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Conserved domains on  [gi|2766962721|ref|WP_363969998|]
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MULTISPECIES: glucose-1-phosphate thymidylyltransferase RfbA [unclassified Alcanivorax]

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];
9-297 3.28e-166

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 462.64  E-value: 3.28e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQ 88
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEK 168
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 169 PAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQAI 248
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2766962721 249 EQRQGLKIACLEEIAWCSGWITSEKLEKLIWQLGKTEYSGYLISLLQTK 297
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
9-297 3.28e-166

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 462.64  E-value: 3.28e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQ 88
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEK 168
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 169 PAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQAI 248
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2766962721 249 EQRQGLKIACLEEIAWCSGWITSEKLEKLIWQLGKTEYSGYLISLLQTK 297
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 10-295 1.44e-157

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: 440.68  E-value: 1.44e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQA 89
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  90 KPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEKP 169
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 170 AEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQAIE 249
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2766962721 250 QRQGLKIACLEEIAWCSGWITSEKLEKLIWQLGKTEYSGYLISLLQ 295
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 9-248 2.61e-141

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: 397.72  E-value: 2.61e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQ 88
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEK 168
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 169 PAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQAI 248
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 7-295 1.50e-111

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 324.32  E-value: 1.50e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   7 ENRKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYA 86
Cdd:PRK15480    2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  87 QQAKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLE 166
Cdd:PRK15480   82 VQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 167 EKPAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQ 246
Cdd:PRK15480  162 EKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2766962721 247 AIEQRQGLKIACLEEIAWCSGWITSEKLEKLIWQLGKTEYSGYLISLLQ 295
Cdd:PRK15480  242 TIEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 10-241 3.91e-82

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: 247.94  E-value: 3.91e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDK-PMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQ 88
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGGIAEVFEIAAEFIGDSPV-CLVLGDNIFYGQGFTPQLQAVAARQR--GATLFAYPVKEPERFGVVSLGAAGQVLRL 165
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2766962721 166 EEKPAEA-FSNLAVTGLYFFDNDVLD-LAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEA 241
Cdd:pfam00483 161 VEKPKLPkASNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEA 238
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
9-297 3.28e-166

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 462.64  E-value: 3.28e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQ 88
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEK 168
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 169 PAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQAI 248
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2766962721 249 EQRQGLKIACLEEIAWCSGWITSEKLEKLIWQLGKTEYSGYLISLLQTK 297
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 10-295 1.44e-157

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: 440.68  E-value: 1.44e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQA 89
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  90 KPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEKP 169
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 170 AEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQAIE 249
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2766962721 250 QRQGLKIACLEEIAWCSGWITSEKLEKLIWQLGKTEYSGYLISLLQ 295
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 9-248 2.61e-141

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: 397.72  E-value: 2.61e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQ 88
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEK 168
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 169 PAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQAI 248
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 7-295 1.50e-111

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 324.32  E-value: 1.50e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   7 ENRKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYA 86
Cdd:PRK15480    2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  87 QQAKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLE 166
Cdd:PRK15480   82 VQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 167 EKPAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEAGTLVQ 246
Cdd:PRK15480  162 EKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2766962721 247 AIEQRQGLKIACLEEIAWCSGWITSEKLEKLIWQLGKTEYSGYLISLLQ 295
Cdd:PRK15480  242 TIEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 10-241 3.91e-82

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: 247.94  E-value: 3.91e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDK-PMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQ 88
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGGIAEVFEIAAEFIGDSPV-CLVLGDNIFYGQGFTPQLQAVAARQR--GATLFAYPVKEPERFGVVSLGAAGQVLRL 165
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2766962721 166 EEKPAEA-FSNLAVTGLYFFDNDVLD-LAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGFVWLDAGTPESLLEA 241
Cdd:pfam00483 161 VEKPKLPkASNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEA 238
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 10-245 1.73e-65

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: 205.11  E-value: 1.73e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEdSGNYQRLFGDGSHLGMRFEYAQQA 89
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  90 KPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGqGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLgAAGQVLRLEEKP 169
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVV-DDGRIVRLVEKP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2766962721 170 AEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGtlqAEVLGR---GFvWLDAGTPESLLEAGTLV 245
Cdd:cd04189   159 KEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRG---RRVGYSivtGW-WKDTGTPEDLLEANRLL 233
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 10-257 2.32e-57

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


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 187.99  E-value: 2.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQQA 89
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  90 KPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGqGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEKP 169
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 170 AEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVL-----KAYQAQGTLqaeVLGRgfvWLDAGTPESLLEAGTL 244
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIqwlieKGYKVGGSK---VTGW---WKDTGKPEDLLDANRL 233

                         250
                  ....*....|....*
gi 2766962721 245 V--QAIEQRQGLKIA 257
Cdd:TIGR01208 234 IldEVEREVQGVDDE 248
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 11-233 2.64e-55

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: 178.16  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  11 GILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEdsGNY-QRLFGDGSHLGMRFEYAQQA 89
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYL--GEQiEEYFGDGSKFGVNIEYVVQE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  90 KPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGqGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRLEEKP 169
Cdd:cd04181    79 EPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2766962721 170 AEAFSNLAVTGLYFFDNDVLDLAKEVRPssRGEKEIVDVLKAYQAQGTLQAeVLGRGFvWLDAG 233
Cdd:cd04181   158 TLPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 10-241 3.94e-48

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: 160.70  E-value: 3.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTtpedsgNY-----QRLFGDGSHLGMRFE 84
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV------GYlaeqiEEYFGDGSRFGVRIT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  85 YAQQAKP----GGIAevfeIAAEFIGDSPVCLVLGDnIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAG 160
Cdd:COG1208    75 YVDEGEPlgtgGALK----RALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 161 QVLRLEEKPAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSrgekeIVDVLKAYQAQGTLQAEVLgRGFvWLDAGTPESLLE 240
Cdd:COG1208   150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFDYIPEGEPFD-----LEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLE 222


                  .
gi 2766962721 241 A 241
Cdd:COG1208   223 A 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 10-241 8.43e-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: 156.22  E-value: 8.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSgNYQRLFGDGSHLGMRFEYAQQA 89
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKE-KVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  90 KPGGIAEVFEIAAEFIGDSpvCLVL-GDNIFygqgfTPQLQAVAARQRGATLFAYPVKEPERFGVVSLgAAGQVLRLEEK 168
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDDE--FLVLnGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVET-DGGRVTGIVEK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2766962721 169 PAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGRGfvWLDAGTPESLLEA 241
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 9-241 3.89e-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: 3.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTP-----EDSGNY-----QRLFGDGSH 78
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiEDHFDRsyeleETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  79 ----------LGMRFEYAQQAKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGF-TPQLQAVAARQRGATLFAYPVKE 147
Cdd:cd02541    81 dlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYEKTGASVIAVEEVPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 148 PE--RFGVVSLGAAG----QVLRLEEKPA--EAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQ 219
Cdd:cd02541   161 EDvsKYGIVKGEKIDgdvfKVKGLVEKPKpeEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPVY 240

                         250       260
                  ....*....|....*....|...
gi 2766962721 220 AEVL-GRgfvWLDAGTPESLLEA 241
Cdd:cd02541   241 AYVFeGK---RYDCGNKLGYLKA 260
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 10-244 1.64e-23

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 96.13  E-value: 1.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTT--PEDSGNYQRLFGDgsHLGMRFEYAQ 87
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEYEK--KLGIKITFSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  88 QAKPGGIAEVFEIAAEFIGDSPVC-LVLGDNIFYGQGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAA-GQVLRL 165
Cdd:cd06425    80 ETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERF 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2766962721 166 EEKPAEAFSNLAVTGLYFFDNDVLDLAkEVRPSSRgEKEIvdvLKAYQAQGTLQAEVLgRGFvWLDAGTPESLLEAGTL 244
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVLDRI-PLRPTSI-EKEI---FPKMASEGQLYAYEL-PGF-WMDIGQPKDFLKGMSL 231
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
9-241 2.68e-20

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 88.17  E-value: 2.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTP-------------------EDSGNY 69
Cdd:COG1210     4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfdrsyeleatlEAKGKE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  70 QRLfgD---GSHLGMRFEYAQQAKP-G-GIAevfeI--AAEFIGDSPVCLVLGDNIFYGQ-GFTPQLQAVAARQRGATLF 141
Cdd:COG1210    84 ELL--EevrSISPLANIHYVRQKEPlGlGHA----VlcARPFVGDEPFAVLLGDDLIDSEkPCLKQMIEVYEETGGSVIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 142 AYPVKEPE--RFGVVSLGA-AGQVLRLE---EKPA--EAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVDVLKAYQ 213
Cdd:COG1210   158 VQEVPPEEvsKYGIVDGEEiEGGVYRVTglvEKPApeEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALA 237

                         250       260
                  ....*....|....*....|....*....
gi 2766962721 214 AQGTLQA-EVLGRgfvWLDAGTPESLLEA 241
Cdd:COG1210   238 KEEPVYAyEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 12-241 4.19e-17

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: 78.36  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  12 ILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTtpedsgNY-----QRLFGDGSHLGMRFEYA 86
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSV------GYlaeqiEEYFGDGYRGGIRIYYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  87 QQAKPGGIAEVFEIAAEFIGDsPVCLVL-GDNIFYGqGFTPQLQAVAARQRGATLFAYPVKEPERFGVVSLGAAGQVLRL 165
Cdd:cd06915    76 IEPEPLGTGGAIKNALPKLPE-DQFLVLnGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAF 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2766962721 166 EEKPAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRgekeiVDVLKAYQAQGTLQA-EVLGRgfvWLDAGTPESLLEA 241
Cdd:cd06915   154 VEKGPGAAPGLINGGVYLLRKEILAEIPADAFSLE-----ADVLPALVKRGRLYGfEVDGY---FIDIGIPEDYARA 222
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 10-241 2.55e-16

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: 76.07  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVlIVTTPEDSGNYQRLFGDgSHLGMRFEYAQQA 89
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTHHLADQIEAHLGD-SRFGLRITISDEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  90 KP-----GGIAEvfeiAAEFIGDSPVCLVLGDnIFYGQGFTPQLQAVAARQRGATLFAYPVKEPE--RFGVVSLGAAGQV 162
Cdd:cd06422    79 DElletgGGIKK----ALPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGhnGVGDFSLDADGRL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2766962721 163 LRleeKPAEAFSNLAVTGLYFFDNDVLDLAKEvRPSSrgekeIVDVLKAYQAQGTLQAEVLgRGFvWLDAGTPESLLEA 241
Cdd:cd06422   154 RR---GGGGAVAPFTFTGIQILSPELFAGIPP-GKFS-----LNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 12-241 3.71e-16

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: 75.63  E-value: 3.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  12 ILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIvttpedSGNYQR-----LFGDGSHLGMRFEYA 86
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYI------SVNYLAemiedYFGDGSKFGVNISYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  87 QQAKPGGIAEVFEIAAEFIgDSPVCLVLGDnIFYGQGFTPQLQAVAARQRGATLFA--YPVKEPerFGVVSLGaAGQVLR 164
Cdd:cd06426    76 REDKPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETE-GGRITS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 165 LEEKPAEAFsnLAVTGLYFFDNDVLDLAKEvrpssrGEK-EIVDVLKAYQAQGtlqaevlGRGFV------WLDAGTPES 237
Cdd:cd06426   151 IEEKPTHSF--LVNAGIYVLEPEVLDLIPK------NEFfDMPDLIEKLIKEG-------KKVGVfpiheyWLDIGRPED 215


                  ....
gi 2766962721 238 LLEA 241
Cdd:cd06426   216 YEKA 219
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 11-241 2.55e-13

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 69.33  E-value: 2.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  11 GILLAGGAGSRLHPATLGVSKhllpvydkPMAYY---------PMSALMLAGIRDVLIVTtpedSGNYQRLFgdgSHLGM 81
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT----QYKSHSLN---DHIGS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  82 RFEY-------------AQQAKPG-----GIAE-VFEIAaEFIGDSPVCLVL---GDNIF---YGQgftpqlqAVAA-RQ 135
Cdd:COG0448    69 GKPWdldrkrggvfilpPYQQREGedwyqGTADaVYQNL-DFIERSDPDYVLilsGDHIYkmdYRQ-------MLDFhIE 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 136 RGA--TLFAYPV--KEPERFGVVSLGAAGQVLRLEEKPAEAFSNLAVTGLYFFDNDVL-DLAKEVRPSSR---GEkeivD 207
Cdd:COG0448   141 SGAdiTVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVLiELLEEDAPNSShdfGK----D 216

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2766962721 208 VLKAYQAQGTLQAEVLgRGFvWLDAGTPESLLEA 241
Cdd:COG0448   217 IIPRLLDRGKVYAYEF-DGY-WRDVGTIDSYYEA 248
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
9-220 6.66e-12

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 64.93  E-value: 6.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   9 RKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTtpEDSGNYQRlfgdgSHLGMRFEY--- 85
Cdd:PRK13389    9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT--HSSKNSIE-----NHFDTSFELeam 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  86 -------------------------AQQAKPGGIAEVFEIAAEFIGDSPVCLVLGDNI---FYGQGFTPQLQAVAAR--Q 135
Cdd:PRK13389   82 lekrvkrqlldevqsicpphvtimqVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeYESDLSQDNLAEMIRRfdE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 136 RGAT-LFAYPVKEPERFGVVSL-------GAAGQVLRLEEKPA--EAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEI 205
Cdd:PRK13389  162 TGHSqIMVEPVADVTAYGVVDCkgvelapGESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQL 241

                         250
                  ....*....|....*
gi 2766962721 206 VDVLKAYQAQGTLQA 220
Cdd:PRK13389  242 TDAIDMLIEKETVEA 256
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 10-66 1.39e-11

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: 62.68  E-value: 1.39e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDS 66
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQ 58
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
8-223 1.21e-10

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 61.06  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   8 NRKGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTtpEDSGNYQRLFGDGSH--------- 78
Cdd:PRK10122    3 NLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT--HASKNAVENHFDTSYeleslleqr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  79 --------------LGMRFEYAQQAKPGGIAEVFEIAAEFIGDSPVCLVLGDNIFYGQGFTP---QLQAVAAR----QRG 137
Cdd:PRK10122   81 vkrqllaevqsicpPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPlryNLAAMIARfnetGRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 138 ATLFAYPVKEPERFGVVS----LGAAGQVLRL------EEKPAEAFSNLAVTGLYFFDNDVLDLAKEVRPSSRGEKEIVD 207
Cdd:PRK10122  161 QVLAKRMPGDLSEYSVIQtkepLDREGKVSRIvefiekPDQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240

                         250
                  ....*....|....*.
gi 2766962721 208 VLKAYQAQGTLQAEVL 223
Cdd:PRK10122  241 AIAELAKKQSVDAMLM 256
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 12-216 1.42e-09

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 58.45  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  12 ILLAGGAGSRLHPAtlgVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDSGNYQRLFGDGshlgmrFEYAQQAKP 91
Cdd:PRK14358   11 VILAAGQGTRMKSA---LPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  92 GGIAEVFEIAAEFI--GDSPVCLVLGDNIFYGqgfTPQLQAVAA--RQRGA--TLFAYPVKEPERFGVVSLGAAGQVLRL 165
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTPLLR---PDTLRALVAdhRAQGSamTILTGELPDATGYGRIVRGADGAVERI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2766962721 166 EEKPAEAFSNLAV----TGLYFFDNDVLDLAKEVRPSSR-GEKEIVDVLKAYQAQG 216
Cdd:PRK14358  159 VEQKDATDAEKAIgefnSGVYVFDARAPELARRIGNDNKaGEYYLTDLLGLYRAGG 214
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
10-61 3.89e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 56.02  E-value: 3.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVT 61
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 10-66 8.16e-09

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: 54.57  E-value: 8.16e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2766962721  10 KGILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPEDS 66
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQ 58
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 12-241 5.55e-08

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: 52.62  E-value: 5.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  12 ILLAGGAGSRLHPATLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTtpedsGnyqrlfgdgsHLGMRFEYAQQAKP 91
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT-----G----------YKKEQIEELLKKYP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  92 G------------GIAEVFEIAAEFIGDSpvCLVL-GDNIFYGQGFtpqLQAVAARQRGATLFAYPVKEPERFGVVSLGA 158
Cdd:cd02523    67 NikfvynpdyaetNNIYSLYLARDFLDED--FLLLeGDVVFDPSIL---ERLLSSPADNAILVDKKTKEWEDEYVKDLDD 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 159 AGQVLRLEEKPAEAFSNLAVT-GLYFFDND----VLDLAKEVRPSSRGEKEIVDVLKAYQAQGTLQAEVLGrGFVWLDAG 233
Cdd:cd02523   142 AGVLLGIISKAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEID 220


                  ....*...
gi 2766962721 234 TPESLLEA 241
Cdd:cd02523   221 DLEDLERA 228
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 144-241 8.79e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 49.87  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721 144 PVKEPERFGVVSLGAAGQVLRLEEKPAEAFSNLAVTGLYFFDNDVL---------------DLAKEVRPSSRGEKEivdV 208
Cdd:PRK05293  155 PWEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLkeyliedeknpnsshDFGKNVIPLYLEEGE---K 231

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2766962721 209 LKAYQAQGtlqaevlgrgfVWLDAGTPESLLEA 241
Cdd:PRK05293  232 LYAYPFKG-----------YWKDVGTIESLWEA 253
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 11-195 1.16e-05

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: 45.71  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  11 GILLAGGA--GSRLHPATLGVSKHLLPVYDKPMAYYPMSAL-MLAGIRDVLIVTTPEDSGNYQRLFGDGSHLGMRFEYAQ 87
Cdd:cd06428     1 AVILVGGPqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  88 QAKPGGIA----------------EVFEIAAEFIGDSPVCLVLGDNIFYGQGFTpqLQAVAARQRGATLFAYPVKEPErf 151
Cdd:cd06428    81 EYKPLGTAgglyhfrdqilagnpsAFFVLNADVCCDFPLQELLEFHKKHGASGT--ILGTEASREQASNYGCIVEDPS-- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2766962721 152 gvvslgaAGQVLRLEEKPAEAFSNLAVTGLYFFDNDVLDLAKEV 195
Cdd:cd06428   157 -------TGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKA 193
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 12-189 2.80e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 45.22  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  12 ILLAGGAGSRLHPATlgvskhllpvyD---KPMAYY---------PMSALMLAGIRDVLIVTtpedsgNYQ-----RLFG 74
Cdd:PRK00725   19 LILAGGRGSRLKELT-----------DkraKPAVYFggkfriidfALSNCINSGIRRIGVLT------QYKahsliRHIQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  75 DG-SHLGMRF-EY-----AQQAKPG-----GIAE-VFE-------IAAEFIgdspvcLVL-GDNIfYGQGFTPQLQAvaA 133
Cdd:PRK00725   82 RGwSFFREELgEFvdllpAQQRVDEenwyrGTADaVYQnldiirrYDPKYV------VILaGDHI-YKMDYSRMLAD--H 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2766962721 134 RQRGATL----FAYPVKEPERFGVVSLGAAGQVLRLEEKPAE-------AFSNLAVTGLYFFDNDVL 189
Cdd:PRK00725  153 VESGADCtvacLEVPREEASAFGVMAVDENDRITAFVEKPANppampgdPDKSLASMGIYVFNADYL 219
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-216 9.43e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 43.67  E-value: 9.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721   8 NRKGILLAGGAGSRLHpatlgvSKH---LLPVYDKPMAYYPMSALMLAGIRDVLIVTtpedsgnyqrlfGDGS-----HL 79
Cdd:PRK14354    2 NRYAIILAAGKGTRMK------SKLpkvLHKVCGKPMVEHVVDSVKKAGIDKIVTVV------------GHGAeevkeVL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  80 GMRFEYAQQAKPGGIAEVFEIAAEFIGDSP-VCLVL-GDNIFygqgFTPQ-LQAVAARQR----GATLFAYPVKEPERFG 152
Cdd:PRK14354   64 GDRSEFALQEEQLGTGHAVMQAEEFLADKEgTTLVIcGDTPL----ITAEtLKNLIDFHEehkaAATILTAIAENPTGYG 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2766962721 153 VVSLGAAGQVLRL-EEKPAEAFSnLAV----TGLYFFDNDVLDLA-KEVRP-SSRGEKEIVDVLKAYQAQG 216
Cdd:PRK14354  140 RIIRNENGEVEKIvEQKDATEEE-KQIkeinTGTYCFDNKALFEAlKKISNdNAQGEYYLTDVIEILKNEG 209
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-65 3.00e-04

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: 40.95  E-value: 3.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2766962721   1 MTMQFrenrKGILLAGGAGSRlhpatLGVSKHLLPVYDKPMAYYPMSALMLAgIRDVLIVTTPED 65
Cdd:COG0746     1 MTMPI----TGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPE 55
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 14-63 4.53e-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: 40.26  E-value: 4.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2766962721  14 LAGGAGSRLHpatlGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTP 63
Cdd:COG2266     1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 11-74 9.41e-04

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: 39.10  E-value: 9.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2766962721  11 GILLAGGAGSRlhpatLGVSKHLLPVYDKPMAYYPMSALMLAGiRDVLIVTTPEDSGNYQRLFG 74
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG 58
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 12-195 9.71e-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: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  12 ILLAGGAGSRLHPATLGVSKHLLPVYDKPMayYPMSALMLAGIRD---VLIVttpedsgnyqrLFGDGSHLGMRfEYAQQ 88
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPM--IEWVIESLAKIFDsrfIFIC-----------RDEHNTKFHLD-ESLKL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2766962721  89 AKPGgiAEVFEIAAEFIGdsPVCLVLG-----DN-----IFYG-QGFTPQLQAVAARQR-----GATLfayPVKEP-ERF 151
Cdd:cd04183    68 LAPN--ATVVELDGETLG--AACTVLLaadliDNddpllIFNCdQIVESDLLAFLAAFRerdldGGVL---TFFSShPRW 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2766962721 152 GVVSLGAAGQVLRLEEKpaEAFSNLAVTGLYFFDN--DVLDLAKEV 195
Cdd:cd04183   141 SYVKLDENGRVIETAEK--EPISDLATAGLYYFKSgsLFVEAAKKM 184
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
11-61 1.18e-03

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 39.37  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2766962721  11 GILLAGGAGSRlhpatLGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVT 61
Cdd:COG2068     6 AIILAAGASSR-----MGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVL 51
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 11-80 2.23e-03

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: 38.29  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2766962721  11 GILLAGGAGSRLHPATLGVSKHLLPVYDKpmaY----YPMSALMLAGIRDVLIVTtpedSGNYQRLFgdgSHLG 80
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR---YrlidFPLSNMVNSGIRNVGVLT----QYKSRSLN---DHLG 64
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 12-65 4.70e-03

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: 37.80  E-value: 4.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2766962721  12 ILLAGGAGSRLHpatLGVSKHLLPVYDKPMAYYPMSALMLAG-IRDVLIVTTPED 65
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDD 52
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 11-65 5.86e-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: 37.15  E-value: 5.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2766962721  11 GILLAGGAGSRLhpatlGVSKHLLPVYDKPMAYYPMSALMLAGIRDVLIVTTPED 65
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEA 52
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 12-65 8.52e-03

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: 36.73  E-value: 8.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2766962721  12 ILLAGGAGSRLHpatLGVSKHLLPVYDKPMAYYPMSALM-LAGIRDVLIVTTPED 65
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDD 55
 
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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