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Conserved domains on  [gi|2695982448|ref|WP_336275014|]
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glucose-1-phosphate thymidylyltransferase RfbA [Halomonas sp. DY715-9]

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];
3-292 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 560.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTI 242
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2695982448 243 EHRQGLKVACLEEIAWQQGWLSDEELRESATALAKTGYGQYLLHRLDAKG 292
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNR 290
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-292 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 560.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTI 242
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2695982448 243 EHRQGLKVACLEEIAWQQGWLSDEELRESATALAKTGYGQYLLHRLDAKG 292
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNR 290
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
4-285 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: 550.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQP 83
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  84 TPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEKP 163
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 164 AKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTIE 243
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2695982448 244 HRQGLKVACLEEIAWQQGWLSDEELRESATALAKTGYGQYLL 285
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLL 282
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
3-242 8.84e-177

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: 487.47  E-value: 8.84e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTI 242
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
3-285 7.18e-141

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 398.66  E-value: 7.18e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:PRK15480    4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:PRK15480   84 PSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTI 242
Cdd:PRK15480  164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2695982448 243 EHRQGLKVACLEEIAWQQGWLSDEELRESATALAKTGYGQYLL 285
Cdd:PRK15480  244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLL 286
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
4-239 4.04e-98

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 288.38  E-value: 4.04e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPV-CLVLGDNIFHGQHFSDQLKRASDQAS--GASVFGYLVKDPERFGVVEFDANGKAVSI 159
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 160 EEKPAKPKSP-YAVTGLYFYDNDVVE-IARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQ 237
Cdd:pfam00483 161 VEKPKLPKASnYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 2695982448 238 YV 239
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-292 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 560.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTI 242
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2695982448 243 EHRQGLKVACLEEIAWQQGWLSDEELRESATALAKTGYGQYLLHRLDAKG 292
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNR 290
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
4-285 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: 550.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQP 83
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  84 TPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEKP 163
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 164 AKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTIE 243
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2695982448 244 HRQGLKVACLEEIAWQQGWLSDEELRESATALAKTGYGQYLL 285
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLL 282
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
3-242 8.84e-177

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: 487.47  E-value: 8.84e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTI 242
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
3-285 7.18e-141

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 398.66  E-value: 7.18e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:PRK15480    4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:PRK15480   84 PSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQYVQTI 242
Cdd:PRK15480  164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2695982448 243 EHRQGLKVACLEEIAWQQGWLSDEELRESATALAKTGYGQYLL 285
Cdd:PRK15480  244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLL 286
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
4-239 4.04e-98

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 288.38  E-value: 4.04e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQ 82
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIGDAPV-CLVLGDNIFHGQHFSDQLKRASDQAS--GASVFGYLVKDPERFGVVEFDANGKAVSI 159
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 160 EEKPAKPKSP-YAVTGLYFYDNDVVE-IARQVKPSERGELEITSINNAYLERGDLHVERLGRGFAWLDTGTHDSLLEASQ 237
Cdd:pfam00483 161 VEKPKLPKASnYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 2695982448 238 YV 239
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
4-239 3.16e-68

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 212.04  E-value: 3.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILII--STPEDLPQYenlLGNGDSFGVRFEYAV 81
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgPTGEEIKEA---LGDGSRFGVRITYIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  82 QPTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHG---QHFSDQLKRASDqasgASVFGYLVKDPERFGVVEFDaNGKAVS 158
Cdd:cd04189    79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEgisPLVRDFLEEDAD----ASILLAEVEDPRRFGVAVVD-DGRIVR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 159 IEEKPAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGdLHVE-RLGRGFaWLDTGTHDSLLEASQ 237
Cdd:cd04189   154 LVEKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRG-RRVGySIVTGW-WKDTGTPEDLLEANR 231

                  ..
gi 2695982448 238 YV 239
Cdd:cd04189   232 LL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
5-227 1.58e-59

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 188.94  E-value: 1.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDlPQYENLLGNGDSFGVRFEYAVQPT 84
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  85 PDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGqHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEKPA 164
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2695982448 165 KPKSPYAVTGLYFYDNDVVEIARQVKPseRGELEITSINNAYLERGDLHVERLgrGFAWLDTG 227
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
4-239 1.85e-58

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: 190.69  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAVQP 83
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  84 TPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGqHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEKP 163
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2695982448 164 AKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGFaWLDTGTHDSLLEASQYV 239
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
4-239 3.70e-47

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


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 162.38  E-value: 3.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDlPQYENLLGNGDSFGVRFEYAVQP 83
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  84 TPDGLAQAFIIGEEFIGDApvCLVL-GDNIFHgqhfSDQLKRASDqASGASVFGYLVKDPERFGVVEFDaNGKAVSIEEK 162
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDDE--FLVLnGDVLLD----SDLLERLIR-AEAPAIAVVEVDDPSDYGVVETD-GGRVTGIVEK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2695982448 163 PAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGDLHVERLGRGfaWLDTGTHDSLLEASQYV 239
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
4-239 1.13e-45

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 154.16  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREIlIIST---PEDLPQYenlLGNGDSFGVRFEYA 80
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVgylAEQIEEY---FGDGSRFGVRITYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  81 VQPTP----DGLAQAfiigEEFIGDAPVCLVLGDNIFhGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKA 156
Cdd:COG1208    77 DEGEPlgtgGALKRA----LPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 157 VSIEEKPAKPKSPYAVTGLYFYDNDVVEIARqvkpsERGELEITSINNAYLERGDLHVERLgRGFaWLDTGTHDSLLEAS 236
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEAN 224

                  ...
gi 2695982448 237 QYV 239
Cdd:COG1208   225 ALL 227
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
3-236 5.07e-33

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: 121.87  E-value: 5.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTP-----EDL----PQYENLL-GNGD- 71
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiEDHfdrsYELEETLeKKGKt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  72 ---------SFGVRFEYAVQPTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHF-SDQLKRASDQaSGASVFGYLVKD 141
Cdd:cd02541    81 dlleevriiSDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYEK-TGASVIAVEEVP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 142 PE---RFGVVE-FDANGKAVSIE---EKPaKPK---SPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERGD 211
Cdd:cd02541   160 PEdvsKYGIVKgEKIDGDVFKVKglvEKP-KPEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238
                         250       260
                  ....*....|....*....|....*.
gi 2695982448 212 LHVERL-GRgfaWLDTGTHDSLLEAS 236
Cdd:cd02541   239 VYAYVFeGK---RYDCGNKLGYLKAT 261
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
6-235 1.13e-24

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: 98.74  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREIlIIST---PEdlpQYENLLGNGDSFGVRFEYAVQ 82
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVnylAE---MIEDYFGDGSKFGVNISYVRE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFIgDAPVCLVLGDnIFHGQHFSDQLKRASDQASGASVFG--YLVKDPerFGVVEFDaNGKAVSIE 160
Cdd:cd06426    78 DKPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETE-GGRITSIE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 161 EkpaKPKSPYAV-TGLYFYDNDVVEiarQVKPSERgeLEITSINNAYLERGdlhvERLG----RGFaWLDTGTHDSLLEA 235
Cdd:cd06426   153 E---KPTHSFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEG----KKVGvfpiHEY-WLDIGRPEDYEKA 219
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-235 8.19e-23

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 95.10  E-value: 8.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTP-----EDL--PQYE---NLLGNGD- 71
Cdd:COG1210     4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiEDHfdRSYEleaTLEAKGKe 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  72 ---------SFGVRFEYAVQPTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQ-HFSDQLKRASDQaSGASVFGylVK- 140
Cdd:COG1210    84 elleevrsiSPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkPCLKQMIEVYEE-TGGSVIA--VQe 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 141 -DPE---RFGVVEFDANGKAV----SIEEKPAKPKSP--YAVTGLYFYDNDVVEIARQVKPSERGELEITSINNAYLERG 210
Cdd:COG1210   161 vPPEevsKYGIVDGEEIEGGVyrvtGLVEKPAPEEAPsnLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEE 240
                         250       260
                  ....*....|....*....|....*.
gi 2695982448 211 DLHVERL-GRgfaWLDTGTHDSLLEA 235
Cdd:COG1210   241 PVYAYEFeGK---RYDCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
6-235 4.91e-21

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: 88.76  E-value: 4.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREIlIISTPEDLPQYENLLGNGDSFGVRFEYAVQPTP 85
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  86 DGLAQAFIIGEEFIGDaPVCLVL-GDNIFHGQhFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEKPA 164
Cdd:cd06915    81 LGTGGAIKNALPKLPE-DQFLVLnGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2695982448 165 KPKSPYAVTGLYFYDNDVVE-IARQVKPSERGELEitsinnAYLERGDLhverlgRGFA----WLDTGTHDSLLEA 235
Cdd:cd06915   159 GAAPGLINGGVYLLRKEILAeIPADAFSLEADVLP------ALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
4-238 6.76e-19

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 83.41  E-value: 6.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIRE-ILIIS-TPEDLPQYENLLgnGDSFGVRFEYAV 81
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEY--EKKLGIKITFSI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  82 QPTPDGLAQAFIIGEEFIGDAPVC-LVLGDNI-----------FHGQHFSDqlkrasdqasgASVFGYLVKDPERFGVVE 149
Cdd:cd06425    80 ETEPLGTAGPLALARDLLGDDDEPfFVLNSDVicdfplaelldFHKKHGAE-----------GTILVTKVEDPSKYGVVV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 150 FDAN-GKAVSIEEKPAKPKSPYAVTGLYFYDNDVVeiarqvkpsERGELEITSINN----AYLERGDLHVERLgRGFaWL 224
Cdd:cd06425   149 HDENtGRIERFVEKPKVFVGNKINAGIYILNPSVL---------DRIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WM 217
                         250
                  ....*....|....
gi 2695982448 225 DTGTHDSLLEASQY 238
Cdd:cd06425   218 DIGQPKDFLKGMSL 231
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-235 2.26e-17

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 78.77  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREIlIIST---PEdlpQYENLLGNgDSFGVRFEYA 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlAD---QIEAHLGD-SRFGLRITIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  81 VQP-----TPDGLAQAfiigEEFIGDAPVCLVLGDNIFHGqHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGK 155
Cdd:cd06422    76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDAD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 156 AVsIEEKPAKPKSPYAVTGLYFYDNDVVEIArqvkpsERGELEITSINNAYLERGDLHVERLgRGFaWLDTGTHDSLLEA 235
Cdd:cd06422   151 GR-LRRGGGGAVAPFTFTGIQILSPELFAGI------PPGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
4-59 1.38e-14

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 71.15  E-value: 1.38e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPED 59
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-200 5.36e-13

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 68.01  E-value: 5.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   3 RKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIIsTPEDLPQYENLLGNGDSFGVRFEYAV- 81
Cdd:PRK13389    9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKNSIENHFDTSFELEAMLEKRVk 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  82 ---------------------QPTPDGLAQAFIIGEEFIGDAPVCLVLGDNI-------FHGQHFSDQLKRAsDQASGAS 133
Cdd:PRK13389   88 rqlldevqsicpphvtimqvrQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeyesdLSQDNLAEMIRRF-DETGHSQ 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2695982448 134 VFGYLVKDPERFGVVefDANGKA---------VSIEEKPAKPKSP--YAVTGLYFYDNDVVEIARQVKPSERGELEIT 200
Cdd:PRK13389  167 IMVEPVADVTAYGVV--DCKGVElapgesvpmVGVVEKPKADVAPsnLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
4-200 6.00e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 64.91  E-value: 6.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIIS------------TPEDLPQY------EN 65
Cdd:PRK10122    5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkRQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  66 LLGNGDSF---GVRFEYAVQPTPDGLAQAFIIGEEFIGDAPVCLVLGDNIFHGQHfSDQLK--------RASDQASGASV 134
Cdd:PRK10122   85 LLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAS-ADPLRynlaamiaRFNETGRSQVL 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2695982448 135 FGYLVKDPERFGVVE----FDANGKAVSIE---EKPAKPK---SPYAVTGLYFYDNDVVEIARQVKPSERGELEIT 200
Cdd:PRK10122  164 AKRMPGDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
4-67 7.86e-12

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 63.43  E-value: 7.86e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLL 67
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLL 65
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
5-182 2.91e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 63.17  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKqllpiydkPMIYY---------PISVLMLAGIREILIistpedLPQYENL-----LGNG 70
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKSHslndhIGSG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  71 DSFGVRFE----YAVQP--TPD------GLAQAFIIGEEFIGDAPVCLVLgdnIFHGQH-----FSDQLKRAsdQASGAS 133
Cdd:COG0448    70 KPWDLDRKrggvFILPPyqQREgedwyqGTADAVYQNLDFIERSDPDYVL---ILSGDHiykmdYRQMLDFH--IESGAD 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2695982448 134 V-FGYL---VKDPERFGVVEFDANGKAVSIEEKPAKPKSPYAVTGLYFYDNDV 182
Cdd:COG0448   145 ItVACIevpREEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
6-225 2.08e-10

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: 59.55  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIIS--TPEdlpQYENLLgnGDSFGVRFEYAVQP 83
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgyKKE---QIEELL--KKYPNIKFVYNPDY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  84 TPDGLAQAFIIGEEFIGDaPVCLVLGDNIFHGQHFSDQLKRASDqasgASVFGYLVKDPERFGVVEFDANGKA-VSIEEK 162
Cdd:cd02523    77 AETNNIYSLYLARDFLDE-DFLLLEGDVVFDPSILERLLSSPAD----NAILVDKKTKEWEDEYVKDLDDAGVlLGIISK 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2695982448 163 PAKPKSPYAVT-GLYFYDND----VVEIARQVKPSERGELEITSINNAYLERGDLHVERLGrGFAWLD 225
Cdd:cd02523   152 AKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-54 3.17e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 59.10  E-value: 3.17e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2695982448   4 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILII 54
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
6-67 1.81e-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: 1.81e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2695982448   6 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPISVLMLAG-IREILIISTPEDLPQYENLL 67
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELL 60
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
6-77 2.06e-08

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: 53.68  E-value: 2.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2695982448   6 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPISVLM-LAGIREILIISTPEDLPQYENLLGNGDSFGVRF 77
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
6-210 2.29e-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: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIIsTPEDLPQYENLLGNGdsfGVRFeyAVQPTP 85
Cdd:PRK14358   11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVV-TGHGAEQVEAALQGS---GVAF--ARQEQQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  86 DGLAQAFIIGEEFI--GDAPVCLVLGDN-IFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKAVSIEEK 162
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2695982448 163 PAKPKSPYAV----TGLYFYDNDVVEIARQV-KPSERGELEITSINNAYLERG 210
Cdd:PRK14358  162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
6-67 6.87e-08

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 52.06  E-value: 6.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2695982448   6 IILAGGSGTRLHPitrGVSKQLLPIYDKPMIYYPISVLMLAG-IREILIISTPEDLPQYENLL 67
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
5-235 1.56e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 52.14  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKQLLP---IYDkpMIYYPISVLMLAGIREILIistpedLPQYE---------------NL 66
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYV------LTQYKshsldrhisqtwrlsGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  67 LGNgdsfgvrfeYaVQPTP----------DGLAQAFIIGEEFIGD-AP--VCLVLGDNIFHgQHFSDQLKRASDQASGAS 133
Cdd:PRK00844   80 LGN---------Y-ITPVPaqqrlgkrwyLGSADAIYQSLNLIEDeDPdyVVVFGADHVYR-MDPRQMVDFHIESGAGVT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 134 VFGYLV--KDPERFGVVEFDANGKAVSIEEKPAKPK----SP---YAVTGLYFYDNDV-VEIARQVKPSERGELEI-TSI 202
Cdd:PRK00844  149 VAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPglpdDPdeaLASMGNYVFTTDAlVDALRRDAADEDSSHDMgGDI 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2695982448 203 NNAYLERGDLHV------------ERlGRGFaWLDTGTHDSLLEA 235
Cdd:PRK00844  229 IPRLVERGRAYVydfstnevpgatER-DRGY-WRDVGTIDAYYDA 271
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
5-204 4.71e-07

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 49.94  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGG--SGTRLHPITRGVSKQLLPIYDKPMIYYPISVL-MLAGIREILIISTPEDLPQYENLLGNGDSFGVRFEYAV 81
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  82 QPTPDGLAQAF-----IIGEE-----FIGDAPVC--LVLGDNI-FHGQHFSDQL---KRASDQAsgASVFGYLVKDPERF 145
Cdd:cd06428    81 EYKPLGTAGGLyhfrdQILAGnpsafFVLNADVCcdFPLQELLeFHKKHGASGTilgTEASREQ--ASNYGCIVEDPSTG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2695982448 146 GVVEFdangkavsiEEKPAKPKSPYAVTGLYFYDNDVVEIARQVKPSERGELEITSINN 204
Cdd:cd06428   159 EVLHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNN 208
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
6-210 5.16e-07

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: 49.56  E-value: 5.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYpiSVLMLAGIRE---ILIIS----TPEDLPQYENLLGNGDSFgvrfe 78
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFICRdehnTKFHLDESLKLLAPNATV----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  79 YAVQPTPDGLAQAFIIGEEFI-GDAPVCLVLGDNIFHGQHFsDQLKRASDQASGASVFGYLVKDPeRFGVVEFDANGKAV 157
Cdd:cd04183    75 VELDGETLGAACTVLLAADLIdNDDPLLIFNCDQIVESDLL-AFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVI 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2695982448 158 SIEEKpaKPKSPYAVTGLYFYDN--DVVEIARQVKP---SERGELEITSINNAYLERG 210
Cdd:cd04183   153 ETAEK--EPISDLATAGLYYFKSgsLFVEAAKKMIRkddSVNGEFYISPLYNELILDG 208
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
5-236 1.34e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 49.10  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPISVLMLAGIREILIIStpedlpQYENLL-----GNGDSF----- 73
Cdd:PRK05293    6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT------QYQPLElnnhiGIGSPWdldri 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  74 --GVrfeYAVQPTPD--------GLAQAFIIGEEFIG--DAPVCLVL-GDNIFHgQHFSDQLK-RASDQASGA-SVFGYL 138
Cdd:PRK05293   80 ngGV---TILPPYSEseggkwykGTAHAIYQNIDYIDqyDPEYVLILsGDHIYK-MDYDKMLDyHKEKEADVTiAVIEVP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 139 VKDPERFGVVEFDANGKAVSIEEKPAKPKSPYAVTGLYFYDNDVVeiaRQVkpSERGELEITSINN-------AYLERGd 211
Cdd:PRK05293  156 WEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRL---KEY--LIEDEKNPNSSHDfgknvipLYLEEG- 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2695982448 212 lhvERLgrgFA------WLDTGTHDSLLEAS 236
Cdd:PRK05293  230 ---EKL---YAypfkgyWKDVGTIESLWEAN 254
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
5-134 4.09e-06

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: 46.38  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKQLLPI---YDkpMIYYPISVLMLAGIREILIistpedLPQYENL-----LGNGDSF--- 73
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGV------LTQYKSRslndhLGSGKEWdld 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2695982448  74 ----GVRFEYAVQ-PTPD---GLAQAFIIGEEFIGDAPVCLVLgdnIFHGQH-----FSDQLKRAsdQASGASV 134
Cdd:cd02508    73 rkngGLFILPPQQrKGGDwyrGTADAIYQNLDYIERSDPEYVL---ILSGDHiynmdYREMLDFH--IESGADI 141
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
8-58 1.28e-05

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 44.88  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2695982448   8 LAGGSGTRLhpitRGVSKQLLPIYDKPMIYYPISVLMLAGIREILII---STPE 58
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAvspNTPK 50
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
5-68 1.43e-05

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 44.49  E-value: 1.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2695982448   5 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPISVLMLAGiREILIISTPEDLPQYENLLG 68
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG 58
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-66 1.57e-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: 44.80  E-value: 1.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2695982448   1 MQRKGIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPISVLMLAGIReiLIISTPEDlPQYENL 66
Cdd:COG0746     3 MPITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQVDE--VVIVANRP-ERYAAL 60
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-182 2.76e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.21  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   1 MQRKGIILAGGSGTRL---HPitrgvsKQLLPIYDKPMIYYPISVLMLAGIREILIIstpedlpqyenlLGNG-----DS 72
Cdd:PRK14354    1 MNRYAIILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGaeevkEV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  73 FGVRFEYAVQPTPDGLAQAFIIGEEFIGDAP-VCLVL-GDN-IFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVE 149
Cdd:PRK14354   63 LGDRSEFALQEEQLGTGHAVMQAEEFLADKEgTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRII 142
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2695982448 150 FDANGKAVSI-EEKPAKPKSpYAV----TGLYFYDNDV 182
Cdd:PRK14354  143 RNENGEVEKIvEQKDATEEE-KQIkeinTGTYCFDNKA 179
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
6-168 3.22e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 44.83  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPISVLMLAGIREILIIStpedlpQYENL-----LGNGDSF--GVRF 77
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLT------QYKAHslirhIQRGWSFfrEELG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  78 EY-----AVQPTPD-----GLAQAF-----IIGEEfigDAPVCLVL-GDNIFHgQHFSDQLkrASDQASGASV-FGYL-- 138
Cdd:PRK00725   93 EFvdllpAQQRVDEenwyrGTADAVyqnldIIRRY---DPKYVVILaGDHIYK-MDYSRML--ADHVESGADCtVACLev 166
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2695982448 139 -VKDPERFGVVEFDANGKAVSIEEKPAKPKS 168
Cdd:PRK00725  167 pREEASAFGVMAVDENDRITAFVEKPANPPA 197
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
6-204 4.77e-05

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 43.66  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLH---PitrgvsKQLLPIYDKPMIYYPISVLMLAGIREILIIsTPEDLPQYENLLGNGDsfgvrFEYAVQ 82
Cdd:cd02540     2 VILAAGKGTRMKsdlP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALANPN-----VEFVLQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  83 PTPDGLAQAFIIGEEFI-----------GDAPvcLVLGDNIfhgQHFsdqLKRASDQASGASVFGYLVKDPERFGVVEFD 151
Cdd:cd02540    70 EEQLGTGHAVKQALPALkdfegdvlvlyGDVP--LITPETL---QRL---LEAHREAGADVTVLTAELEDPTGYGRIIRD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448 152 ANGKAVSI-EEKPAKP--KSPYAV-TGLY----------------------FYDNDVVEIARQ-------VKPSErgELE 198
Cdd:cd02540   142 GNGKVLRIvEEKDATEeeKAIREVnAGIYafdaeflfealpkltnnnaqgeYYLTDIIALAVAdglkvaaVLADD--EEE 219

                  ....*.
gi 2695982448 199 ITSINN 204
Cdd:cd02540   220 VLGVND 225
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
5-54 6.58e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 42.84  E-value: 6.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPISVLMLAGIREILII 54
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV 50
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
5-110 1.02e-04

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: 42.16  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQyENLLGNGDSFGVRFEYAVQpt 84
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAV-RAALAGLPVVVVINPDWEE-- 74
                          90       100
                  ....*....|....*....|....*...
gi 2695982448  85 pdGLAQAFIIG-EEFIGDAPVCLV-LGD 110
Cdd:cd04182    75 --GMSSSLAAGlEALPADADAVLIlLAD 100
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
5-54 2.31e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 42.15  E-value: 2.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKQLLPI---YDkpMIYYPISVLMLAGIREILII 54
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
4-36 3.85e-04

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 41.02  E-value: 3.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2695982448   4 KGIILAGGSGTRLHPITR-GVSKQLLPIY-DKPMI 36
Cdd:cd02509     2 YPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLL 36
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
6-204 6.02e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.00  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPeDLPQYENLLGngdSFGVRFEYAVQPTP 85
Cdd:PRK14353    9 IILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAAA---KIAPDAEIFVQKER 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  86 DGLAQAFIIGEEFI--GDAPVCLVLGDNIFHGQhfsDQLKRASDQ-ASGAS--VFGYLVKDPERFG--VVEfdaNGKAVS 158
Cdd:PRK14353   82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITA---ETLARLRERlADGADvvVLGFRAADPTGYGrlIVK---GGRLVA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2695982448 159 I-EEKPAKPKSpYAVT----GLY----------------------FYDNDVVEIAR----QVKPSERGELEITSINN 204
Cdd:PRK14353  156 IvEEKDASDEE-RAITlcnsGVMaadgadalalldrvgndnakgeYYLTDIVAIARaeglRVAVVEAPEDEVRGINS 231
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
5-54 7.60e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.64  E-value: 7.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPISVLMLAGIREILII 54
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
5-66 8.95e-04

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.48  E-value: 8.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2695982448   5 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPISvlMLAGIREILIISTPEDLPQYENL 66
Cdd:cd02503     3 GVILAGGKSRRM-----GGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
5-113 9.64e-04

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: 39.63  E-value: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLhpitrgVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTpeDLPQYENLLGNgdsFGVRFEYAVQPT 84
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT--DSEEIADVAKE---FGAGVVMTSGSL 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2695982448  85 PDGLAQAFIIGEEFIGDAP--VCLVLGDNIF 113
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNDHDdiIVNIQGDNPL 101
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
6-167 9.86e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.50  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448   6 IILAGGSGTRLhpiTRGVSKQLLPIYDKPMIYYPISVLMLAGIREILIISTPEDLPQYENLLGNGD-SFGVRFE-----Y 79
Cdd:PRK14355    7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDvSFALQEEqlgtgH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695982448  80 AV---QPTPDGLAQAFIIgeeFIGDAPvclvlgdnIFHGQHFSDQLKRASDQASGASVFGYLVKDPERFGVVEFDANGKA 156
Cdd:PRK14355   84 AVacaAPALDGFSGTVLI---LCGDVP--------LLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRV 152
                         170
                  ....*....|..
gi 2695982448 157 VSI-EEKPAKPK 167
Cdd:PRK14355  153 LRIvEEKDATPE 164
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-36 1.08e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.05  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2695982448   1 MQRKGIILAGGSGTRLHPITRGVS-KQLLPIY-DKPMI 36
Cdd:COG0836     1 SMIYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLL 38
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
6-69 1.51e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 39.83  E-value: 1.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2695982448   6 IILAGGSGTRLhpiTRGVSKQLLPIYDKPMIYYPISVLMLAG-IREILIISTPEDLPQYENLLGN 69
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
5-54 1.59e-03

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 39.13  E-value: 1.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2695982448   5 GIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPISVLMLAGIREILII 54
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
4-64 3.15e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 37.86  E-value: 3.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2695982448   4 KGIILAGGSGTRLHpitrGVSKQLLPIYDKPMIYYPISVL--MLAGIreilIISTPEDLPQYE 64
Cdd:PRK00317    5 TGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERLapQVDEI----VINANRNLARYA 59
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
6-40 9.90e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 37.28  E-value: 9.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2695982448   6 IILAGGSGTRLHPITrgvSKQLLPIYDKPMIYYPI 40
Cdd:PRK14359    6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYIL 37
 
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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