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Conserved domains on  [gi|1449726551|ref|WP_115875788|]
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MULTISPECIES: glucose-1-phosphate thymidylyltransferase RfbA [Enterobacter]

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];
1-287 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 555.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 161 PKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1449726551 241 EKRQGFKIACLEEIAYNQGWLSKEDIKSIGSSLSKTGYGNYLLSLIK 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: 555.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 161 PKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1449726551 241 EKRQGFKIACLEEIAYNQGWLSKEDIKSIGSSLSKTGYGNYLLSLIK 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: 546.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  82 SPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 162 KHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1449726551 242 KRQGFKIACLEEIAYNQGWLSKEDIKSIGSSLSKTGYGNYLLSLIK 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 ...
 1-240 4.47e-171

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: 472.44  E-value: 4.47e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 161 PKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-287 3.17e-144

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 406.75  E-value: 3.17e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  82 SPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 162 KHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1449726551 242 KRQGFKIACLEEIAYNQGWLSKEDIKSIGSSLSKTGYGNYLLSLIK 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 1.95e-99

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: 291.46  E-value: 1.95e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKV-CLVLGDNIFFGQAFGKQLRHAVD--NLSGATVFGYKVMDPERFGVVEFDDNFNAISI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 158 EEKPKHPK-SNWAVTGLYFYDNQVVE-IAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1449726551 236 FV 237
Cdd:pfam00483 241 FL 242
 
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: 555.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 161 PKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1449726551 241 EKRQGFKIACLEEIAYNQGWLSKEDIKSIGSSLSKTGYGNYLLSLIK 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: 546.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  82 SPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 162 KHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1449726551 242 KRQGFKIACLEEIAYNQGWLSKEDIKSIGSSLSKTGYGNYLLSLIK 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 ...
 1-240 4.47e-171

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: 472.44  E-value: 4.47e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 161 PKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-287 3.17e-144

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 406.75  E-value: 3.17e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  82 SPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 162 KHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1449726551 242 KRQGFKIACLEEIAYNQGWLSKEDIKSIGSSLSKTGYGNYLLSLIK 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 1.95e-99

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: 291.46  E-value: 1.95e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKV-CLVLGDNIFFGQAFGKQLRHAVD--NLSGATVFGYKVMDPERFGVVEFDDNFNAISI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 158 EEKPKHPK-SNWAVTGLYFYDNQVVE-IAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFAWLDTGTHDSLLEASQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1449726551 236 FV 237
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-237 1.65e-70

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 217.44  E-value: 1.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDcDSFKRLLGNGARLGINLSYKVQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIANDKVCLVLGDNiFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNfNAISIEEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDN-LIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1449726551 161 PKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFaWLDTGTHDSLLEASQFV 237
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-249 1.36e-62

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: 201.09  E-value: 1.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKVQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  82 SPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAfGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGI-SRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 162 KHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGFaWLDTGTHDSLLEASQFV-QTV 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIlDEV 238

                         250
                  ....*....|
gi 1449726551 241 EKR-QGFKIA 249
Cdd:TIGR01208 239 EREvQGVDDE 248
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 5.14e-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: 5.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   3 GIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDcDSFKRLLGNGARLGINLSYKVQPS 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  83 PDGLAQAFILGEEFIANDKVCLVLGDNIFFGqAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEKPK 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1449726551 163 HPKSNWAVTGLYFYDNQVVEIAKKVKPsdRGELEITSINQEYLNQGALKVEQLgrGFAWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-235 2.00e-48

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: 165.46  E-value: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDcDSFKRLLGNGARLGINLSYKVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  81 PSPDGLAQAFILGEEFIaNDKVCLVLGDNIFFGQAfgkqLRHAVDnLSGATVFGYKVMDPERFGVVEFDDNfNAISIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDL----LERLIR-AEAPAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1449726551 161 PKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGRGfaWLDTGTHDSLLEASQ 235
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANE 225
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-237 6.56e-41

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: 141.44  E-value: 6.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDIlIITTPEDCDSFKRLLGNGARLGINLSYKVQP 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  82 SPDGLAQAFILGEEFIANDKVCLVLGDnIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAISIEEKP 161
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEKP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1449726551 162 KHPKSNWAVTGLYFYDNQVVEIAKKVKPSDrgeleITSINQEYLNQGALKVEQLgRGFaWLDTGTHDSLLEASQFV 237
Cdd:COG1208   159 EEPPSNLINAGIYVLEPEIFDYIPEGEPFD-----LEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANALL 227
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-234 5.37e-29

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


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 111.09  E-value: 5.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTP----------EDCDSFKRLLGNG-- 68
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdRSYELEETLEKKGkt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  69 --------ARLGINLSYKVQPSPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFG-KQLRHAVdNLSGATVFGYKVMD 139
Cdd:cd02541    81 dlleevriISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPClKQLIEAY-EKTGASVIAVEEVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 140 PE---RFGVVEF----DDNFNAISIEEKPKhPK---SNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGA 209
Cdd:cd02541   160 PEdvsKYGIVKGekidGDVFKVKGLVEKPK-PEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238

                         250       260
                  ....*....|....*....|....*..
gi 1449726551 210 LkveqLGRGF--AWLDTGTHDSLLEAS 234
Cdd:cd02541   239 V----YAYVFegKRYDCGNKLGYLKAT 261
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-226 2.58e-23

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 95.36  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITT--PEDCDSFKRLLgnGARLGINLSYK 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEY--EKKLGIKITFS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  79 VQPSPDGLAQAFILGEEFIA-NDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNFNAI-S 156
Cdd:cd06425    79 IETEPLGTAGPLALARDLLGdDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIeR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1449726551 157 IEEKPKHPKSNWAVTGLYFYDNQVVeiakkvkpsDRGELEITSINQE----YLNQGALKVEQLgRGFaWLDTGT 226
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVL---------DRIPLRPTSIEKEifpkMASEGQLYAYEL-PGF-WMDIGQ 221
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-233 3.10e-20

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: 86.41  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDIlIITTPEDCDSFKRLLGNGARLGINLSYKVQPSP 83
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  84 DGLAQAFILGEEFIaNDKVCLVLGDnIFFGQAFGKQLRHAVDNLSGATV----FGYKVmdPerFGVVEFDDNFnAISIEE 159
Cdd:cd06426    81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVcvreYEVQV--P--YGVVETEGGR-ITSIEE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1449726551 160 KPKHpksNWAV-TGLYFYDNQVVEiakKVKPSDRgeLEITSINQEYLNQGalkvEQLG----RGFaWLDTGTHDSLLEA 233
Cdd:cd06426   154 KPTH---SFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEG----KKVGvfpiHEY-WLDIGRPEDYEKA 219
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 7.44e-18

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: 80.29  E-value: 7.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIittpedCDSFKR-----LLGNGARLGINLSYK 78
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVL------SVGYLAeqieeYFGDGYRGGIRIYYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  79 VQPSPDGLAQAFILGEEFIANDKVCLVLGDNIF---FGQAFGKQLRHAVDnlsgATVFGYKVMDPERFGVVEFDDNFNAI 155
Cdd:cd06915    76 IEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFdvdLLALLAALRASGAD----ATMALRRVPDASRYGNVTVDGDGRVI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1449726551 156 SIEEKPKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRgeleiTSINQEYLNQGALKV-EQLGRgFawLDTGTHDSLLEA 233
Cdd:cd06915   152 AFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFSLE-----ADVLPALVKRGRLYGfEVDGY-F--IDIGIPEDYARA 222
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 8.91e-16

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 75.45  E-value: 8.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYplSV--LMLAGIRDILIITTP-----EdcDSF-------KRLLGN 67
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiE--DHFdrsyeleATLEAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  68 G----------ARLGINLSYKVQPSPDGLAQAFILGEEFIANDKVCLVLGDNIFFGQAFG-KQLRHAVDNlSGATVFGYK 136
Cdd:COG1210    81 GkeelleevrsISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPClKQMIEVYEE-TGGSVIAVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 137 VMDPE---RFGVV---EFDDNFNAIS-IEEKPKHPK--SNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQ 207
Cdd:COG1210   160 EVPPEevsKYGIVdgeEIEGGVYRVTgLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                         250       260
                  ....*....|....*....|....*....
gi 1449726551 208 G---ALKVEqlGRgfaWLDTGTHDSLLEA 233
Cdd:COG1210   240 EpvyAYEFE--GK---RYDCGDKLGYLKA 263
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-57 2.91e-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: 72.69  E-value: 2.91e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPED 57
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-177 2.55e-13

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 69.33  E-value: 2.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   3 GIILAGGSGSRLHPITLGTSKqllpiydkPMIYY---------PLSVLMLAGIRDILIITtpedcdSFK-----RLLGNG 68
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT------QYKshslnDHIGSG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  69 ARLGIN--------LSYKVQPSPD----GLAQAFILGEEFI--ANDKVCLVL-GDNIF---FGQAfgkqLRHAVDNLSGA 130
Cdd:COG0448    70 KPWDLDrkrggvfiLPPYQQREGEdwyqGTADAVYQNLDFIerSDPDYVLILsGDHIYkmdYRQM----LDFHIESGADI 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1449726551 131 TVFGYKV--MDPERFGVVEFDDNFNAISIEEKPKHPKSNWAVTGLYFYD 177
Cdd:COG0448   146 TVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-223 1.82e-12

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: 65.33  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDcDSFKRLLgnGARLGINLSYKVQPSP 83
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELL--KKYPNIKFVYNPDYAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  84 DGLAQAFILGEEFIANDkvCLVL-GDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDPErfgVVEFDDNFNAISIEEKPK 162
Cdd:cd02523    79 TNNIYSLYLARDFLDED--FLLLeGDVVFDPSILERLLSSPADNAILVDKKTKEWEDEY---VKDLDDAGVLLGIISKAK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1449726551 163 HPKSN-WAVTGLYFYDNQ----VVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQLGrGFAWLD 223
Cdd:cd02523   154 NLEEIqGEYVGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-57 2.62e-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: 64.58  E-value: 2.62e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPED 57
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHS 57
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 1.09e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 60.25  E-value: 1.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIIT 53
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-209 3.05e-10

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: 58.80  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYplSVLMLAGIRD--ILIITTPEDCDSFK-----RLLGNGARLginls 76
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrFIFICRDEHNTKFHldeslKLLAPNATV----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  77 YKVQPSPDGLAQAFILGEEFIANDKVCLVL-GDNIFFGQAFGKQLRHAVDNLSGATVFGYKVMDpeRFGVVEFDDNFNAI 155
Cdd:cd04183    75 VELDGETLGAACTVLLAADLIDNDDPLLIFnCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP--RWSYVKLDENGRVI 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1449726551 156 SIEEKpkHPKSNWAVTGLYFYDN--QVVEIAKKVKPSDR---GELEITSINQEYLNQGA 209
Cdd:cd04183   153 ETAEK--EPISDLATAGLYYFKSgsLFVEAAKKMIRKDDsvnGEFYISPLYNELILDGK 209
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-65 3.62e-09

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 55.91  E-value: 3.62e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1449726551   4 IILAGGSGSRLHpitLGTSKQLLPIYDKPMIYYPLSVLMLAG-IRDILIITTPEDCDSFKRLL 65
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELL 60
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-198 4.11e-08

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 53.37  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDcDSFKRLLGNGARLGINLSYKV-- 79
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSK-NSIENHFDTSFELEAMLEKRVkr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  80 --------------------QPSPDGLAQAFILGEEFIANDKVCLVLGDNIFfgQAFGKQLRHavDNLSG---------- 129
Cdd:PRK13389   89 qlldevqsicpphvtimqvrQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIL--DEYESDLSQ--DNLAEmirrfdetgh 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1449726551 130 ATVFGYKVMDPERFGVVEFD-------DNFNAISIEEKPK--HPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEIT 198
Cdd:PRK13389  165 SQIMVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-51 5.84e-08

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: 52.19  E-value: 5.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1449726551   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILI 51
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV 50
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 1.05e-07

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 52.20  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIIT------------TPEDCDSF------K 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  63 RLLGNGARL---GINLSYKVQPSPDGLAQAFILGEEFIANDKVCLVLGDnIFFGQAFGKQLRH------AVDNLSGATVF 133
Cdd:PRK10122   84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPD-VVIDDASADPLRYnlaamiARFNETGRSQV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1449726551 134 GYKVM--DPERFGVVEFDDNFNA-------ISIEEKPKHPK---SNWAVTGLYFYDNQVVEIAKKVKPSDRGELEIT 198
Cdd:PRK10122  163 LAKRMpgDLSEYSVIQTKEPLDRegkvsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 1.20e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 51.29  E-value: 1.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1449726551   4 IILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYPLSVLMLAG-IRDILIITTPEDCDSFKRLL 65
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-166 1.92e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 51.75  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   3 GIILAGGSGSRLHPITLGTSKQLLP---IYDkpMIYYPLSVLMLAGIRDILIITtpedcdSFK---------------RL 64
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLT------QYKshsldrhisqtwrlsGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  65 LGN-------GARLG--------------INLSYKVQPspdglaqafilgeefianDKVCLVLGDNIF---FGQafgkQL 120
Cdd:PRK00844   80 LGNyitpvpaQQRLGkrwylgsadaiyqsLNLIEDEDP------------------DYVVVFGADHVYrmdPRQ----MV 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1449726551 121 RHAVDNLSGATVFGYKV--MDPERFGVVEFDDNFNAISIEEKPKHPKS 166
Cdd:PRK00844  138 DFHIESGAGVTVAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPG 185
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-73 2.33e-07

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 50.21  E-value: 2.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1449726551   4 IILAGGSGSRLHpitLGTSKQLLPIYDKPMIYYPLSVLM-LAGIRDILIITTPEDCDSFKRLLGNGARLGI 73
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVV 71
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-234 5.05e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 50.25  E-value: 5.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILIITtpedcdSFKRLL-----GNGARLGIN 74
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT------QYQPLElnnhiGIGSPWDLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  75 --------LS----------YKvqpspdGLAQAFILGEEFI--ANDKVCLVL-GDNIFfGQAFGKQLRHAVDNLSGATVf 133
Cdd:PRK05293   78 ringgvtiLPpyseseggkwYK------GTAHAIYQNIDYIdqYDPEYVLILsGDHIY-KMDYDKMLDYHKEKEADVTI- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551 134 gyKVMD-----PERFGVVEFDDNFNAISIEEKPKHPKSNWAVTGLYFYDNQV-----VEIAKKVKPS-DRGELEITSinq 202
Cdd:PRK05293  150 --AVIEvpweeASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRlkeylIEDEKNPNSShDFGKNVIPL--- 224

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1449726551 203 eYLNQGalkveqlGRGFA------WLDTGTHDSLLEAS 234
Cdd:PRK05293  225 -YLEEG-------EKLYAypfkgyWKDVGTIESLWEAN 254
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-166 7.00e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 49.84  E-value: 7.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILIITT-----------------PEDCDSFKRLL 65
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQykahslirhiqrgwsffREELGEFVDLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  66 GNGARLGINLSYKvqpspdGLAQAF-----ILGEEfiaNDKVCLVL-GDNIfFGQAFGKQLRHAVDnlSGA--TVFGYKV 137
Cdd:PRK00725   99 PAQQRVDEENWYR------GTADAVyqnldIIRRY---DPKYVVILaGDHI-YKMDYSRMLADHVE--SGAdcTVACLEV 166

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1449726551 138 --MDPERFGVVEFDDNFNAISIEEKPKHPKS 166
Cdd:PRK00725  167 prEEASAFGVMAVDENDRITAFVEKPANPPA 197
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-132 1.10e-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: 47.57  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   3 GIILAGGSGSRlhpitLGTSKQLLPIYDKPMIYYPLSVLMLAGiRDILIITTPEDCDSFKRLLGngarlginLSYKVQPS 82
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1449726551  83 PD-----GLAQAFilgEEFIANDKVCLVLGDNIFFGQAFGKQLRHAVDNLSGATV 132
Cdd:pfam12804  67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
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 1.33e-06

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: 48.40  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   3 GIILAGG--SGSRLHPITLGTSKQLLPIYDKPMIYYPLSVL-MLAGIRDILIITTPEDcDSFKRLLGNGAR-LGINLSYK 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPE-SVFSDFISDAQQeFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  79 VQPSPDGLAQAF------ILGEE----FIANDKVC--LVLGDnifFGQAFGKQLRHAV-----DNLSGATVFGYKVMDPE 141
Cdd:cd06428    80 QEYKPLGTAGGLyhfrdqILAGNpsafFVLNADVCcdFPLQE---LLEFHKKHGASGTilgteASREQASNYGCIVEDPS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1449726551 142 RFGVVEFddnfnaisiEEKPKHPKSNWAVTGLYFYDNQVVEIAKKVKPSDRGELEITSINQEYLNQGALKVEQ 214
Cdd:cd06428   157 TGEVLHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQ 220
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-53 1.58e-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: 47.54  E-value: 1.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1449726551   3 GIILAGGSGSRLHPITLGTSKQLLPI---YDkpMIYYPLSVLMLAGIRDILIIT 53
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT 52
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-108 2.91e-06

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: 46.78  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   3 GIILAGGSGSRLhpitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDCDSFKRLLGNGARLGINLSYKvqps 82
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWE---- 73

                          90       100
                  ....*....|....*....|....*...
gi 1449726551  83 pDGLAQAFILGEEFIAND-KVCLV-LGD 108
Cdd:cd04182    74 -EGMSSSLAAGLEALPADaDAVLIlLAD 100
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-53 3.56e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 46.69  E-value: 3.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1449726551   3 GIILAGGSGSRLhpitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIIT 53
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVL 51
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-55 2.45e-05

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 44.11  E-value: 2.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1449726551   6 LAGGSGSRLHpitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTP 55
Cdd:COG2266     1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-200 5.04e-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: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   1 MKGIILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYplsVLMLAG-IRDILIITTPEDCDSFKRLLGNgarlgiNLSYKV 79
Cdd:PRK14357    1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINW---VIDTAKkVAQKVGVVLGHEAELVKKLLPE------WVKIFL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  80 QPSPDGLAQAFILGEEFIA-NDKVCLVLGDNIFFGQAFGKQL--RHAVDNlSGATVFGYKVMDPERFG-VVEFDDNFNAI 155
Cdd:PRK14357   69 QEEQLGTAHAVMCARDFIEpGDDLLILYGDVPLISENTLKRLieEHNRKG-ADVTILVADLEDPTGYGrIIRDGGKYRIV 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1449726551 156 SIEEKPKHPKSNWAV-TGLYFYD-NQVVEIAKKVKPSD-RGELEITSI 200
Cdd:PRK14357  148 EDKDAPEEEKKIKEInTGIYVFSgDFLLEVLPKIKNENaKGEYYLTDA 195
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-57 5.17e-05

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 43.26  E-value: 5.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1449726551   1 MKGIILAGGSGSRlhpitLGTSKQLLPIYDKPMIYYPLSVLMLAgIRDILIITTPED 57
Cdd:COG0746     5 ITGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPE 55
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-53 9.77e-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: 42.95  E-value: 9.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1449726551   1 MKGIILAGGSGSRLHPI-TLGTSKQLLPIY-DKPMIYYPLS-VLMLAGIRDILIIT 53
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVT 56
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 1.33e-04

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 42.75  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1449726551   1 MKGIILAGGSGSRL-------HPitlgtsKQLLPIY-DKPMIYypLSVLMLAGI---RDILIIT 53
Cdd:COG0836     3 IYPVILAGGSGTRLwplsresYP------KQFLPLLgEKSLLQ--QTVERLAGLvppENILVVT 58
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-160 3.91e-04

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: 40.96  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITTPEDcDSFKRLLGNgarlgINLSYKVQPSP 83
Cdd:cd02540     2 VILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA-EQVKKALAN-----PNVEFVLQEEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  84 DGLAQAFILGEEFIA--NDKVcLVL-GDNIFF-GQAFGKQLRHAVDNLSGATVFGYKVMDPERFG--VVEFDDNFNAIsI 157
Cdd:cd02540    73 LGTGHAVKQALPALKdfEGDV-LVLyGDVPLItPETLQRLLEAHREAGADVTVLTAELEDPTGYGriIRDGNGKVLRI-V 150


                  ...
gi 1449726551 158 EEK 160
Cdd:cd02540   151 EEK 153
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-213 5.04e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.36  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRL---HPitlgtsKQLLPIYDKPMIYYPLSVLMLAGIRDILIIttpedcdsfkrlLGNGA-----RLGINL 75
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGAeevkeVLGDRS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  76 SYKVQPSPDGLAQAFILGEEFIANDK-VCLVL-GDNIFF-GQAFGKQLRHAVDNLSGATVFGYKVMDPERFGVVEFDDNF 152
Cdd:PRK14354   68 EFALQEEQLGTGHAVMQAEEFLADKEgTTLVIcGDTPLItAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1449726551 153 NAISI-EEK---PKHPKSNWAVTGLYFYDNQV-VEIAKKVKPSD-RGELEITSINQEYLNQGaLKVE 213
Cdd:PRK14354  148 EVEKIvEQKdatEEEKQIKEINTGTYCFDNKAlFEALKKISNDNaQGEYYLTDVIEILKNEG-EKVG 213
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-53 5.55e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.99  E-value: 5.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1449726551   3 GIILAGGSGSRLHPITLGTSKQLLPI---YDkpMIYYPLSVLMLAGIRDILIIT 53
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLT 57
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-67 5.69e-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: 40.99  E-value: 5.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1449726551   4 IILAGGSGSRLhpiTLGTSKQLLPIYDKPMIYYPLSVLMLAG-IRDILIITTPEDCDSFKRLLGN 67
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-209 7.78e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.73  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551   4 IILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILIITtpedcdsfkrllGNGAR------LGINLSY 77
Cdd:PRK14358   11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVT------------GHGAEqveaalQGSGVAF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449726551  78 KVQPSPDGLAQAFILGEEFIAN-DKVCLVL-GDNIFFGQAFGKQL--RHAVDNlSGATVFGYKVMDPERFG-VVEFDDNF 152
Cdd:PRK14358   76 ARQEQQLGTGDAFLSGASALTEgDADILVLyGDTPLLRPDTLRALvaDHRAQG-SAMTILTGELPDATGYGrIVRGADGA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1449726551 153 NAISIEEKPKHPKSNwAV----TGLYFYDNQVVEIAKKVKPSDR-GELEITSINQEYLNQGA 209
Cdd:PRK14358  155 VERIVEQKDATDAEK-AIgefnSGVYVFDARAPELARRIGNDNKaGEYYLTDLLGLYRAGGA 215
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-64 1.07e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.10  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1449726551   1 MKGIILAGGSGSRlhpitLGTSKQLLPIYDKPMIYYPLSvlMLAGIRDILIITTPEDCDSFKRL 64
Cdd:cd02503     1 ITGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-53 2.94e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 38.71  E-value: 2.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1449726551   3 GIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILIIT 53
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
 
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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