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Conserved domains on  [gi|1731150939|ref|WP_148409044|]
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glucose-1-phosphate thymidylyltransferase RfbA [Murimonas intestini]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

sugar nucleotidyltransferase such as glucose-1-phosphate thymidylyltransferase, which catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis

CATH:  3.90.550.10
EC:  2.7.7.-
Gene Ontology:  GO:0016779|GO:0046872|GO:0000271
PubMed:  9445404|12691742
SCOP:  4000694

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 534.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 161 PEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAAF 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1731150939 241 QKRQGLYISCIEEIAYRQRFINKEQLIELAQPLLKTEYGKYLVEVAE 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 534.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 161 PEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAAF 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1731150939 241 QKRQGLYISCIEEIAYRQRFINKEQLIELAQPLLKTEYGKYLVEVAE 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-287 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: 519.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQE 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  82 QPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 162 EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAAFQ 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1731150939 242 KRQGLYISCIEEIAYRQRFINKEQLIELAQPLLKTEYGKYLVEVAE 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-239 9.76e-167

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: 461.66  E-value: 9.76e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731150939 161 PEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAA 239
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQT 239
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-289 7.70e-144

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 405.98  E-value: 7.70e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  82 QPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 162 EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAAFQ 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1731150939 242 KRQGLYISCIEEIAYRQRFINKEQLIELAQPLLKTEYGKYLVEVAEGL 289
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 7.73e-95

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: 279.91  E-value: 7.73e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDK-PMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSV-ALILGDNIFYGQSFSKILKKVASRES--GATIFGYYVRDPREYGVVEFDEEGNALSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 158 EEKPEQPK-SNYAVPGLYFYDNDVIE-IAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAAD 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 1731150939 236 FVA 238
Cdd:pfam00483 241 FLL 243
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 534.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 161 PEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAAF 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1731150939 241 QKRQGLYISCIEEIAYRQRFINKEQLIELAQPLLKTEYGKYLVEVAE 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-287 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: 519.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQE 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  82 QPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 162 EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAAFQ 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1731150939 242 KRQGLYISCIEEIAYRQRFINKEQLIELAQPLLKTEYGKYLVEVAE 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-239 9.76e-167

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: 461.66  E-value: 9.76e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731150939 161 PEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAA 239
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQT 239
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-289 7.70e-144

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 405.98  E-value: 7.70e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  82 QPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 162 EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAADFVAAFQ 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1731150939 242 KRQGLYISCIEEIAYRQRFINKEQLIELAQPLLKTEYGKYLVEVAEGL 289
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 7.73e-95

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: 279.91  E-value: 7.73e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDK-PMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSV-ALILGDNIFYGQSFSKILKKVASRES--GATIFGYYVRDPREYGVVEFDEEGNALSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 158 EEKPEQPK-SNYAVPGLYFYDNDVIE-IAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFAWLDTGNHDALLDAAD 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 1731150939 236 FVA 238
Cdd:pfam00483 241 FLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-233 3.55e-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: 213.97  E-value: 3.55e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDI-LIISTPRDLpvFKDLFGTGEQLGLNMSYAV 79
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIgIVVGPTGEE--IKEALGDGSRFGVRITYIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  80 QEQPRGLADAFIVGEEFIGDDSVALILGDNIFYGqSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDeEGNALSIEE 159
Cdd:cd04189    79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVE 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731150939 160 KPEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFaWLDTGNHDALLDA 233
Cdd:cd04189   157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEA 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-225 7.79e-64

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: 199.73  E-value: 7.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   3 GIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDlPVFKDLFGTGEQLGLNMSYAVQEQ 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  83 PRGLADAFIVGEEFIGDDSVALILGDNIFYGqSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEKPE 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731150939 163 QPKSNYAVPGLYFYDNDVIEIAKNVKPsaRGEIEITSVNNEYLRRGTLKVETLgrGFAWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-233 4.38e-57

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


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 186.84  E-value: 4.38e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQE 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  82 QPRGLADAFIVGEEFIGDDSVALILGDNIFYGqSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731150939 162 EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGFaWLDTGNHDALLDA 233
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-233 6.89e-52

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: 174.70  E-value: 6.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVfKDLFGTGEQLGLNMSYAVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKV-REYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIgDDSVALILGDNIFYGQSFSKILkkvasRESGATIFGYYVRDPREYGVVEFDEeGNALSIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731150939 161 PEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGRGfaWLDTGNHDALLDA 233
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDA 223
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-233 2.50e-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: 147.99  E-value: 2.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDIlIISTpRDLP-VFKDLFGTGEQLGLNMSYAVQ 80
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINV-GYLAeQIEEYFGDGSRFGVRITYVDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  81 EQPRGLADAFIVGEEFIGDDSVALILGDnIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEK 160
Cdd:COG1208    79 GEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731150939 161 PEQPKSNYAVPGLYFYDNDVIE-IAKNVKPSargeieITSVNNEYLRRGTLKVETLgRGFaWLDTGNHDALLDA 233
Cdd:COG1208   158 PEEPPSNLINAGIYVLEPEIFDyIPEGEPFD------LEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-233 7.82e-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: 121.49  E-value: 7.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIIsTPRDLPVFKDLFGTGEQL--------- 71
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIV-TGRGKRAIEDHFDRSYELeetlekkgk 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  72 ------------GLNMSYAVQEQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSfsKILKKVASR--ESGATIFGYYV 137
Cdd:cd02541    80 tdlleevriisdLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKE--PCLKQLIEAyeKTGASVIAVEE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 138 RDPRE---YGVVEFDE-EGNALSIE---EKP--EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRG 208
Cdd:cd02541   158 VPPEDvskYGIVKGEKiDGDVFKVKglvEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEE 237
                         250       260
                  ....*....|....*....|....*.
gi 1731150939 209 T-LKVETLGRgfaWLDTGNHDALLDA 233
Cdd:cd02541   238 PvYAYVFEGK---RYDCGNKLGYLKA 260
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-198 8.39e-27

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 105.88  E-value: 8.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYplsI---LMLAGIRDILIIsTPRDLPVFKDLF------------- 65
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY---VveeAVAAGIEEIIFV-TGRGKRAIEDHFdrsyeleatleak 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  66 GTGEQL--------GLNMSYAVQEQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQsfSKILKKV--ASRESGATIFGy 135
Cdd:COG1210    81 GKEELLeevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQMieVYEETGGSVIA- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731150939 136 yVRD-PRE----YGVVEFDE-EGNALSIE---EKP--EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEIT 198
Cdd:COG1210   158 -VQEvPPEevskYGIVDGEEiEGGVYRVTglvEKPapEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLT 230
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-233 6.97e-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: 88.34  E-value: 6.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDIlIISTPRDLPVFKDLFGTGEQLGLNMSYAVQEQP 83
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  84 RGLADAFIVGEEFIgDDSVALILGDnIFYGQSFSKILKKVASRESGATIFG--YYVRDPreYGVVEFDeEGNALSIEEKP 161
Cdd:cd06426    81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETE-GGRITSIEEKP 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731150939 162 EQpksNYAV-PGLYFYDNDVIE-IAKNVKpsargeIEITSVNNEYLRRGtlkvETLG----RGFaWLDTGNHDALLDA 233
Cdd:cd06426   156 TH---SFLVnAGIYVLEPEVLDlIPKNEF------FDMPDLIEKLIKEG----KKVGvfpiHEY-WLDIGRPEDYEKA 219
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-226 4.94e-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: 4.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRD-ILIIS-TPRDLPVFKDLFgtGEQLGLNMSYA 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEY--EKKLGIKITFS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  79 VQEQPRGLADAFIVGEEFIGDDSVA-LILGDNIFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEE-GNALS 156
Cdd:cd06425    79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIER 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731150939 157 IEEKPEQPKSNYAVPGLYFYDNDVIEiaknvkpsaRGEIEITSVNNE----YLRRGTLKVETLgRGFaWLDTGN 226
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVLD---------RIPLRPTSIEKEifpkMASEGQLYAYEL-PGF-WMDIGQ 221
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-190 9.67e-17

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


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 77.21  E-value: 9.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDIlIISTPRDLPVFKDLFGTGEQLGLNMSYAVQEQP 83
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  84 RGLADAFIVGEEFIGDDSVALILGDNIFYGqSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEKPEQ 163
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159
                         170       180
                  ....*....|....*....|....*..
gi 1731150939 164 PKSNYAVPGLYFYDNDVIEIAKNVKPS 190
Cdd:cd06915   160 AAPGLINGGVYLLRKEILAEIPADAFS 186
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 9.43e-16

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 75.70  E-value: 9.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVfKDLFGTGEQL--------- 71
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAV-ENHFDTSYELeslleqrvk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  72 -------------GLNMSYAVQEQPRGLADAFIVGEEFIGDDSVALILGDNIFYGQSFSKILKKVAS-----RESG-ATI 132
Cdd:PRK10122   83 rqllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAmiarfNETGrSQV 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731150939 133 FGYYVR-DPREYGVVE----FDEEGNALSIE---EKPEQPK---SNYAVPGLYFYDNDVIEIAKNVKPSARGEIEIT 198
Cdd:PRK10122  163 LAKRMPgDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-198 1.51e-15

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 75.33  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIIsTPRDLPVFKDLFGTGEQLGLNMSYAVQE 81
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKNSIENHFDTSFELEAMLEKRVKR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  82 Q----------------------PRGLADAFIVGEEFIGDDSVALILGDNIF--YGQSFSKI-LKKVASR--ESGAT-IF 133
Cdd:PRK13389   89 QlldevqsicpphvtimqvrqglAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQDnLAEMIRRfdETGHSqIM 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731150939 134 GYYVRDPREYGVVefDEEGNAL---------SIEEKP--EQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEIT 198
Cdd:PRK13389  169 VEPVADVTAYGVV--DCKGVELapgesvpmvGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-57 2.07e-15

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 73.46  E-value: 2.07e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRD 57
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-180 3.81e-14

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 71.64  E-value: 3.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   3 GIILAGGSGTRLYPLTKSISkqimpvydKPMIYY---------PLSILMLAGIRDILIIsTPrdlpvFK-----DLFGTG 68
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRA--------KPAVPFggkyriidfPLSNCVNSGIRRVGVL-TQ-----YKshslnDHIGSG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  69 EQLGLNMSY-------AVQEQP-----RGLADAFIVGEEFIGD---DSVaLIL-GDNIfYGQSFSKILKkvASRESGA-- 130
Cdd:COG0448    70 KPWDLDRKRggvfilpPYQQREgedwyQGTADAVYQNLDFIERsdpDYV-LILsGDHI-YKMDYRQMLD--FHIESGAdi 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1731150939 131 TIFgyYVRDPRE----YGVVEFDEEGNALSIEEKPEQPKSNYAVPGLYFYDNDV 180
Cdd:COG0448   146 TVA--CIEVPREeasrFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-216 3.21e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 66.39  E-value: 3.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLypltKS-ISKQIMPVYDKPMIYYPLSILMLAGIRDILIIstprdlpvfkdlFGTG-----EQLGLNMSY 77
Cdd:PRK14354    6 IILAAGKGTRM----KSkLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGaeevkEVLGDRSEF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  78 AVQEQPRGLADAFIVGEEFIGDDS--VALILGDN-IFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNA 154
Cdd:PRK14354   70 ALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEV 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731150939 155 LSI-EEK---PEQPKSNYAVPGLYFYDNDVI-EIAKNVKP-SARGE------IEItsVNNEYLRRGTLKV----ETLG 216
Cdd:PRK14354  150 EKIvEQKdatEEEKQIKEINTGTYCFDNKALfEALKKISNdNAQGEyyltdvIEI--LKNEGEKVGAYQTedfeESLG 225
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-202 5.46e-12

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: 64.07  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLypltKS-ISKQIMPVYDKPMIYYPLSILMLAGIRDILIIsTPRDLPVFKDLFGtgeqlGLNMSYAVQEQ 82
Cdd:cd02540     2 VILAAGKGTRM----KSdLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALA-----NPNVEFVLQEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  83 PRGLADAFIVGEEFI-GDDSVALILgdnifYG-------QSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNA 154
Cdd:cd02540    72 QLGTGHAVKQALPALkDFEGDVLVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKV 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731150939 155 LSI-EEK---PEQPKSN------YAVPG--LY--------------FYDNDVIEIAKNVKPSAR-----GEIEITSVNN 202
Cdd:cd02540   147 LRIvEEKdatEEEKAIRevnagiYAFDAefLFealpkltnnnaqgeYYLTDIIALAVADGLKVAavladDEEEVLGVND 225
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-52 5.51e-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: 63.81  E-value: 5.51e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILII 52
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
4-266 2.14e-10

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 60.76  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLyplTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGeqlglnMSYAVQEQP 83
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  84 RGLADAFIVGEEFI--GDDSVALILGDN-IFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSIEEK 160
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 161 PEQPKSNYAV----PGLYFYDNDVIEIAKNV-KPSARGEIEITSVNNEYlRRGTLKVetlgRGFAWLDTgnhDALLDAAD 235
Cdd:PRK14358  162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLY-RAGGAQV----RAFKLSDP---DEVLGAND 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1731150939 236 fvaafqkRQGLyiscIEEIAYRQRFINKEQL 266
Cdd:PRK14358  234 -------RAGL----AQLEATLRRRINEAHM 253
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-223 1.02e-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: 57.24  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDlPVFKDLFGTGEQLGL---------N 74
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKKYPNIKFvynpdyaetN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  75 MSYAVQeqprgladafiVGEEFIGDDSVaLILGDNIFYgqsfSKILKKVASRESGATIFgyyVRDPREYGVVEFDE---- 150
Cdd:cd02523    81 NIYSLY-----------LARDFLDEDFL-LLEGDVVFD----PSILERLLSSPADNAIL---VDKKTKEWEDEYVKdldd 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731150939 151 EGNALSIEEKPEQPKSNYAVP-GLYFYDND----VIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVETLGrGFAWLD 223
Cdd:cd02523   142 AGVLLGIISKAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-132 1.86e-09

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: 56.40  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   3 GIILAGGSGTRLYPLTKSISKQIMPV---YDkpMIYYPLSILMLAGIRDILIISTPRDLPVFK--------DLFGTGEql 71
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLTQYKSRSLNDhlgsgkewDLDRKNG-- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731150939  72 GLNMSYAVQEQP----RGLADAFIVGEEFIGDDSV--ALILGDNIFYGQSFSKILKKvaSRESGATI 132
Cdd:cd02508    77 GLFILPPQQRKGgdwyRGTADAIYQNLDYIERSDPeyVLILSGDHIYNMDYREMLDF--HIESGADI 141
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-163 6.61e-09

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 56.19  E-value: 6.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLypltKS-ISKQIMPVYDKPMIYYPLSILMLAGIRDILIIstprdlpvfkdlFGTG-EQL-----GLNMS 76
Cdd:COG1207     6 VILAAGKGTRM----KSkLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGaEQVraalaDLDVE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  77 YAVQEQPRGLADAFIVGEEFI-GDDSVALILgdnifYG-------QSFSKILKKVASRESGATIFGYYVRDPREYGVVEF 148
Cdd:COG1207    70 FVLQEEQLGTGHAVQQALPALpGDDGTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVR 144
                         170
                  ....*....|....*....
gi 1731150939 149 DEEGNALSI-EEK---PEQ 163
Cdd:COG1207   145 DEDGRVLRIvEEKdatEEQ 163
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-52 7.21e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 54.86  E-value: 7.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILII 52
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-214 1.76e-08

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: 54.18  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   3 GIILAGG--SGTRLYPLTKSISKQIMPVYDKPMIYYPLS-ILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAV 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEaCAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  80 QEQPRGLADAFIVGEEFI--GDDSVALILGDNIFYGQSFSKILKKVASRESGATIFGYYVR--DPREYG-VVEFDEEGNA 154
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQIlaGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASreQASNYGcIVEDPSTGEV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939 155 LSIEEKPEQPKSNYAVPGLYFYDNDVIEIAKNVKPSARGEIEITSVNNEYLRRGTLKVET 214
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQ 220
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-174 2.07e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 54.49  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPLTKSISKQIMPVYDK-PMIYYPLSILMLAGIRDILIISTPRDLPVFKDLfGTGEQLGLNM---- 75
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHI-GIGSPWDLDRingg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  76 -----SYAVQEQPR---GLADAFIVGEEFIG--DDSVALIL-GDNIfYGQSFSKILKKVASRESGATIFGYYVrdPRE-- 142
Cdd:PRK05293   83 vtilpPYSESEGGKwykGTAHAIYQNIDYIDqyDPEYVLILsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEV--PWEea 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1731150939 143 --YGVVEFDEEGNALSIEEKPEQPKSNYAVPGLY 174
Cdd:PRK05293  160 srFGIMNTDENMRIVEFEEKPKNPKSNLASMGIY 193
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-166 6.58e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 53.29  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   3 GIILAGGSGTRLYPLTKSISKQIMP---VYDkpMIYYPLSILMLAGIRDILI------------ISTPRDLPVFKDLFGT 67
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhISQTWRLSGLLGNYIT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  68 geqlglnmsyAVQEQPR-------GLADAFIVGEEFIGD---DSVALILGDNIfYGQSFSKILKkvASRESGA--TIFGy 135
Cdd:PRK00844   86 ----------PVPAQQRlgkrwylGSADAIYQSLNLIEDedpDYVVVFGADHV-YRMDPRQMVD--FHIESGAgvTVAA- 151
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1731150939 136 yVRDPRE----YGVVEFDEEGNALSIEEKPEQPKS 166
Cdd:PRK00844  152 -IRVPREeasaFGVIEVDPDGRIRGFLEKPADPPG 185
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-213 1.23e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 52.46  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLypltKS-ISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLpvfkdlfgTGEQLGLNMSYAV 79
Cdd:PRK14357    1 MRALVLAAGKGTRM----KSkIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--------VKKLLPEWVKIFL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  80 QEQPRGLADAFIVGEEFIGDDSVALIL-GDNIFYGQ-SFSKILKKVASRESGATIFGYYVRDPREYGVVeFDEEGNALSI 157
Cdd:PRK14357   69 QEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISEnTLKRLIEEHNRKGADVTILVADLEDPTGYGRI-IRDGGKYRIV 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731150939 158 EEK--PEQPKSNYAV-PGLYFYDND-VIEIAKNVKP-SARGEIEITSVNNEYLRRGTLKVE 213
Cdd:PRK14357  148 EDKdaPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAVNFAEKVRVVKTE 208
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
4-172 1.74e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 51.77  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLYPLTKSISKQIMPVYDK-PMIYYPLSILMLAGIRDILIIST-----------------PRDLPVFKDLF 65
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQykahslirhiqrgwsffREELGEFVDLL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  66 GTGEQLGLNMSYavqeqpRGLADAF-----IVGEEfigDDSVALIL-GDNIfYGQSFSKILKkvASRESGA--TIFGYYV 137
Cdd:PRK00725   99 PAQQRVDEENWY------RGTADAVyqnldIIRRY---DPKYVVILaGDHI-YKMDYSRMLA--DHVESGAdcTVACLEV 166
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1731150939 138 rdPRE----YGVVEFDEEGNALSIEEKPEQPKsnyAVPG 172
Cdd:PRK00725  167 --PREeasaFGVMAVDENDRITAFVEKPANPP---AMPG 200
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-51 2.20e-07

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: 50.65  E-value: 2.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1731150939   2 KGIILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYPLSILMLAGIRDILI 51
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV 50
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
3-162 5.87e-07

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 50.24  E-value: 5.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   3 GIILAGGSGTRLYPLTKSISKQIMPV---YDkpMIYYPLSILMLAGIRDILII----ST----------PRDLPVFkdlF 65
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLtqfnSAslnrhlsrayNFGNGGN---F 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  66 GTG--EQLGLNMSYAVQEQPRGLADA---FI-VGEEF-IGDDSVALIL-GDNIfYGQSFSKILKKvaSRESGA--TIFGY 135
Cdd:PLN02241   81 GDGfvEVLAATQTPGEKGWFQGTADAvrqFLwLFEDAkNKNVEEVLILsGDHL-YRMDYMDFVQK--HRESGAdiTIACL 157
                         170       180
                  ....*....|....*....|....*....
gi 1731150939 136 YVRDPR--EYGVVEFDEEGNALSIEEKPE 162
Cdd:PLN02241  158 PVDESRasDFGLMKIDDTGRIIEFSEKPK 186
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
3-161 8.63e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 49.88  E-value: 8.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   3 GIILAGGSGTRLYPLTKSISKQIMPVYDK-PMIYYPLSILMLAGIRDILII------STPRDLP---VFkDLFGTG--EQ 70
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLtqfnsaSLNRHISqtyNF-DGFSGGfvEV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  71 LglnmsyAVQEQP------RGLADAFIVGEEFIGDDSV--ALIL-GDNIfYGQSFSKILKKvaSRESGA--TIFGYYV-- 137
Cdd:PRK02862   85 L------AAQQTPenpswfQGTADAVRKYLWHFQEWDVdeYLILsGDQL-YRMDYRLFVQH--HRETGAdiTLAVLPVde 155
                         170       180
                  ....*....|....*....|....
gi 1731150939 138 RDPREYGVVEFDEEGNALSIEEKP 161
Cdd:PRK02862  156 KDASGFGLMKTDDDGRITEFSEKP 179
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-213 1.33e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 49.36  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLypltKS-ISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLFGTGEqlglnMSYAVQEQ 82
Cdd:PRK14355    7 IILAAGKGTRM----KSdLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  83 PRGLADAFIVG-EEFIGDDSVALIL-GDN-IFYGQSFSKILKKVASRESGATIFGYYVRDPREYGVVEFDEEGNALSI-E 158
Cdd:PRK14355   78 QLGTGHAVACAaPALDGFSGTVLILcGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvE 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731150939 159 EK---PEQPKSNYAVPGLYFYDNDVIEIA-KNVK-PSARGEIEITSV----NNEYLRRGTLKVE 213
Cdd:PRK14355  158 EKdatPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIvamaAAEGLRCLAFPVA 221
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-34 1.92e-05

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: 45.26  E-value: 1.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1731150939   1 MKGIILAGGSGTRLYPL-TKSISKQIMPVY-DKPMI 34
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLL 36
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-64 2.14e-05

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: 44.44  E-value: 2.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731150939   4 IILAGGSGTRlypLTKSISKQIMPVYDKPMIYYPLSILM-LAGIRDILIISTPRDLPVFKDL 64
Cdd:cd02516     4 IILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKEL 62
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-212 2.57e-05

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: 44.55  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLYPLTKSISKQIMPVYDKPMIYYplSILMLAGIRDILIISTPRDLPVFKDLFGTGEQLGLNMSYAVQEQP 83
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDSRFIFICRDEHNTKFHLDESLKLLAPNATVVELDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939  84 --RGLADAFIVGEEFI-GDDSVALILGDNIFYGQSFSKILKKVASRESGAtIFGYYVRDPReYGVVEFDEEGNALSIEEK 160
Cdd:cd04183    80 etLGAACTVLLAADLIdNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGG-VLTFFSSHPR-WSYVKLDENGRVIETAEK 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1731150939 161 peQPKSNYAVPGLYFYDN--DVIEIAKNV-KPSAR--GEIEITSVNNEYLRRGtLKV 212
Cdd:cd04183   158 --EPISDLATAGLYYFKSgsLFVEAAKKMiRKDDSvnGEFYISPLYNELILDG-KKV 211
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-64 5.53e-05

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: 43.19  E-value: 5.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731150939   4 IILAGGSGTRlypLTKSISKQIMPVYDKPMIYYPLSILMLAG-IRDILIISTPRDLPVFKDL 64
Cdd:COG1211     1 IIPAAGSGSR---MGAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEEL 59
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-94 6.70e-05

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 43.90  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   1 MKGIILAGGSGTRLYPL-TKSISKQIMPVY-DKPMI---YypLSILMLAGIRDILIIstprdlpvfkdlfgTGEQLglnm 75
Cdd:COG0836     3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLLqqtV--ERLAGLVPPENILVV--------------TNEEH---- 62
                          90
                  ....*....|....*....
gi 1731150939  76 SYAVQEQPRGLADAFIVGE 94
Cdd:COG0836    63 RFLVAEQLPELGPANILLE 81
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-64 1.07e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 39.35  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731150939   4 IILAGGSGTRlypLTKSISKQIMPVYDKPMIYYPLSILMLAG-IRDILIISTPRDLPVFKDL 64
Cdd:PRK00155    7 IIPAAGKGSR---MGADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAEL 65
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-144 8.15e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.53  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731150939   4 IILAGGSGTRLypltKS-ISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPRDLPVFKDLfgtgEQLGLNMSYAVQEQ 82
Cdd:PRK14353    9 IILAAGEGTRM----KSsLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAA----AKIAPDAEIFVQKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731150939  83 PRGLADAFIVGEEFI--GDDSVALILGDNIFygQSFSKILKKVASRESGATI--FGYYVRDPREYG 144
Cdd:PRK14353   81 RLGTAHAVLAAREALagGYGDVLVLYGDTPL--ITAETLARLRERLADGADVvvLGFRAADPTGYG 144
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-56 9.98e-03

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: 36.40  E-value: 9.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1731150939   6 LAGGSGTRLypltKSISKQIMPVYDKPMIYYPLSILMLAGIRDILIISTPR 56
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPN 47
 
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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