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Conserved domains on  [gi|1434599840|ref|WP_114340694|]
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glucose-1-phosphate thymidylyltransferase RfbA [Rhodanobacter denitrificans]

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];
4-294 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQTIE 243
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1434599840 244 NRQGLKVCCPEEIAYLNGWINAEQLLALAAPLAKTGYGQYLQQLTQQGLAR 294
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRAR 292
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
4-294 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQTIE 243
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1434599840 244 NRQGLKVCCPEEIAYLNGWINAEQLLALAAPLAKTGYGQYLQQLTQQGLAR 294
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRAR 292
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 4-289 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: 545.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQTIE 243
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1434599840 244 NRQGLKVCCPEEIAYLNGWINAEQLLALAAPLAKTGYGQYLQQLTQ 289
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 4-242 1.10e-168

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: 466.67  E-value: 1.10e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQTI 242
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-289 9.24e-141

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 398.28  E-value: 9.24e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   2 STKGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAV 81
Cdd:PRK15480    3 TRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  82 QPSPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEE 161
Cdd:PRK15480   83 QPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 162 KPAQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQT 241
Cdd:PRK15480  163 KPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIAT 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1434599840 242 IENRQGLKVCCPEEIAYLNGWINAEQLLALAAPLAKTGYGQYLQQLTQ 289
Cdd:PRK15480  243 IEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 4-239 6.46e-104

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: 303.02  E-value: 6.46e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDK-PMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQ 82
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  83 PSPDGLAQAFTIGRDFV-DGKPSCLVLGDNIFYGHGFTERLKRAAARE--HGATVFGYWVRDPERYGVAEFDGAGKVIGL 159
Cdd:pfam00483  81 PEGKGTAPAVALAADFLgDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 160 EEKPAQPK-SHYAVTGLYFYDGRVCDYAAS-LKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGN 237
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLAKyLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1434599840 238 YI 239
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
4-294 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQTIE 243
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1434599840 244 NRQGLKVCCPEEIAYLNGWINAEQLLALAAPLAKTGYGQYLQQLTQQGLAR 294
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRAR 292
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 4-289 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: 545.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQTIE 243
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1434599840 244 NRQGLKVCCPEEIAYLNGWINAEQLLALAAPLAKTGYGQYLQQLTQ 289
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 4-242 1.10e-168

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: 466.67  E-value: 1.10e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQTI 242
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-289 9.24e-141

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 398.28  E-value: 9.24e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   2 STKGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAV 81
Cdd:PRK15480    3 TRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  82 QPSPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEE 161
Cdd:PRK15480   83 QPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 162 KPAQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGNYIQT 241
Cdd:PRK15480  163 KPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIAT 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1434599840 242 IENRQGLKVCCPEEIAYLNGWINAEQLLALAAPLAKTGYGQYLQQLTQ 289
Cdd:PRK15480  243 IEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 4-239 6.46e-104

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: 303.02  E-value: 6.46e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDK-PMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQ 82
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  83 PSPDGLAQAFTIGRDFV-DGKPSCLVLGDNIFYGHGFTERLKRAAARE--HGATVFGYWVRDPERYGVAEFDGAGKVIGL 159
Cdd:pfam00483  81 PEGKGTAPAVALAADFLgDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 160 EEKPAQPK-SHYAVTGLYFYDGRVCDYAAS-LKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFAWLDTGTHESLMEAGN 237
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLAKyLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1434599840 238 YI 239
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 4-235 8.94e-74

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: 225.91  E-value: 8.94e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHeQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGhGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGaGKVIGLEEKP 163
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD-GRIVRLVEKP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFaWLDTGTHESLMEA 235
Cdd:cd04189   159 KEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEA 229
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 4-249 2.05e-63

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: 203.40  E-value: 2.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGhGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKP 163
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 164 AQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGFaWLDTGTHESLMEAgNYI---Q 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA-NRLildE 237


                  ....*....
gi 1434599840 241 TIENRQGLK 249
Cdd:TIGR01208 238 VEREVQGVD 246
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-227 1.05e-62

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: 197.03  E-value: 1.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   5 GIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVlVINTPHEQDMFQRLLGDGSQWGIDIRYAVQPS 84
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEI-ILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  85 PDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGhGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKPA 164
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1434599840 165 QPKSHYAVTGLYFYDGRVCDYAASLKpsPRGELEITDLNRCYLDDDSLhleqlgRGF----AWLDTG 227
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKV------YGYpvdgYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 3-239 6.80e-50

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: 169.70  E-value: 6.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   3 TKGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEqDMFQRLLGDGSQWGIDIRYAVQ 82
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  83 PSPDGLAQAFTIGRDFVDGKpsCLVL-GDNIFyghgfTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGaGKVIGLEE 161
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDDE--FLVLnGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434599840 162 KPAQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGRGfaWLDTGTHESLMEAGNYI 239
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-235 2.04e-47

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: 158.78  E-value: 2.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVlVINTPHEQDMFQRLLGDGSQWGIDIRYAVQP 83
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SP----DGLAQAftigRDFVDGKPSCLVLGDnIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGL 159
Cdd:COG1208    80 EPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1434599840 160 EEKPAQPKSHYAVTGLYFYDGRVCDYAaslkpsPRGE-LEITDLNRCYLDDDSLHLEQLgRGFaWLDTGTHESLMEA 235
Cdd:COG1208   155 VEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 3-235 2.28e-32

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: 120.33  E-value: 2.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   3 TKGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHE---QDMFQR-------LLGDGSQ 72
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKraiEDHFDRsyeleetLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  73 ----------WGIDIRYAVQPSPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYghGFTERLKR--AAAREHGATVFGYWVR 140
Cdd:cd02541    81 dlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLID--SKEPCLKQliEAYEKTGASVIAVEEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 141 DPE---RYGVAEFDGAG----KVIGLEEKPAQ--PKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDS 211
Cdd:cd02541   159 PPEdvsKYGIVKGEKIDgdvfKVKGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238

                         250       260
                  ....*....|....*....|....*
gi 1434599840 212 LHLEQL-GRgfaWLDTGTHESLMEA 235
Cdd:cd02541   239 VYAYVFeGK---RYDCGNKLGYLKA 260
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 6-235 9.93e-25

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: 98.78  E-value: 9.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   6 IILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVlVINTPHEQDMFQRLLGDGSQWGIDIRYAVQPSP 85
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  86 DGLAQAFTIGRDFVDGkPSCLVL-GDNIFYGhGFTERLKRAAAREHGATVFGYWVRDPERYGVAEFDGAGKVIGLEEKPA 164
Cdd:cd06915    81 LGTGGAIKNALPKLPE-DQFLVLnGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434599840 165 QPKSHYAVTGLYFYDGRVCDYAASLKPSprgeLEiTDLNRCYLDDDSLhleqlgRGFA----WLDTGTHESLMEA 235
Cdd:cd06915   159 GAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-235 7.80e-22

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 92.40  E-value: 7.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   3 TKGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPH--------------EQ-------- 60
Cdd:COG1210     4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGkraiedhfdrsyelEAtleakgke 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  61 ---DMFQRLLGDGsqwgiDIRYAVQPSPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGHgfTERLKR--AAAREHGATVF 135
Cdd:COG1210    84 ellEEVRSISPLA-----NIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQmiEVYEETGGSVI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 136 GywVR--DPE---RYGVAEFDGAG----KVIGLEEKPAQPK--SHYAVTGLYFYDGRVCDYAASLKPSPRGELEITD-LN 203
Cdd:COG1210   157 A--VQevPPEevsKYGIVDGEEIEggvyRVTGLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDaIA 234

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1434599840 204 RcYLDDDSLH-LEQLGRgfaWLDTGTHESLMEA 235
Cdd:COG1210   235 A-LAKEEPVYaYEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-235 1.37e-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: 90.26  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   6 IILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVlVINTPHEQDMFQRLLGDGSQWGIDIRYAVQPSP 85
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  86 DGLAQAFTigrdFVDGKPSCLVL---GD---NIFYGHGFTERLKRAA-----AREHGATVfgywvrdPerYGVAEFDGaG 154
Cdd:cd06426    81 LGTAGALS----LLPEKPTDPFLvmnGDiltNLNYEHLLDFHKENNAdatvcVREYEVQV-------P--YGVVETEG-G 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 155 KVIGLEEKPAQpkSHYAVTGLYFYDGRVCDYAaslkpsPRGE-LEITDLNRCYLDDDslhlEQLG----RGFaWLDTGTH 229
Cdd:cd06426   147 RITSIEEKPTH--SFLVNAGIYVLEPEVLDLI------PKNEfFDMPDLIEKLIKEG----KKVGvfpiHEY-WLDIGRP 213


                  ....*.
gi 1434599840 230 ESLMEA 235
Cdd:cd06426   214 EDYEKA 219
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 4-185 3.16e-19

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 84.18  E-value: 3.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREV-LVINTPHEqDMFQRLLGDGSQWGIDIRYAVQ 82
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIiLAVNYRPE-DMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  83 PSPDGLAQAFTIGRDFVDGKPSC-LVLGDNIFYGHGFTERLKraAAREHG--ATVFGYWVRDPERYGVAEFDGA-GKVIG 158
Cdd:cd06425    81 TEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLD--FHKKHGaeGTILVTKVEDPSKYGVVVHDENtGRIER 158

                         170       180
                  ....*....|....*....|....*..
gi 1434599840 159 LEEKPAQPKSHYAVTGLYFYDGRVCDY 185
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVLDR 185
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-235 1.43e-17

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 79.54  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVlVINTPHEQDMFQRLLGDgSQWGIDIRYavQP 83
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTHHLADQIEAHLGD-SRFGLRITI--SD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPD-------GLAQAftigRDFVDGKPSCLVLGDnIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYGVAEF--DGAG 154
Cdd:cd06422    77 EPDelletggGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDADG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 155 KVIGLEEKPAQPkshYAVTGLYFYDGRVCDYAaslkpsPRGELEITDLNRCYLDDDSLHLEqLGRGFaWLDTGTHESLME 234
Cdd:cd06422   152 RLRRGGGGAVAP---FTFTGIQILSPELFAGI------PPGKFSLNPLWDRAIAAGRLFGL-VYDGL-WFDVGTPERLLA 220


                  .
gi 1434599840 235 A 235
Cdd:cd06422   221 A 221
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-67 6.36e-14

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 69.22  E-value: 6.36e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLL 67
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-235 3.89e-13

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: 67.26  E-value: 3.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   6 IILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVlVINTPHEQDMFQRLLGDgsqwGIDIRYAVQPSP 85
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDI-VIVTGYKKEQIEELLKK----YPNIKFVYNPDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  86 D--GLAQAFTIGRDFVDGkpSCLVL-GDNIFYgHGFTERLKRAAAREhGATVFGYWVRDPERYGVAeFDGAGKVIGLEEK 162
Cdd:cd02523    77 AetNNIYSLYLARDFLDE--DFLLLeGDVVFD-PSILERLLSSPADN-AILVDKKTKEWEDEYVKD-LDDAGVLLGIISK 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434599840 163 PAQPKS-HYAVTGLYFYDG----RVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQLGrGFAWLDTGTHESLMEA 235
Cdd:cd02523   152 AKNLEEiQGEYVGISKFSPedadRLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-239 1.15e-12

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 66.03  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVInTPHEQDMFQRLLGdgsQWGIDIRYAVQP 83
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV-TGYKAELIEEALA---RPGPDVTFVYNP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFT--IGRDFVDGkpSCLVL-GDNIFyghgftER--LKRAAAREHGATVF--GYWVR---DPERYgvaEFDGA 153
Cdd:COG1213    77 DYDETNNIYSlwLAREALDE--DFLLLnGDVVF------DPaiLKRLLASDGDIVLLvdRKWEKpldEEVKV---RVDED 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 154 GKVIGLEEKPAQPKSHYAVTGLYFYDG----RVCDYAASLKPSPRGELEITDLNRCYLDDD-SLHLEQLGRGFaWLDTGT 228
Cdd:COG1213   146 GRIVEIGKKLPPEEADGEYIGIFKFSAegaaALREALEALIDEGGPNLYYEDALQELIDEGgPVKAVDIGGLP-WVEIDT 224

                         250
                  ....*....|.
gi 1434599840 229 HESLMEAGNYI 239
Cdd:COG1213   225 PEDLERAEELF 235
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 4-61 1.48e-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: 65.35  E-value: 1.48e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQD 61
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQA 59
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 5-179 1.88e-12

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 66.64  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   5 GIILAGGSGTRLHPIT--RAtskqllpvydKPMIYY---------PLATLMLAGIREVLVIntphEQDMFQRL---LGDG 70
Cdd:COG0448     4 AIILAGGRGSRLGPLTkdRA----------KPAVPFggkyriidfPLSNCVNSGIRRVGVL----TQYKSHSLndhIGSG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  71 SQWGIDIRY-------AVQPSPD-----GLAQAFTIGRDFVDGKPSCLVL---GDNIF---YG-----Hgfterlkraaa 127
Cdd:COG0448    70 KPWDLDRKRggvfilpPYQQREGedwyqGTADAVYQNLDFIERSDPDYVLilsGDHIYkmdYRqmldfH----------- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1434599840 128 REHGA--TVFGYWVRDPE--RYGVAEFDGAGKVIGLEEKPAQPKSHYAVTGLYFYD 179
Cdd:COG0448   139 IESGAdiTVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 5-216 6.09e-11

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: 61.50  E-value: 6.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   5 GIILAGG--SGTRLHPITRATSKQLLPVYDKPMIYYPLATL-MLAGIREVLVINTpHEQDMFQRLLGDGSQ-WGIDIRYA 80
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGF-YPESVFSDFISDAQQeFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  81 VQPSPDGLAQAFTIGRDFV-DGKPsclvlgDNIFYGHG-------FTERLkrAAAREHGATV--------------FGYW 138
Cdd:cd06428    80 QEYKPLGTAGGLYHFRDQIlAGNP------SAFFVLNAdvccdfpLQELL--EFHKKHGASGtilgteasreqasnYGCI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434599840 139 VRDPErygvaefdgAGKVIGLEEKPAQPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITDLNRCYLDDDSLHLEQ 216
Cdd:cd06428   152 VEDPS---------TGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQ 220
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-202 7.39e-11

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: 60.61  E-value: 7.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   6 IILAGGSGTRLHpitRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVInTPHEQDMFQRLLGDgsqwgIDIRYAVQPSP 85
Cdd:cd02540     2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALAN-----PNVEFVLQEEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  86 DGLAQAFTIGRDFVDGKPScLVLgdnIFYG----------HGFTERLKRAAArehGATVFGYWVRDPERYG-VAEfDGAG 154
Cdd:cd02540    73 LGTGHAVKQALPALKDFEG-DVL---VLYGdvplitpetlQRLLEAHREAGA---DVTVLTAELEDPTGYGrIIR-DGNG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1434599840 155 KVIG-LEEK---PAQPKSHYAVTGLYFYDGRVC-DYAASLKPSP-RGELEITDL 202
Cdd:cd02540   145 KVLRiVEEKdatEEEKAIREVNAGIYAFDAEFLfEALPKLTNNNaQGEYYLTDI 198
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
4-201 2.68e-10

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 59.92  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVI------------NTPHE-----QDMFQRL 66
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthssknsienhfDTSFEleamlEKRVKRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  67 LGDGSQW----GIDIRYAVQPSPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYGH-------GFTERLKRAAAREHgATVF 135
Cdd:PRK13389   90 LLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYesdlsqdNLAEMIRRFDETGH-SQIM 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434599840 136 GYWVRDPERYGVAEFDGA-------GKVIGLEEKPA--QPKSHYAVTGLYFYDGRVCDYAASLKPSPRGELEITD 201
Cdd:PRK13389  169 VEPVADVTAYGVVDCKGVelapgesVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
4-201 5.93e-10

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 58.75  E-value: 5.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVI------------NTPH------EQDMFQR 65
Cdd:PRK10122    5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthasknavenhfDTSYelesllEQRVKRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  66 LLGDGSQW---GIDIRYAVQPSPDGLAQAFTIGRDFVDGKPSCLVLGDNIFYG-------HGFTERLKRAAAREHGATVF 135
Cdd:PRK10122   85 LLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplrYNLAAMIARFNETGRSQVLA 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434599840 136 GYWVRDPERYGVAE----FDGAGKV---IGLEEKPAQPK---SHYAVTGLYFYDGRVCDYAASLKPSPRGELEITD 201
Cdd:PRK10122  165 KRMPGDLSEYSVIQtkepLDREGKVsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-167 3.11e-09

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 57.45  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   6 IILAGGSGTRLhpiTRATSKQLLPVYDKPMIYYPLATLMLAGIrEVLVINTPHEQDMFQRLLGDGSqwgiDIRYAVQPSP 85
Cdd:PRK14355    7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGA-GRIVLVVGHQAEKVREHFAGDG----DVSFALQEEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  86 DGLAQAFTIGRDFVDG-KPSCLVL-GDNIFYGHGFTERLKRAAAREHGA-TVFGYWVRDPERYGVAEFDGAGKVIGL-EE 161
Cdd:PRK14355   79 LGTGHAVACAAPALDGfSGTVLILcGDVPLLRAETLQGMLAAHRATGAAvTVLTARLENPFGYGRIVRDADGRVLRIvEE 158


                  ....*.
gi 1434599840 162 KPAQPK 167
Cdd:PRK14355  159 KDATPE 164
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 5-235 8.43e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 55.64  E-value: 8.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   5 GIILAGGSGTRLHPITRATSKQLLPVYDK-PMIYYPLATLMLAGIREVLVINT--PHEqdmFQRLLGDGSQWGIDIR--- 78
Cdd:PRK05293    6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQyqPLE---LNNHIGIGSPWDLDRIngg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  79 -YAVQPSPD--------GLAQAFTIGRDFVDGKPSCLVL---GDNIfYGHGFTERLKRAAAREHGATVFGYWVRDPE--R 144
Cdd:PRK05293   83 vTILPPYSEseggkwykGTAHAIYQNIDYIDQYDPEYVLilsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEVPWEEasR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840 145 YGVAEFDGAGKVIGLEEKPAQPKSHYAVTGLYFYDGRVcdyaasLKpsprgELEITDlnrcYLDDDSLH----------L 214
Cdd:PRK05293  162 FGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKR------LK-----EYLIED----EKNPNSSHdfgknviplyL 226

                         250       260
                  ....*....|....*....|....*..
gi 1434599840 215 EQLGRGFA------WLDTGTHESLMEA 235
Cdd:PRK05293  227 EEGEKLYAypfkgyWKDVGTIESLWEA 253
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-181 8.51e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 55.92  E-value: 8.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   4 KGIILAGGSGTRLHpitRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINtpHEQDMFQRLLGDgsqwgiDIRYAVQP 83
Cdd:PRK14357    2 RALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLG--HEAELVKKLLPE------WVKIFLQE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  84 SPDGLAQAFTIGRDFVDGKPSCLVL-GDNIFYGHGFTERLKRAAAREHG-ATVFGYWVRDPERYGVAEFDGaGKVIGLEE 161
Cdd:PRK14357   71 EQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEHNRKGAdVTILVADLEDPTGYGRIIRDG-GKYRIVED 149

                         170       180
                  ....*....|....*....|...
gi 1434599840 162 KPAQPKSHYAV---TGLYFYDGR 181
Cdd:PRK14357  150 KDAPEEEKKIKeinTGIYVFSGD 172
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 6-206 4.55e-08

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 53.83  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   6 IILAGGSGTRLHpitRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQDMFQRLLGDGsqwgidIRYAVQPSP 85
Cdd:PRK14358   11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  86 DGLAQAFTIGRD-FVDGKPSCLVLGDNIFYGHGFTERLKRAAAREHGA--TVFGYWVRDPERYG--VAEFDGAGKVIgLE 160
Cdd:PRK14358   82 LGTGDAFLSGASaLTEGDADILVLYGDTPLLRPDTLRALVADHRAQGSamTILTGELPDATGYGriVRGADGAVERI-VE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1434599840 161 EKPAQPKSHyAV----TGLYFYDGRVCDYAASL-KPSPRGELEITDLNRCY 206
Cdd:PRK14358  161 QKDATDAEK-AIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLY 210
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-69 4.95e-08

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: 52.44  E-value: 4.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434599840   6 IILAGGSGTRLHpitRATSKQLLPVYDKPMIYYPLATLMLAG-IRE-VLVINtPHEQDMFQRLLGD 69
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEiVVVVP-PDDIEYFEELLAK 62
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 5-138 3.26e-07

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: 49.48  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   5 GIILAGGSGTRLHPItratsKQLLPVYDKPMIYYPLATLMLAGIREVLVInTPHEQDMFQRLLgdgsqWGIDIRYAVQPS 84
Cdd:cd04182     3 AIILAAGRSSRMGGN-----KLLLPLDGKPLLRHALDAALAAGLSRVIVV-LGAEADAVRAAL-----AGLPVVVVINPD 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1434599840  85 PD-GLAQAFTIGRDFVDGKPS-CLV-LGDNIFYGHGFTERLKRAAAREHGATVFGYW 138
Cdd:cd04182    72 WEeGMSSSLAAGLEALPADADaVLIlLADQPLVTAETLRALIDAFREDGAGIVAPVY 128
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-70 4.58e-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: 49.44  E-value: 4.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434599840   6 IILAGGSGTRLHpitRATSKQLLPVYDKPMIYYPLATLM-LAGIREVLVINTPHEQDMFQRLLGDG 70
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-202 9.58e-07

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: 49.64  E-value: 9.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   1 MSTKGIILAGGSGTRLHpitRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVInTPHEQDMFQRLLGDgsqwgIDIRYA 80
Cdd:COG1207     1 SPLAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVRAALAD-----LDVEFV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  81 VQPSPDGLAQAFTIGRDFVDGKPS-CLVL-GDnifyghgfT-----ERLKR--AAAREHGA-----TVFgywVRDPERYG 146
Cdd:COG1207    72 LQEEQLGTGHAVQQALPALPGDDGtVLVLyGD--------VpliraETLKAllAAHRAAGAaatvlTAE---LDDPTGYG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434599840 147 VAEFDGAGKVIGL-EEK---PAQPKSHYAVTGLYFYDGRVC-DYAASLKPS-PRGELEITDL 202
Cdd:COG1207   141 RIVRDEDGRVLRIvEEKdatEEQRAIREINTGIYAFDAAALrEALPKLSNDnAQGEYYLTDV 202
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-134 1.16e-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: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   5 GIILAGGSGTRLhpitrATSKQLLPVYDKPMIYYPLATlmLAGIREVLVINTPHEQ--DMFQRLlgdgsqwgiDIRYAVQ 82
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLER--LRPAGDEVVVVANDEEvlAALAGL---------GVPVVPD 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1434599840  83 PSPD-----GLAQAFtigrDFVDGKPSCLVL-GDNIFYGHGFTERLKRAAAREHGATV 134
Cdd:pfam12804  65 PDPGqgplaGLLAAL----RAAPGADAVLVLaCDMPFLTPELLRRLLAAAEESGADIV 118
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-69 3.72e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 46.69  E-value: 3.72e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434599840   1 MSTKGIILAGGSGTRLhpitrATSKQLLPVYDKPMIYYPLATLMLAGIREVLVInTPHEQDMFQRLLGD 69
Cdd:COG2068     2 SKVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LGADAEEVAAALAG 64
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
6-67 4.54e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.67  E-value: 4.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434599840   6 IILAGGSGTRL---HPitratsKQLLPVYDKPMIYYPLATLMLAG-IREVLVINTPHEQDMFQRLL 67
Cdd:PRK00155    7 IIPAAGKGSRMgadRP------KQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 5-76 6.35e-06

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 46.00  E-value: 6.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434599840   5 GIILAGGSGTRLHPITRATSKQLLPV---YDkpMIYYPLATLMLAGIREVLVInTPHEQDMFQRLLGDGSQWGID 76
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVL-TQYKSRSLNDHLGSGKEWDLD 72
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-146 2.27e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 45.62  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   1 MSTKGIILAGGSGTRLHpitRATSKQLLPVYDKPMIYYPLATLMLAGI-REVLVINTPHEQ--DMFQRLLGDGSQwgidi 77
Cdd:PRK14353    4 RTCLAIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPsRVAVVVGPGAEAvaAAAAKIAPDAEI----- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434599840  78 ryAVQPSPDGLAQAFTIGRD-FVDGKPSCLVL-GDNIFYGHGFTERLKRAAAREHGATVFGYWVRDPERYG 146
Cdd:PRK14353   76 --FVQKERLGTAHAVLAAREaLAGGYGDVLVLyGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYG 144
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 5-168 3.29e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.82  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   5 GIILAGGSGTRLHPITRATSKQLLP---VYDkpMIYYPLATLMLAGIRE--VLVINTPHEQD--------MF-------- 63
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRiyVLTQYKSHSLDrhisqtwrLSgllgnyit 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  64 -----QRLlgdGSQWgidirYavQPSPDGLAQAFTIGRDFvdgKPS--CLVLGDNIfYGHGFTERLKRAAAREHGATVFG 136
Cdd:PRK00844   86 pvpaqQRL---GKRW-----Y--LGSADAIYQSLNLIEDE---DPDyvVVFGADHV-YRMDPRQMVDFHIESGAGVTVAA 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1434599840 137 ywVRDP----ERYGVAEFDGAGKVIGLEEKPAQPKS 168
Cdd:PRK00844  152 --IRVPreeaSAFGVIEVDPDGRIRGFLEKPADPPG 185
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-168 4.14e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 44.45  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   3 TKGIILAGGSGTRLHPIT--RAtskqllpvydKPMIY---------YPLATLMLAGIREVLVInTPHEQDMFQRLLGDGs 71
Cdd:PRK00725   16 TLALILAGGRGSRLKELTdkRA----------KPAVYfggkfriidFALSNCINSGIRRIGVL-TQYKAHSLIRHIQRG- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  72 qWG---------IDIRYAVQPSPD-----GLAQAFTIGRDFVDG-KPS-CLVL-GDNIfYGHGFTERLkrAAAREHGA-- 132
Cdd:PRK00725   84 -WSffreelgefVDLLPAQQRVDEenwyrGTADAVYQNLDIIRRyDPKyVVILaGDHI-YKMDYSRML--ADHVESGAdc 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1434599840 133 TVFGYWVRDPE--RYGVAEFDGAGKVIGLEEKPAQPKS 168
Cdd:PRK00725  160 TVACLEVPREEasAFGVMAVDENDRITAFVEKPANPPA 197
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-58 9.01e-05

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 43.52  E-value: 9.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434599840   1 MSTKGIILAGGSGTRLHPITRATS-KQLLPVY-DKPMIYyplATLM----LAGIREVLVI-NTPH 58
Cdd:COG0836     1 SMIYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ---QTVErlagLVPPENILVVtNEEH 62
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-58 9.77e-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: 42.18  E-value: 9.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1434599840   8 LAGGSGTRLhpitRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPH 58
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPN 47
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 4-36 9.86e-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: 9.86e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1434599840   4 KGIILAGGSGTRLHPITR-ATSKQLLPVY-DKPMI 36
Cdd:cd02509     2 YPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLL 36
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 5-60 2.52e-04

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 41.44  E-value: 2.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1434599840   5 GIILAGGSGTRLHPITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVINTPHEQ 60
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSD 58
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-61 2.96e-04

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 40.95  E-value: 2.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434599840   1 MSTKGIILAGGSGTRLhpitrATSKQLLPVYDKPMIYYPLATlmLAGIREVLVINTPHEQD 61
Cdd:COG0746     3 MPITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRPER 56
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-182 7.04e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   1 MSTKGIILAGGSGTRlhpITRATSKQLLPVYDKPMIYYPLATLMLAGIREVLVInTPHEQDMFQRLLGDGSQwgidirYA 80
Cdd:PRK14354    1 MNRYAIILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTV-VGHGAEEVKEVLGDRSE------FA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840  81 VQPSPDGLAQAFTIGRDFVDGKP-SCLVL-GDNIFyghgFT-ERLKRAAA--REHG--ATVFGYWVRDPERYGVAEFDGA 153
Cdd:PRK14354   71 LQEEQLGTGHAVMQAEEFLADKEgTTLVIcGDTPL----ITaETLKNLIDfhEEHKaaATILTAIAENPTGYGRIIRNEN 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1434599840 154 GKVIGL-EEKPAQP---KSHYAVTGLYFYDGRV 182
Cdd:PRK14354  147 GEVEKIvEQKDATEeekQIKEINTGTYCFDNKA 179
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 5-66 7.56e-04

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.48  E-value: 7.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434599840   5 GIILAGGSGTRLhpitrATSKQLLPVYDKPMIYYPLATlmLAGIREVLVINTPHEQDMFQRL 66
Cdd:cd02503     3 GVILAGGKSRRM-----GGDKALLELGGKPLLEHVLER--LKPLVDEVVISANRDQERYALL 57
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 5-54 3.24e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 38.68  E-value: 3.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434599840   5 GIILAGGSGTRLHPITRATSKQLLPV---YDkpMIYYPLATLMLAGIREVLVI 54
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 5-54 3.42e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 38.71  E-value: 3.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1434599840   5 GIILAGGSGTRLHPITRATSKQLLPVYDK-PMIYYPLATLMLAGIREVLVI 54
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 6-64 4.98e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase


Pssm-ID: 215387  Cd Length: 252  Bit Score: 37.79  E-value: 4.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434599840   6 IILAGGSGTRLHPitrATSKQLLPVYDKPMIYYPLATLM-LAGIREVLVINTPHEQDMFQ 64
Cdd:PLN02728   28 ILLAGGVGKRMGA---NMPKQYLPLLGQPIALYSLYTFArMPEVKEIVVVCDPSYRDVFE 84
 
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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