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Conserved domains on  [gi|928482255|gb|ALE87595|]
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glucose-1-phosphate thymidylyltransferase [Pseudomonas versuta]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-291 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 564.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEK 165
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 166 PSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTI 245
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 928482255 246 EQRQGLKVACLEEIAFNSGWITPDMLAVQAERFKKTGYGQYLLRLL 291
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-291 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 564.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEK 165
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 166 PSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTI 245
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 928482255 246 EQRQGLKVACLEEIAFNSGWITPDMLAVQAERFKKTGYGQYLLRLL 291
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 7-291 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: 561.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQP 86
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   87 SPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEKP 166
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  167 SKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTIE 246
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 928482255  247 QRQGLKVACLEEIAFNSGWITPDMLAVQAERFKKTGYGQYLLRLL 291
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-245 7.04e-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: 7.04e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEK 165
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 166 PSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTI 245
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 6-291 3.62e-151

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 424.86  E-value: 3.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:PRK15480   4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEK 165
Cdd:PRK15480  84 PSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 166 PSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTI 245
Cdd:PRK15480 164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 928482255 246 EQRQGLKVACLEEIAFNSGWITPDMLAVQAERFKKTGYGQYLLRLL 291
Cdd:PRK15480 244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-243 3.33e-100

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 293.78  E-value: 3.33e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   86 PSPDGLAQAFIIGEEFIGADPV-CLILGDNIFYGQHFSDNLRSAM--TQETGATVFGYHVSDPERFGVVEFDSRGRALSI 162
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIekAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  163 EEKPSKPK-SNYAVTGLYFYDNQVVE-IAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASH 240
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ...
gi 928482255  241 FVH 243
Cdd:pfam00483 241 FLL 243
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-291 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 564.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEK 165
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 166 PSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTI 245
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 928482255 246 EQRQGLKVACLEEIAFNSGWITPDMLAVQAERFKKTGYGQYLLRLL 291
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 7-291 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: 561.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQP 86
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   87 SPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEKP 166
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  167 SKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTIE 246
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 928482255  247 QRQGLKVACLEEIAFNSGWITPDMLAVQAERFKKTGYGQYLLRLL 291
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-245 7.04e-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: 7.04e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEK 165
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 166 PSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTI 245
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 6-291 3.62e-151

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 424.86  E-value: 3.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:PRK15480   4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEK 165
Cdd:PRK15480  84 PSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 166 PSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASHFVHTI 245
Cdd:PRK15480 164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 928482255 246 EQRQGLKVACLEEIAFNSGWITPDMLAVQAERFKKTGYGQYLLRLL 291
Cdd:PRK15480 244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-243 3.33e-100

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 293.78  E-value: 3.33e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQ 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   86 PSPDGLAQAFIIGEEFIGADPV-CLILGDNIFYGQHFSDNLRSAM--TQETGATVFGYHVSDPERFGVVEFDSRGRALSI 162
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIekAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  163 EEKPSKPK-SNYAVTGLYFYDNQVVE-IAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFAWLDTGTHDSLLEASH 240
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ...
gi 928482255  241 FVH 243
Cdd:pfam00483 241 FLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 7-242 8.15e-69

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 213.58  E-value: 8.15e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILII--STPEDlpcFKKLLGDGNRYGIELSYAE 84
Cdd:cd04189    2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgPTGEE---IKEALGDGSRFGVRITYIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  85 QPSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQhFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSrGRALSIEE 164
Cdd:cd04189   79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG-ISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD-GRIVRLVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928482255 165 KPSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGFaWLDTGTHDSLLEASHFV 242
Cdd:cd04189  157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-230 5.41e-60

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 190.10  E-value: 5.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPE-DLpcFKKLLGDGNRYGIELSYAEQP 86
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLgEQ--IEEYFGDGSKFGVNIEYVVQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  87 SPDGLAQAFIIGEEFIGADPVCLILGDNIFYGqHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEKP 166
Cdd:cd04181   79 EPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKP 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 928482255 167 SKPKSNYAVTGLYFYDNQVVEIAKKMKpsPRGELEITDVNRAYLEQNSLTVeMLGRGFaWLDTG 230
Cdd:cd04181  158 TLPESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 7-238 1.31e-59

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


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 193.77  E-value: 1.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGNRYGIELSYAEQP 86
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   87 SPDGLAQAFIIGEEFIGADPVCLILGDNIFYGqHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSIEEKP 166
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928482255  167 SKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRaYLEQNSLTVEMLGRGFAWLDTGTHDSLLEA 238
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQ-WLIEKGYKVGGSKVTGWWKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 7-239 1.37e-44

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: 155.83  E-value: 1.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDlPCFKKLLGDGNRYGIELSYAEQP 86
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   87 SPDGLAQAFIIGEEFIgADPVCLILGDNIFygqhfSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSrGRALSIEEKP 166
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEKP 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928482255  167 SKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVEMLGRGfaWLDTGTHDSLLEAS 239
Cdd:TIGR03992 154 ENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDAN 224
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-238 4.67e-43

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: 147.22  E-value: 4.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREIlIIST---PEDlpcFKKLLGDGNRYGIELSYA 83
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVgylAEQ---IEEYFGDGSRFGVRITYV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  84 EQPSP----DGLAQAfiigEEFIGADPVCLILGDnIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRA 159
Cdd:COG1208   77 DEGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 160 LSIEEKPSKPKSNYAVTGLYFYDNQVVEIAkkmkpsPRGE-LEITDVNRAYLEQNSLTVEMLgRGFaWLDTGTHDSLLEA 238
Cdd:COG1208  152 TRFVEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-239 4.97e-31

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 116.86  E-value: 4.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTP-----EDLpcF-------------- 66
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiEDH--Fdrsyeleetlekkg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  67 KKLLGDGNR---YGIELSYAEQPSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQHfsDNLRSAMT--QETGATVFGYH 141
Cdd:cd02541   79 KTDLLEEVRiisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKE--PCLKQLIEayEKTGASVIAVE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 142 VSDPE---RFGVVE-FDSRGRALSIE---EKPsKPK---SNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLE 211
Cdd:cd02541  157 EVPPEdvsKYGIVKgEKIDGDVFKVKglvEKP-KPEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLE 235

                        250       260
                 ....*....|....*....|....*....
gi 928482255 212 QNS-LTVEMLGRgfaWLDTGTHDSLLEAS 239
Cdd:cd02541  236 EEPvYAYVFEGK---RYDCGNKLGYLKAT 261
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 6-238 4.60e-26

UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273443 [Multi-domain]  Cd Length: 260  Bit Score: 103.59  E-value: 4.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIIS-----TPED-------LPCfkKLLGDG 73
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTgrgkrAIEDhfdysyeLEH--QLEKRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   74 NRYGIE----------LSYAEQPSPDGLAQAFIIGEEFIGADPVCLILGDNIFygQHFSDNLRSAMT--QETGATVFGYH 141
Cdd:TIGR01099  79 KEELLEevrkisnlatIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIV--VNEEPALKQMIKayEKTGCSIIAVQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  142 VSDPE---RFGVVEF----DSRGRALSIEEKPSK--PKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLE- 211
Cdd:TIGR01099 157 EVPKEevsKYGVIDGegieKDLYKVKNMVEKPKPeeAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLEn 236

                         250       260
                  ....*....|....*....|....*..
gi 928482255  212 QNSLTVEMLGRGFawlDTGTHDSLLEA 238
Cdd:TIGR01099 237 ETVLAYKFNGKRY---DCGSKLGYLEA 260
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 9-238 6.43e-21

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


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 88.72  E-value: 6.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREIlIIST---PEDLpcfKKLLGDGNRYGIELSYAEQ 85
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVnylAEMI---EDYFGDGSKFGVNISYVRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  86 PSPDGLAQAFIIGEEFIGaDPVCLILGDnIFYGQHFSDNLRSAMTQETGATVFG--YHVSDPerFGVVEFDSrGRALSIE 163
Cdd:cd06426   78 DKPLGTAGALSLLPEKPT-DPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETEG-GRITSIE 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928482255 164 EKPSKpksNYAV-TGLYFYDNQVVEIAkkmkpsPRGE-LEITDVNRAYLEQNSLTVEMLGRGFaWLDTGTHDSLLEA 238
Cdd:cd06426  153 EKPTH---SFLVnAGIYVLEPEVLDLI------PKNEfFDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 9-238 1.29e-20

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


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 87.99  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREIL---------IIStpedlpcfkkLLGDGNRYGIE 79
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVlsvgylaeqIEE----------YFGDGYRGGIR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  80 LSYAEQPSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQhFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRA 159
Cdd:cd06915   72 IYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 160 LSIEEKPSKPKSNYAVTGLYFYDNQVVEIAKKMKPSprgeLEiTDVNRAYLEQNSLtvemlgRGFA----WLDTGTHDSL 235
Cdd:cd06915  151 IAFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDY 219


                 ...
gi 928482255 236 LEA 238
Cdd:cd06915  220 ARA 222
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-238 2.01e-20

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 88.55  E-value: 2.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYplSV--LMLAGMREILIISTP-----ED---------------- 62
Cdd:COG1210    4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiEDhfdrsyeleatleakg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  63 -LPCFKKLLGDGNryGIELSYAEQPSPDGLAQAFIIGEEFIGADPVCLILGDNIFYGQhfsdnlRSAMTQ------ETGA 135
Cdd:COG1210   82 kEELLEEVRSISP--LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE------KPCLKQmievyeETGG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 136 TVFG-YHVSDPE--RFGVVEF-DSRGRALSIE---EKPSKPK--SNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVN 206
Cdd:COG1210  154 SVIAvQEVPPEEvsKYGIVDGeEIEGGVYRVTglvEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAI 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 928482255 207 RAYL-EQNSLTVEMLGRgfaWLDTGTHDSLLEA 238
Cdd:COG1210  234 AALAkEEPVYAYEFEGK---RYDCGDKLGYLKA 263
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 7-186 4.32e-20

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 86.50  E-value: 4.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMRE-ILIIS-TPEDLPCFKKLLGDgnRYGIELSYAE 84
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFSI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  85 QPSPDGLAQAFIIGEEFIGADPVC-LILGDNIFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFD-SRGRALSI 162
Cdd:cd06425   80 ETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDeNTGRIERF 159

                        170       180
                 ....*....|....*....|....
gi 928482255 163 EEKPSKPKSNYAVTGLYFYDNQVV 186
Cdd:cd06425  160 VEKPKVFVGNKINAGIYILNPSVL 183
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
6-218 9.78e-15

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 73.02  E-value: 9.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIIS------------TPEDLPCF------K 67
Cdd:PRK13389   9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEAMlekrvkR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  68 KLLGDGNRY---GIELSYAEQPSPDGLAQAFIIGEEFIGADPVCLILGDNIF--YGQHFS-DNLrSAMTQ---ETGAT-V 137
Cdd:PRK13389  89 QLLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSqDNL-AEMIRrfdETGHSqI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 138 FGYHVSDPERFGVVefDSRGRAL---------SIEEKP--SKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVN 206
Cdd:PRK13389 168 MVEPVADVTAYGVV--DCKGVELapgesvpmvGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAI 245

                        250
                 ....*....|..
gi 928482255 207 RAYLEQNslTVE 218
Cdd:PRK13389 246 DMLIEKE--TVE 255
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-238 5.70e-14

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: 69.52  E-value: 5.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREIlIIST---PEDLpcfKKLLGDgNRYGIELSYA 83
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlADQI---EAHLGD-SRFGLRITIS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  84 EQP-----SPDGLAQAfiigEEFIGADPVCLILGDnIFYGQHFSDNLRSAMTQETG--ATVFGYHVSDPERFGVVEFDSR 156
Cdd:cd06422   76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDAllLLLPLVRNPGHNGVGDFSLDAD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 157 GRalsIEEKPSKPKSNYAVTGLYFYDNQVVEIAkkmkpsPRGELEITDVNRAYLEQNSLTVEMLgRGFaWLDTGTHDSLL 236
Cdd:cd06422  151 GR---LRRGGGGAVAPFTFTGIQILSPELFAGI------PPGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLL 219


                 ..
gi 928482255 237 EA 238
Cdd:cd06422  220 AA 221
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 7-62 6.64e-14

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 69.22  E-value: 6.64e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 928482255   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPED 62
Cdd:cd04198    2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 8-182 1.12e-13

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 70.49  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGGSGTRLHPLTLGVSKQMLPI---Y---DkpmiFyPLSVLMLAGMREILIIsTPedlpcFKKL-----LGDGNRY 76
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFggkYriiD----F-PLSNCVNSGIRRVGVL-TQ-----YKSHslndhIGSGKPW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  77 -------GIELSYAEQPSPD-----GLAQAFIIGEEFI---GADPVcLIL-GDNIF---YGQ----HfsdnlrsamtQET 133
Cdd:COG0448   73 dldrkrgGVFILPPYQQREGedwyqGTADAVYQNLDFIersDPDYV-LILsGDHIYkmdYRQmldfH----------IES 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 928482255 134 GA--TVFGYHVSDPE--RFGVVEFDSRGRALSIEEKPSKPKSNYAVTGLYFYD 182
Cdd:COG0448  142 GAdiTVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
4-204 1.65e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 69.53  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   4 IKRKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIIS------------TPEDLPCF----- 66
Cdd:PRK10122   2 TNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrv 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  67 -KKLLGDGNRY---GIELSYAEQPSPDGLAQAFIIGEEFIGADPVCLILGDnIFYGQHFSDNLR---SAMT---QETG-A 135
Cdd:PRK10122  82 kRQLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPD-VVIDDASADPLRynlAAMIarfNETGrS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 136 TVFGYHVS-DPERFGVVE----FDSRGRALSIE---EKPSKPK---SNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITD 204
Cdd:PRK10122 161 QVLAKRMPgDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 7-57 5.42e-11

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 61.12  E-value: 5.42e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 928482255   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILII 57
Cdd:cd02507    2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 9-218 3.33e-09

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: 56.09  E-value: 3.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIIS--TPEdlpCFKKLLGDgnRYGIELSYAEQP 86
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgyKKE---QIEELLKK--YPNIKFVYNPDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  87 SPDGLAQAFIIGEEFIGaDPVCLILGDNIFYGQHfsdnLRSAMTQETGATVFgyhVSDPERFGVVEFD----SRGRALSI 162
Cdd:cd02523   77 AETNNIYSLYLARDFLD-EDFLLLEGDVVFDPSI----LERLLSSPADNAIL---VDKKTKEWEDEYVkdldDAGVLLGI 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928482255 163 EEKPSKPKSNYAVT-GLYFYDNQ----VVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVE 218
Cdd:cd02523  149 ISKAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVK 209
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
7-57 5.18e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 55.63  E-value: 5.18e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 928482255   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREILII 57
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 8-218 9.17e-09

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 54.95  E-value: 9.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGG--SGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVL-MLAGMREILIISTPEDLPcFKKLLGDGNR-YGIELSYA 83
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQQeFNVPIRYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  84 EQPSPDGLA---------------QAFIIgeefIGADPVC-LILGDNI-FYGQHfsDNLRSAMTQE---TGATVFGYHVS 143
Cdd:cd06428   80 QEYKPLGTAgglyhfrdqilagnpSAFFV----LNADVCCdFPLQELLeFHKKH--GASGTILGTEasrEQASNYGCIVE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928482255 144 DPerfgvvefdSRGRALSIEEKPSKPKSNYAVTGLYFYDNQVVEIAKKMKPSPRGELEITDVNRAYLEQNSLTVE 218
Cdd:cd06428  154 DP---------STGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 9-80 9.29e-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: 51.76  E-value: 9.29e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928482255   9 IILAGGSGTRLHpltLGVSKQMLPIYDKPMIFYPLSVLM-LAGMREILIISTPEDLPCFKKLLGDGNRYGIEL 80
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-74 3.03e-07

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 50.13  E-value: 3.03e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928482255   9 IILAGGSGTRLHpltLGVSKQMLPIYDKPMIFYPLSVLMLAG-MREILIISTPEDLPCFKKLLGDGN 74
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAKYG 64
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 8-143 3.00e-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: 46.77  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGGSGTRLHPLTLGVSKQMLPI---YDkpMIFYPLSVLMLAGMREILII------STPEDLPCFKKLLGDGNRYGI 78
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLtqyksrSLNDHLGSGKEWDLDRKNGGL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928482255  79 ELSYAEQ-PSPD---GLAQAFIIGEEFI---GADPVCLILGDNIfYGQHFSDNLRSAmtQETGATV-FGYHVS 143
Cdd:cd02508   79 FILPPQQrKGGDwyrGTADAIYQNLDYIersDPEYVLILSGDHI-YNMDYREMLDFH--IESGADItVVYKAS 148
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
9-70 4.11e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.67  E-value: 4.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928482255   9 IILAGGSGTRLHPltlGVSKQMLPIYDKPMIFYPLSVLMLAG-MREILIISTPEDLPCFKKLL 70
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 8-239 5.11e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 47.17  E-value: 5.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREILI--------------ISTPEDLpcfkkllgD 72
Cdd:PRK05293   6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVltqyqplelnnhigIGSPWDL--------D 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  73 GNRYGIEL--SYAEQPSPD---GLAQAFIIGEEFIG-ADP-VCLIL-GDNIfYGQHFSDNLRSAMTQETGATVFGYHVSD 144
Cdd:PRK05293  78 RINGGVTIlpPYSESEGGKwykGTAHAIYQNIDYIDqYDPeYVLILsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEVPW 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255 145 PE--RFGVVEFDSRGRALSIEEKPSKPKSNYAVTGLYFYD----NQVVEIAKKMKPSPR--GEleitDVNRAYLEQNSLT 216
Cdd:PRK05293 157 EEasRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNwkrlKEYLIEDEKNPNSSHdfGK----NVIPLYLEEGEKL 232

                        250       260
                 ....*....|....*....|...
gi 928482255 217 VEMLGRGFaWLDTGTHDSLLEAS 239
Cdd:PRK05293 233 YAYPFKGY-WKDVGTIESLWEAN 254
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-137 5.44e-06

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: 45.65  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255    8 GIILAGGSGTRlhpltLGVSKQMLPIYDKPMIFYPLSVLMLAGmREILIISTPEDLPCFKKLLGdgnrygieLSYAEQPS 87
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 928482255   88 PD-----GLAQAFiigEEFIGADPVCLILGDNIFYGQHFSDNLRSAMTQETGATV 137
Cdd:pfam12804  67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 9-205 9.22e-06

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: 45.97  E-value: 9.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   9 IILAGGSGTR--------LHPLtLGvskqmlpiydKPMIFYPL-SVLMLAGMREILIISTPEDLpcFKKLLGDGNrygie 79
Cdd:cd02540    2 VILAAGKGTRmksdlpkvLHPL-AG----------KPMLEHVLdAARALGPDRIVVVVGHGAEQ--VKKALANPN----- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  80 LSYAEQPSPDGLAQAFIIGEEFIGADP-VCLILgdnifYG----------QHFSDNLRSAmtqETGATVFGYHVSDPERF 148
Cdd:cd02540   64 VEFVLQEEQLGTGHAVKQALPALKDFEgDVLVL-----YGdvplitpetlQRLLEAHREA---GADVTVLTAELEDPTGY 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928482255 149 GVVEFDSRGRALSI-EEK---PSKPKSNYAVTGLYFYDNQVVEIA-KKMKPSP-RGELEITDV 205
Cdd:cd02540  136 GRIIRDGNGKVLRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDI 198
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 9-171 3.74e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 44.83  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIF-YPLSVLMLAGMREILIISTpedlpcFK-----KLLGDG--------N 74
Cdd:PRK00725  19 LILAGGRGSRLKELTDKRAKPAVYFGGKFRIIdFALSNCINSGIRRIGVLTQ------YKahsliRHIQRGwsffreelG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  75 RYgIELSYAEQPSPD-----GLAQAF-----IIGEEfiGADPVcLIL-GDNIfYGQHFSDNLRSAMtqETGA--TVFGYH 141
Cdd:PRK00725  93 EF-VDLLPAQQRVDEenwyrGTADAVyqnldIIRRY--DPKYV-VILaGDHI-YKMDYSRMLADHV--ESGAdcTVACLE 165

                        170       180       190
                 ....*....|....*....|....*....|..
gi 928482255 142 VSDPE--RFGVVEFDSRGRALSIEEKPSKPKS 171
Cdd:PRK00725 166 VPREEasAFGVMAVDENDRITAFVEKPANPPA 197
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 8-171 4.25e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.43  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGGSGTRLHPLTLGVSKQMLP---IYDkpMIFYPLSVLMLAGMREILIistpedLPCFKK---------------L 69
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYV------LTQYKShsldrhisqtwrlsgL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  70 LGdgnRYgIELSYAEQP--------SPDGLAQAF-IIGEEfiGADPVCLILGDNIfYGQHFSDNLRSAMTQETGATVFGY 140
Cdd:PRK00844  80 LG---NY-ITPVPAQQRlgkrwylgSADAIYQSLnLIEDE--DPDYVVVFGADHV-YRMDPRQMVDFHIESGAGVTVAAI 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 928482255 141 HV--SDPERFGVVEFDSRGRALSIEEKPSKPKS 171
Cdd:PRK00844 153 RVprEEASAFGVIEVDPDGRIRGFLEKPADPPG 185
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-205 5.44e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 44.37  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   7 KGIILAGGSGTRLHPltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLpcFKKLLGDgnrygiELSYAEQP 86
Cdd:PRK14357   2 RALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPE------WVKIFLQE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  87 SPDGLAQAFIIGEEFIGADPVCLIL-GDNIFYGQHFSDNL-RSAMTQETGATVFGYHVSDPERFGVVEFDSrGRALSIEE 164
Cdd:PRK14357  71 EQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLiEEHNRKGADVTILVADLEDPTGYGRIIRDG-GKYRIVED 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 928482255 165 K--PSKPKSNYAV-TGLYFYD-NQVVEIAKKMKP-SPRGELEITDV 205
Cdd:PRK14357 150 KdaPEEEKKIKEInTGIYVFSgDFLLEVLPKIKNeNAKGEYYLTDA 195
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 11-83 1.17e-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: 42.18  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  11 LAGGSGTRLHpltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDlPCFKKLL---------GDGNRYGIELS 81
Cdd:COG2266    1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNT-PKTREYLkergvevieTPGEGYVEDLN 75


                 ..
gi 928482255  82 YA 83
Cdd:COG2266   76 EA 77
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 8-113 1.59e-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: 41.78  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGGSGTRLhpltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPcFKKLLGDGNRYGIELSYAEQps 87
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADA-VRAALAGLPVVVVINPDWEE-- 74

                         90       100
                 ....*....|....*....|....*...
gi 928482255  88 pdGLAQAFIIGEEFIGAD-PVCLI-LGD 113
Cdd:cd04182   75 --GMSSSLAAGLEALPADaDAVLIlLAD 100
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
8-113 3.16e-04

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 40.91  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   8 GIILAGGSGTRLhpltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIIsTPEDLPCFKKLLGDgnrYGIELSYAEQPS 87
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LGADAEEVAAALAG---LGVRVVVNPDWE 76

                         90       100
                 ....*....|....*....|....*...
gi 928482255  88 pDGLAQAFIIGEEFI--GADPVCLILGD 113
Cdd:COG2068   77 -EGMSSSLRAGLAALpaDADAVLVLLGD 103
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 9-72 7.23e-04

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: 40.60  E-value: 7.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928482255   9 IILAGGSGTRLhplTLGVSKQMLPIYDKPMIFYPLSVLMLAG-MREILIISTPEDLPCFKKLLGD 72
Cdd:PRK09382   9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 8-38 9.72e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.22  E-value: 9.72e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 928482255   8 GIILAGGSGTRLHPLTLGVSKQMLPI---Y---DKPM 38
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYrliDIPM 42
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-170 1.10e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   9 IILAGGSGTRLHPltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREILIISTPEDLPCFKKLLGDGnryGIELSYAEQPSP 88
Cdd:PRK14355   7 IILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG---DVSFALQEEQLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  89 DGLAQAFIIGEEFIGADPVCLILGDN-IFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSRGRALSI-EEKP 166
Cdd:PRK14355  81 TGHAVACAAPALDGFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEEKD 160


                 ....
gi 928482255 167 SKPK 170
Cdd:PRK14355 161 ATPE 164
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-62 1.32e-03

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: 39.02  E-value: 1.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928482255   1 MTTiKRKGIILAGGSGTRlhpltLGVSKQMLPIYDKPMIFYPLSVLMLAGMReiLIISTPED 62
Cdd:COG0746    1 MTM-PITGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQVDE--VVIVANRP 54
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 8-57 2.75e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 39.10  E-value: 2.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 928482255   8 GIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREILII 57
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 8-59 2.75e-03

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


Pssm-ID: 396773  Cd Length: 217  Bit Score: 38.47  E-value: 2.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 928482255    8 GIILAGGSGTRLhPLtlgvsKQMLPIYDKPMIFYPLSVLMLAGMREILIIST 59
Cdd:pfam02348   2 AIIPARLGSKRL-PG-----KNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT 47
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 7-39 3.80e-03

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 38.33  E-value: 3.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 928482255   7 KGIILAGGSGTRLHPLtlgvS-----KQMLPIY-DKPMI 39
Cdd:cd02509    2 YPVILAGGSGTRLWPL----SresypKQFLKLFgDKSLL 36
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
5-39 4.00e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 38.12  E-value: 4.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 928482255   5 KRKGIILAGGSGTRLHPLtlgvS-----KQMLPIY-DKPMI 39
Cdd:COG0836    2 MIYPVILAGGSGTRLWPL----SresypKQFLPLLgEKSLL 38
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-205 5.07e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.27  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255   5 KRKGIILAGGSGTRL---HPltlgvsKQMLPIYDKPMIFYPLSVLMLAGMREILII--STPEDLpcfKKLLGDGNRYGIE 79
Cdd:PRK14354   2 NRYAIILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVvgHGAEEV---KEVLGDRSEFALQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928482255  80 lsyAEQPspdGLAQAFIIGEEFI-GADPVCLIL-GDN-IFYGQHFSDNLRSAMTQETGATVFGYHVSDPERFGVVEFDSR 156
Cdd:PRK14354  73 ---EEQL---GTGHAVMQAEEFLaDKEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 928482255 157 GRALSI-EEKPSKPKS------NyavTGLYFYDNQV-VEIAKKMKP-SPRGELEITDV 205
Cdd:PRK14354 147 GEVEKIvEQKDATEEEkqikeiN---TGTYCFDNKAlFEALKKISNdNAQGEYYLTDV 201
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 7-63 6.21e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 37.09  E-value: 6.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 928482255   7 KGIILAGGSGTRLHpltlGVSKQMLPIYDKPMIFYplsVLM-LAGMREILIISTPEDL 63
Cdd:PRK00317   5 TGVILAGGRSRRMG----GVDKGLQELNGKPLIQH---VIErLAPQVDEIVINANRNL 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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