDGSRFGVRITYVDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  82 PSPDGLAQAFLIGEEFIGDDSVCLILGDNIFhGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEK 161
Cdd:COG1208    79 GEPLGTGGALKRALPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044928587 162 PTQPKSSYAVTGLYFYDNDVIKIAkavkpsPRGE-LEITDINNAYLNRGSLNVQLLgRGFaWLDTGTHDSLLEASQYV 238
Cdd:COG1208   158 PEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANALL 227
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 2-235 3.14e-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: 111.86  E-value: 3.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   2 TKGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQdlpqyKQLLGDGSQFGIEL----- 76
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRG-----KRAIEDHFDRSYELeetle 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  77 --------------------SYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGF-TPQLRKAAQQgKGATVFG 135
Cdd:cd02541    76 kkgktdlleevriisdlaniHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYEK-TGASVIA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 136 YWVKDPE---RFGVVEFDDKG----HALSIEEKPTQ--PKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYL 206
Cdd:cd02541   155 VEEVPPEdvsKYGIVKGEKIDgdvfKVKGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLL 234

                         250       260       270
                  ....*....|....*....|....*....|
gi 2044928587 207 NRGSLN-VQLLGRgfaWLDTGTHDSLLEAS 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 6.29e-23

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: 93.77  E-value: 6.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLiSTPQDLPQYKQLLGDGSQFGIELSYAEQPSP 84
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVL-SVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  85 DGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKPTQ 164
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044928587 165 PKSSYAVTGLYFYDNDVIKIAKAVKPSprgeLEiTDINNAYLNRGSLnvqllgRGFA----WLDTGTHDSLLEA 234
Cdd:cd06915   160 AAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-234 3.95e-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: 89.11  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREIlLISTPQDLPQYKQLLGDGSQFGIELSYAEQPSP 84
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  85 DGLAQAFLIGEEFIgDDSVCLILGDnIFHGQGFTPQLRKAAQQGKGATVFG--YWVKDPerFGVVEFDDkGHALSIEEKP 162
Cdd:cd06426    81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETEG-GRITSIEEKP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044928587 163 TQpkSSYAVTGLYFYDNDVIKIAkavkpsPRGE-LEITDINNAYLNRG-SLNVQLLgRGFaWLDTGTHDSLLEA 234
Cdd:cd06426   156 TH--SFLVNAGIYVLEPEVLDLI------PKNEfFDMPDLIEKLIKEGkKVGVFPI-HEY-WLDIGRPEDYEKA 219
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 3-237 9.17e-20

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 85.73  E-value: 9.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILL-IS-TPQDLPQYKQLLGDgsQFGIELSYAE 80
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNyRPEDMVPFLKEYEK--KLGIKITFSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  81 QPSPDGLAQAFLIGEEFIGDDSVC-LILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFD-DKGHALSI 158
Cdd:cd06425    80 ETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDeNTGRIERF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 159 EEKPTQPKSSYAVTGLYFYDNDVIKiakavkpspRGELEITDINN----AYLNRGSLNVQLLgRGFaWLDTGTHDSLLEA 234
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVLD---------RIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WMDIGQPKDFLKG 228


                  ...
gi 2044928587 235 SQY 237
Cdd:cd06425   229 MSL 231
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-234 5.00e-19

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 84.70  E-value: 5.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   2 TKGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTP------------QDLPQY------K 63
Cdd:COG1210     4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfdrsYELEATleakgkE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  64 QLLG--DGSQFGIELSYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQ-GFTPQLRKAAQQgKGATVFGywVK- 139
Cdd:COG1210    84 ELLEevRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkPCLKQMIEVYEE-TGGSVIA--VQe 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 140 -DPE---RFGVVEFDDKGHAL----SIEEKPTQPK--SSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINNAYLNRG 209
Cdd:COG1210   161 vPPEevsKYGIVDGEEIEGGVyrvtGLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEE 240

                         250       260
                  ....*....|....*....|....*.
gi 2044928587 210 SLNVQLL-GRgfaWLDTGTHDSLLEA 234
Cdd:COG1210   241 PVYAYEFeGK---RYDCGDKLGYLKA 263
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
3-216 1.21e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 69.53  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLIS------------TPQDLPQY------KQ 64
Cdd:PRK10122    5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  65 LLGDGSQF---GIELSYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFTPqLR--------KAAQQGKGATV 133
Cdd:PRK10122   85 LLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADP-LRynlaamiaRFNETGRSQVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 134 FGYWVKDPERFGVVE----FDDKGHALSIE---EKPTQPK---SSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINN 203
Cdd:PRK10122  164 AKRMPGDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243

                         250
                  ....*....|...
gi 2044928587 204 AYLNRGSLNVQLL 216
Cdd:PRK10122  244 ELAKKQSVDAMLM 256
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-66 1.26e-12

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: 65.37  E-value: 1.26e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLL 66
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-234 1.36e-12

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: 65.67  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREIlLIST---PQdlpQYKQLLGDgSQFGIELSYA 79
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlAD---QIEAHLGD-SRFGLRITIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  80 EQP-----SPDGLAQAfligEEFIGDDSVCLILGDNIFHGqGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEF--DDK 152
Cdd:cd06422    76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDAD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 153 GHALSIEEKPTQPkssYAVTGLYFYDNDVIKIAkavkpsPRGELEITDINNAYLNRGSLnVQLLGRGFaWLDTGTHDSLL 232
Cdd:cd06422   151 GRLRRGGGGAVAP---FTFTGIQILSPELFAGI------PPGKFSLNPLWDRAIAAGRL-FGLVYDGL-WFDVGTPERLL 219


                  ..
gi 2044928587 233 EA 234
Cdd:cd06422   220 AA 221
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-200 3.59e-12

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 65.31  E-value: 3.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI--STPQDLPQY----------------KQ 64
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthSSKNSIENHfdtsfeleamlekrvkRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  65 LLGDGSQF---GIELSYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNI-------FHGQGFTPQLRKAAQQGKgATVF 134
Cdd:PRK13389   90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeyesdLSQDNLAEMIRRFDETGH-SQIM 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044928587 135 GYWVKDPERFGVVefDDKGHAL---------SIEEKP--TQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITD 200
Cdd:PRK13389  169 VEPVADVTAYGVV--DCKGVELapgesvpmvGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-53 1.83e-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: 62.27  E-value: 1.83e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI 53
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-224 8.60e-11

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 60.71  E-value: 8.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDlPQYKQLLGDgsQFGIELSYAEQPSP 84
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKK--YPNIKFVYNPDYAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  85 DGLAQAFLIGEEFIGDDsvCLIL-GDNIFHGQGFtpqLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSIEEKPT 163
Cdd:cd02523    79 TNNIYSLYLARDFLDED--FLLLeGDVVFDPSIL---ERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGIISKAK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044928587 164 QPKSSYAVT-GLYFYDND----VIKIAKAVKPSPRGELEITDINNAYLNRGSLNVQLLGrGFAWLD 224
Cdd:cd02523   154 NLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 4-181 8.18e-10

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 58.93  E-value: 8.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLHPITLGVSKqllpiydkPMIYY---------PISVLMLAGIREILListpqdLPQYKQL-----LGDG 69
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKSHslndhIGSG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  70 SQF-------GIELSYAEQPSPD-----GLAQAFLIGEEFIGDDSV--CLIL-GDNIFHgQGFTPQLRKAAQQGKGATVF 134
Cdd:COG0448    70 KPWdldrkrgGVFILPPYQQREGedwyqGTADAVYQNLDFIERSDPdyVLILsGDHIYK-MDYRQMLDFHIESGADITVA 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2044928587 135 GYWV--KDPERFGVVEFDDKGHALSIEEKPTQPKSSYAVTGLYFYDNDV 181
Cdd:COG0448   149 CIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-68 1.65e-09

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 56.68  E-value: 1.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044928587   5 IVLAGGSGTRLHpitLGVSKQLLPIYDKPMIYYPISVLMLAG-IREILLISTPQDLPQYKQLLGD 68
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
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 3.41e-09

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: 56.11  E-value: 3.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGG--SGTRLHPITLGVSKQLLPIYDKPMIYYPISVL-MLAGIREILLISTPQDLpQYKQLLGDGSQ-FGIELSYA 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPES-VFSDFISDAQQeFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  80 EQPSPDGLA---------------QAFLIgeefIGDDSVC-LILGDNI-FH---GQGFTPQLRKAAQQgkGATVFGYWVK 139
Cdd:cd06428    80 QEYKPLGTAgglyhfrdqilagnpSAFFV----LNADVCCdFPLQELLeFHkkhGASGTILGTEASRE--QASNYGCIVE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044928587 140 DPERFGVVEFddkghalsiEEKPTQPKSSYAVTGLYFYDNDVIKIAKAVKPSPRGELEITDINN 203
Cdd:cd06428   154 DPSTGEVLHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNN 208
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-201 5.74e-09

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 55.21  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTR--------LHPItLGvskqllpiydKPMIYYPISVLMLAGIREILLIsTPQDLPQYKQLLGDGSqfgieL 76
Cdd:cd02540     2 VILAAGKGTRmksdlpkvLHPL-AG----------KPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALANPN-----V 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  77 SYAEQPSPDGLAQAFLIGEEFI-GDDSVCLIL-GDnifhgqgfTPQLR---------KAAQQGKGATVFGYWVKDPERFG 145
Cdd:cd02540    65 EFVLQEEQLGTGHAVKQALPALkDFEGDVLVLyGD--------VPLITpetlqrlleAHREAGADVTVLTAELEDPTGYG 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044928587 146 VVEFDDKGHALSI-EEK---PTQPKSSYAVTGLYFYDNDVIKIA-KAVKPSP-RGELEITDI 201
Cdd:cd02540   137 RIIRDGNGKVLRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDI 198
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
3-53 1.37e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 54.09  E-value: 1.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2044928587   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI 53
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 5-210 2.59e-08

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 54.60  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFgielsyAEQPSP 84
Cdd:PRK14358   11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAF------ARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  85 DGLAQAFLIGEEFI--GDDSVCLILGDnifhgqgfTPQLRKAA---------QQGKGATVFGYWVKDPERFGVVEFDDKG 153
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGD--------TPLLRPDTlralvadhrAQGSAMTILTGELPDATGYGRIVRGADG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044928587 154 HALSIEEKPTQPKSSYAV----TGLYFYDNDVIKIAKAV-KPSPRGELEITDINNAYLNRGS 210
Cdd:PRK14358  154 AVERIVEQKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGGA 215
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-66 6.67e-08

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 52.06  E-value: 6.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044928587   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAG-IREILLISTPQDLPQYKQLL 66
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-69 2.18e-07

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: 50.60  E-value: 2.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044928587   5 IVLAGGSGTRLHpitLGVSKQLLPIYDKPMIYYPISVLM-LAGIREILLISTPQDLPQYKQLLGDG 69
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 4-181 1.32e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 49.05  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLHPITLGVSKQLLP---IYDkpMIYYPISVLMLAGIREILListpqdLPQYKqllgdgSQ--------- 71
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYV------LTQYK------SHsldrhisqt 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  72 ---FGIELSYAEqPSP----------DGLAQAFLIGEEFIGD---DSVCLILGDNIFHgQGFTPQLRKAAQQGKGATVFG 135
Cdd:PRK00844   74 wrlSGLLGNYIT-PVPaqqrlgkrwyLGSADAIYQSLNLIEDedpDYVVVFGADHVYR-MDPRQMVDFHIESGAGVTVAA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2044928587 136 YWV--KDPERFGVVEFDDKGHALSIEEKPTQPKS-------SYAVTGLYFYDNDV 181
Cdd:PRK00844  152 IRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDA 206
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 2-181 1.07e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 46.37  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   2 TKGIVLAGGSGTRLHPITLGVSKQLLPIYDK-PMIYYPISVLMLAGIREILLIStpqdlpQYK-----QLLGDG-----S 70
Cdd:PRK00725   16 TLALILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLT------QYKahsliRHIQRGwsffrE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  71 QFG--IELSYAEQPSPD-----GLAQAFLIGEEFIG--DDSVCLIL-GDNIFHgQGFTPQLRKAAQQGKGATVFGYWV-- 138
Cdd:PRK00725   90 ELGefVDLLPAQQRVDEenwyrGTADAVYQNLDIIRryDPKYVVILaGDHIYK-MDYSRMLADHVESGADCTVACLEVpr 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2044928587 139 KDPERFGVVEFDDKGHALSIEEKPTQPKS-------SYAVTGLYFYDNDV 181
Cdd:PRK00725  169 EEASAFGVMAVDENDRITAFVEKPANPPAmpgdpdkSLASMGIYVFNADY 218
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 4-109 1.96e-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: 44.47  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLhpitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGSQFGIELSYAEqps 83
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE--- 74

                          90       100
                  ....*....|....*....|....*...
gi 2044928587  84 pdGLAQAFLIGEEFIGDD-SVCLI-LGD 109
Cdd:cd04182    75 --GMSSSLAAGLEALPADaDAVLIlLAD 100
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-53 5.04e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 43.23  E-value: 5.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2044928587   1 MTKGIVLAGGSGTRLhpitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI 53
Cdd:COG2068     3 KVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV 50
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-65 5.25e-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: 5.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044928587   1 MTK---GIVLAGGSGTRlhpitLGVSKQLLPIYDKPMIYYPISVLMLAGIReiLLISTPQDlPQYKQL 65
Cdd:COG0746     1 MTMpitGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQVDE--VVIVANRP-ERYAAL 60
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 4-133 7.14e-05

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 42.18  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRlhpitLGVSKQLLPIYDKPMIYYpiSVLMLAGIREILLISTPqdlpqYKQLLGDGSQFGIElsYAEQPS 83
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLER--VLERLRPAGDEVVVVAN-----DEEVLAALAGLGVP--VVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2044928587  84 PD-GLAQAFLIGEEFIGDDSVCLIL-GDNIFHGQGFTPQLRKAAQQGKGATV 133
Cdd:pfam12804  67 PGqGPLAGLLAALRAAPGADAVLVLaCDMPFLTPELLRRLLAAAEESGADIV 118
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-201 1.03e-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: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTR--------LHPItLGvskqllpiydKPMIYYPISVLMLAGIREILLISTPQ-DlpQYKQLLGDgsqfgIE 75
Cdd:COG1207     6 VILAAGKGTRmksklpkvLHPL-AG----------KPMLEHVLDAARALGPDRIVVVVGHGaE--QVRAALAD-----LD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  76 LSYAEQPSPDGLAQAFLIGEEFI-GDDSVCLIL-GDnifhgqgfTPQLRKA---------AQQGKGATVFGYWVKDPERF 144
Cdd:COG1207    68 VEFVLQEEQLGTGHAVQQALPALpGDDGTVLVLyGD--------VPLIRAEtlkallaahRAAGAAATVLTAELDDPTGY 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044928587 145 GVVEFDDKGHALSI-EEK---PTQpkssYAV----TGLYFYDNDVIKIA-KAVKPS-PRGELEITDI 201
Cdd:COG1207   140 GRIVRDEDGRVLRIvEEKdatEEQ----RAIreinTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 4-91 1.23e-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: 42.14  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLHPITLGVSKQLLPI---YDkpMIYYPISVLMLAGIREILListpqdLPQYK--QLL----------GD 68
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGV------LTQYKsrSLNdhlgsgkewdLD 72

                          90       100
                  ....*....|....*....|....*..
gi 2044928587  69 GSQFGIELSYAEQ-PSPD---GLAQAF 91
Cdd:cd02508    73 RKNGGLFILPPQQrKGGDwyrGTADAI 99
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 7-56 1.71e-04

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: 41.41  E-value: 1.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2044928587   7 LAGGSGTRLHpitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTP 56
Cdd:COG2266     1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-53 3.70e-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: 41.05  E-value: 3.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI 53
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-166 4.58e-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: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYKQLLGDGsqfgiELSYAEQPSP 84
Cdd:PRK14355    7 IILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG-----DVSFALQEEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  85 DGLAQAFLIG-EEFIGDDSVCLIL-GDN-IFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALSI-EE 160
Cdd:PRK14355   79 LGTGHAVACAaPALDGFSGTVLILcGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158


                  ....*.
gi 2044928587 161 KPTQPK 166
Cdd:PRK14355  159 KDATPE 164
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-188 9.08e-04

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 39.93  E-value: 9.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYpiSVLMLAGIR--EILLI-----STPQDLPQYKQLLGDGSQFgIELs 77
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFdsRFIFIcrdehNTKFHLDESLKLLAPNATV-VEL- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  78 yaeQPSPDGLAQAFLIGEEFI-GDDSVCLILGDNIFHGqGFTPQLRKAAQQGKGATVFGYWVKDPeRFGVVEFDDKGHAL 156
Cdd:cd04183    78 ---DGETLGAACTVLLAADLIdNDDPLLIFNCDQIVES-DLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVI 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2044928587 157 SIEEKptQPKSSYAVTGLYFYDN--DVIKIAKAV 188
Cdd:cd04183   153 ETAEK--EPISDLATAGLYYFKSgsLFVEAAKKM 184
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-201 1.25e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.13  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   3 KGIVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLpqYKQLLGDgsqfgiELSYAEQP 82
Cdd:PRK14357    2 RALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPE------WVKIFLQE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  83 SPDGLAQAFLIGEEFIGDDSVCLIL-GDNIFHGQGFTPQLRKA-AQQGKGATVFGYWVKDPERFGVVeFDDKGHALSIEE 160
Cdd:PRK14357   71 EQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEhNRKGADVTILVADLEDPTGYGRI-IRDGGKYRIVED 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2044928587 161 K--PTQPKSSYAV-TGLYFYDND-VIKIAKAVKP-SPRGELEITDI 201
Cdd:PRK14357  150 KdaPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 5-70 1.81e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 38.97  E-value: 1.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044928587   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAG-IREILLISTPQDLPQYKQLLGDGS 70
Cdd:pfam01128   2 VIPAAGSGKRMGA---GVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAVSPDDTPEFRQLLGDPS 65
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 143-235 2.03e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.08  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587 143 RFGVVEFDDKGHALSIEEKPTQPKSSYAVTGLYFYDNDVIK---IAKAVKPSPR---GEleitDINNAYLNRGSLNVQLL 216
Cdd:PRK05293  161 RFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKeylIEDEKNPNSShdfGK----NVIPLYLEEGEKLYAYP 236

                          90
                  ....*....|....*....
gi 2044928587 217 GRGFaWLDTGTHDSLLEAS 235
Cdd:PRK05293  237 FKGY-WKDVGTIESLWEAN 254
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-161 2.52e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.07  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPqDLPQYKQLLgdgSQFGIELSYAEQPSP 84
Cdd:PRK14353    9 IILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAA---AKIAPDAEIFVQKER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  85 DGLAQAFLIGEEFI--GDDSVCLILGDNIFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDkGHALSI-EEK 161
Cdd:PRK14353   82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGRLIVKG-GRLVAIvEEK 160
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-65 3.48e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 37.86  E-value: 3.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044928587   1 MTKGIVLAGGSGTRLHpitlGVSKQLLPIYDKPMIYYPISVL--MLAGIreilLISTPQDLPQYKQL 65
Cdd:PRK00317    3 PITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERLapQVDEI----VINANRNLARYAAF 61
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-35 3.56e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 38.51  E-value: 3.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2044928587   1 MTKGIVLAGGSGTRLHPitlgVS-----KQLLPIY-DKPMI 35
Cdd:COG0836     2 MIYPVILAGGSGTRLWP----LSresypKQFLPLLgEKSLL 38
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 5-68 4.15e-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: 38.29  E-value: 4.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044928587   5 IVLAGGSGTRLhpiTLGVSKQLLPIYDKPMIYYPISVLMLAG-IREILLISTPQDLPQYKQLLGD 68
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 4-50 4.67e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 38.30  E-value: 4.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLHPITLGVSKQLLPI---YDkpMIYYPISVLMLAGIREI 50
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKI 53
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-209 5.78e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.89  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   5 IVLAGGSGTRL---HPitlgvsKQLLPIYDKPMIYYPISVLMLAGIREILLI-STPQDlpQYKQLLGDGSQFGIElsyAE 80
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVvGHGAE--EVKEVLGDRSEFALQ---EE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587  81 QPspdGLAQAFLIGEEFIGD-DSVCLIL-GDN-IFHGQGFTPQLRKAAQQGKGATVFGYWVKDPERFGVVEFDDKGHALS 157
Cdd:PRK14354   75 QL---GTGHAVMQAEEFLADkEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEK 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2044928587 158 I-EEK---PTQPKSSYAVTGLYFYDNDVIKIA-KAVKP-SPRGELEITDINNAYLNRG 209
Cdd:PRK14354  152 IvEQKdatEEEKQIKEINTGTYCFDNKALFEAlKKISNdNAQGEYYLTDVIEILKNEG 209
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-112 5.92e-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: 37.32  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044928587   4 GIVLAGGSGTRLhpitlgVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTpqDLPQYKQLLgdgSQFGIELSYAEQPS 83
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT--DSEEIADVA---KEFGAGVVMTSGSL 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2044928587  84 PDGLAQAFLIGEEFIG--DDSVCLILGDNIF 112
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNdhDDIIVNIQGDNPL 101
 
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.
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