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Conserved domains on  [gi|2272037971|ref|WP_254468582|]
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glucose-1-phosphate thymidylyltransferase RfbA [Pseudomonas donghuensis]

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];
3-289 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 562.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2272037971 243 HRQGLKVACLEEIAYQKQWISRDRLLERAQALGKTGYGQYLYSLADE 289
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 562.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2272037971 243 HRQGLKVACLEEIAYQKQWISRDRLLERAQALGKTGYGQYLYSLADE 289
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 3-287 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: 543.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2272037971 243 HRQGLKVACLEEIAYQKQWISRDRLLERAQALGKTGYGQYLYSLA 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 3-241 1.33e-174

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: 481.69  E-value: 1.33e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTI 241
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-286 1.83e-143

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 405.21  E-value: 1.83e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2272037971 243 HRQGLKVACLEEIAYQKQWISRDRLLERAQALGKTGYGQYLYSL 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-238 1.10e-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: 292.23  E-value: 1.10e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDK-PMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQ 81
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  82 PSPDGLAQAFLIGEEFIGDDSV-CLILGDNIFHGQGFSEQLLRAIDRPS--GATVFGYWVKDPERFGVVDFDAQGRALSI 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 159 EEKPSQPK-SNYAVTGLYFYDNDVIE-IAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQ 236
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2272037971 237 YV 238
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 562.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2272037971 243 HRQGLKVACLEEIAYQKQWISRDRLLERAQALGKTGYGQYLYSLADE 289
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 3-287 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: 543.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2272037971 243 HRQGLKVACLEEIAYQKQWISRDRLLERAQALGKTGYGQYLYSLA 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 3-241 1.33e-174

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: 481.69  E-value: 1.33e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTI 241
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-286 1.83e-143

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 405.21  E-value: 1.83e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQYVQTIE 242
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2272037971 243 HRQGLKVACLEEIAYQKQWISRDRLLERAQALGKTGYGQYLYSL 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-238 1.10e-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: 292.23  E-value: 1.10e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDK-PMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQ 81
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  82 PSPDGLAQAFLIGEEFIGDDSV-CLILGDNIFHGQGFSEQLLRAIDRPS--GATVFGYWVKDPERFGVVDFDAQGRALSI 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 159 EEKPSQPK-SNYAVTGLYFYDNDVIE-IAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGFAWLDTGTHDSLLEASQ 236
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2272037971 237 YV 238
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 3-238 1.28e-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: 217.82  E-value: 1.28e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI--STPQDLPQYrqlFGDGSQFGIQLHYAE 80
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgPTGEEIKEA---LGDGSRFGVRITYIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  81 QPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDaQGRALSIEE 160
Cdd:cd04189    79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2272037971 161 KPSQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGdLRVE-RFGRGFaWLDTGTHDSLLEASQYV 238
Cdd:cd04189   157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRG-RRVGySIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 4-226 3.21e-65

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: 203.58  E-value: 3.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDlPQYRQLFGDGSQFGIQLHYAEQPS 83
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  84 PDGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKPS 163
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2272037971 164 QPKSNYAVTGLYFYDNDVIEIAKGVKPsaRGELEITDITNAYLKRGDLRVERFgrGFAWLDTG 226
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 3-238 6.47e-59

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


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 191.85  E-value: 6.47e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEQP 82
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEKP 162
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 163 SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITD-----ITNAYlKRGDLRVERFgrgfaWLDTGTHDSLLEASQY 237
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDaiqwlIEKGY-KVGGSKVTGW-----WKDTGKPEDLLDANRL 233


                  .
gi 2272037971 238 V 238
Cdd:TIGR01208 234 I 234
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 2-238 3.97e-51

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: 172.78  E-value: 3.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   2 TKGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDlPQYRQLFGDGSQFGIQLHYAEQ 81
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  82 PSPDGLAQAFLIGEEFIgDDSVCLILGDNIFhgqgfSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAqGRALSIEEK 161
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2272037971 162 PSQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVERFGRGfaWLDTGTHDSLLEASQYV 238
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 3-238 5.46e-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: 157.24  E-value: 5.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLIStpQDLP-QYRQLFGDGSQFGIQLHYAEQ 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV--GYLAeQIEEYFGDGSRFGVRITYVDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  82 PSPDGLAQAFLIGEEFIGDDSVCLILGDNIFhGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIEEK 161
Cdd:COG1208    79 GEPLGTGGALKRALPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2272037971 162 PSQPKSNYAVTGLYFYDNDVIE-IAKGVKPSargeleITDITNAYLKRGDLRVERFgRGFaWLDTGTHDSLLEASQYV 238
Cdd:COG1208   158 PEEPPSNLINAGIYVLEPEIFDyIPEGEPFD------LEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANALL 227
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 2-235 1.54e-33

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


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 123.41  E-value: 1.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   2 TKGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQ------------DLPQyrQLFGDG 69
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfdrsyELEE--TLEKKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  70 SQ----------FGIQLHYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQGF-SEQLLRAIDRpSGATVFGYWV 138
Cdd:cd02541    79 KTdlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYEK-TGASVIAVEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 139 KDPE---RFGVVDFDAQG----RALSIEEKPSQ--PKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRG 209
Cdd:cd02541   158 VPPEdvsKYGIVKGEKIDgdvfKVKGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEE 237

                         250       260
                  ....*....|....*....|....*..
gi 2272037971 210 DLRVERF-GRgfaWLDTGTHDSLLEAS 235
Cdd:cd02541   238 PVYAYVFeGK---RYDCGNKLGYLKAT 261
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-234 5.57e-25

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: 99.51  E-value: 5.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREIlLIST---PQDLPQYrqlFGDGSQFGIQLHYAEQ 81
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVnylAEMIEDY---FGDGSKFGVNISYVRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  82 PSPDGLAQAFLIGEEFIgDDSVCLILGDnIFHGQGFSEQLLRAIDRPSGATVFG--YWVKDPerFGVVDFDaQGRALSIE 159
Cdd:cd06426    78 DKPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETE-GGRITSIE 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2272037971 160 EKPSQpksNYAV-TGLYFYDNDVIE-IAKGVKpsargeLEITDITNAYLKRGDlRVERFG-RGFaWLDTGTHDSLLEA 234
Cdd:cd06426   153 EKPTH---SFLVnAGIYVLEPEVLDlIPKNEF------FDMPDLIEKLIKEGK-KVGVFPiHEY-WLDIGRPEDYEKA 219
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-234 2.93e-24

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: 97.62  E-value: 2.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLiSTPQDLPQYRQLFGDGSQFGIQLHYAEQPSP 84
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVL-SVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  85 DGLAQAFLIGEEFIGDDSVCLILGDNIFHGqGFSEqLLRAIDRPSG-ATVFGYWVKDPERFGVVDFDAQGRALSIEEKPS 163
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDV-DLLA-LLAALRASGAdATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2272037971 164 QPKSNYAVTGLYFYDNDVIEIAKGVKPSargeLEiTDITNAYLKRGDLRV----ERFgrgfawLDTGTHDSLLEA 234
Cdd:cd06915   159 GAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRLYGfevdGYF------IDIGIPEDYARA 222
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-234 7.45e-24

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 97.80  E-value: 7.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   2 TKGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTP------------QDLpqYRQLFGDG 69
Cdd:COG1210     4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfdrsYEL--EATLEAKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  70 ----------SQFGIQLHYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFHGQ-GFSEQLLRAIDRpSGATVFGywV 138
Cdd:COG1210    82 keelleevrsISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkPCLKQMIEVYEE-TGGSVIA--V 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 139 K--DPE---RFGVVDFDAQ-GRALSIE---EKPSQPK--SNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLK 207
Cdd:COG1210   159 QevPPEevsKYGIVDGEEIeGGVYRVTglvEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAK 238

                         250       260
                  ....*....|....*....|....*...
gi 2272037971 208 RGDLRVERF-GRgfaWLDTGTHDSLLEA 234
Cdd:COG1210   239 EEPVYAYEFeGK---RYDCGDKLGYLKA 263
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 3-182 3.82e-21

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: 89.58  E-value: 3.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILL-IS-TPQDLPQYRQLFGDgsQFGIQLHYAE 80
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNyRPEDMVPFLKEYEK--KLGIKITFSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  81 QPSPDGLAQAFLIGEEFIGDDSVC-LILGDNIFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQ-GRALSI 158
Cdd:cd06425    80 ETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERF 159

                         170       180
                  ....*....|....*....|....
gi 2272037971 159 EEKPSQPKSNYAVTGLYFYDNDVI 182
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVL 183
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-234 1.50e-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: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREIlLIST---PQdlpQYRQLFGDgSQFGIQLHYA 79
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlAD---QIEAHLGD-SRFGLRITIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  80 EQP-----SPDGLAQAfligEEFIGDDSVCLILGDNIFHGqGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDF--DAQ 152
Cdd:cd06422    76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDAD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 153 GRalsIEEKPSQPKSNYAVTGLYFYDNDVIEiakGVKPsarGELEITDITNAYLKRGDLRVERFgRGFaWLDTGTHDSLL 232
Cdd:cd06422   151 GR---LRRGGGGAVAPFTFTGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLL 219


                  ..
gi 2272037971 233 EA 234
Cdd:cd06422   220 AA 221
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-200 1.66e-15

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 74.94  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI--STPQDLPQY----------------RQ 64
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthSSKNSIENHfdtsfeleamlekrvkRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  65 LFGDGSQF---GIQLHYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNIFH------GQGFSEQLLRAIDRPSGATVFG 135
Cdd:PRK13389   90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDeyesdlSQDNLAEMIRRFDETGHSQIMV 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2272037971 136 YWVKDPERFGVVdfDAQGRAL---------SIEEKP--SQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITD 200
Cdd:PRK13389  170 EPVADVTAYGVV--DCKGVELapgesvpmvGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-215 4.70e-15

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: 72.65  E-value: 4.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDlPQYRQLFGDgsQFGIQLHYAEQPSP 84
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKK--YPNIKFVYNPDYAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  85 DGLAQAFLIGEEFIGDDsvCLIL-GDNIFHGQGFSEqlLRAIDRPSGATVFGYWVKDPERFgVVDFDAQGRALSIEEKPS 163
Cdd:cd02523    79 TNNIYSLYLARDFLDED--FLLLeGDVVFDPSILER--LLSSPADNAILVDKKTKEWEDEY-VKDLDDAGVLLGIISKAK 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2272037971 164 QPKSNYAVT-GLYFYDND----VIEIAKGVKPSARGELEITDITNAYLKRGDLRVER 215
Cdd:cd02523   154 NLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKD 210
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
3-200 1.38e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 69.53  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLIS------------TPQDLPQY------RQ 64
Cdd:PRK10122    5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  65 LFGDGSQF---GIQLHYAEQPSPDGLAQAFLIGEEFIGDDSVCLILGDNI-------------------FHGQGFSEQLL 122
Cdd:PRK10122   85 LLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVViddasadplrynlaamiarFNETGRSQVLA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 123 RAI-DRPSGATVFGywVKDPerfgvVDFDAQ-GRALSIEEKPSQPK---SNYAVTGLYFYDNDVIEIAKGVKPSARGELE 197
Cdd:PRK10122  165 KRMpGDLSEYSVIQ--TKEP-----LDREGKvSRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQ 237


                  ...
gi 2272037971 198 ITD 200
Cdd:PRK10122  238 LTD 240
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-66 1.03e-12

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: 65.76  E-value: 1.03e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLF 66
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 4-235 1.07e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 64.33  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLHPITLGVSKqllpiydkPMIYY---------PISVLMLAGIREILListpqdLPQYR----------- 63
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKshslndhigsg 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  64 ---QLfgDGSQFGIQLHYAEQPSPD-----GLAQAFLIGEEFIGDDSV--CLIL-GDNIFHgQGFSEQLLRAIDRPSGAT 132
Cdd:COG0448    70 kpwDL--DRKRGGVFILPPYQQREGedwyqGTADAVYQNLDFIERSDPdyVLILsGDHIYK-MDYRQMLDFHIESGADIT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 133 VFGYWV--KDPERFGVVDFDAQGRALSIEEKPSQPKSNYAVTGLYFYDNDV-IEIakgVKPSARGELE--ITDITNAYLK 207
Cdd:COG0448   147 VACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVlIEL---LEEDAPNSSHdfGKDIIPRLLD 223

                         250       260
                  ....*....|....*....|....*...
gi 2272037971 208 RGDLRVERFgRGFaWLDTGTHDSLLEAS 235
Cdd:COG0448   224 RGKVYAYEF-DGY-WRDVGTIDSYYEAN 249
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
3-238 1.68e-11

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 62.57  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLpQYRQLFGdgsQFGIQLHYAEQP 82
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAE-LIEEALA---RPGPDVTFVYNP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  83 SPD--GLAQAFLIGEEFIGDDsvCLIL-GDNIFHGQGFSEqlLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSIE 159
Cdd:COG1213    77 DYDetNNIYSLWLAREALDED--FLLLnGDVVFDPAILKR--LLASDGDIVLLVDRKWEKPLDEEVKVRVDEDGRIVEIG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 160 EKPSQPKSNYAVTGLYFYDND----VIEIAKGVKPSARGELEITDITNAYLKRG-DLRVERFGRGFaWLDTGTHDSLLEA 234
Cdd:COG1213   153 KKLPPEEADGEYIGIFKFSAEgaaaLREALEALIDEGGPNLYYEDALQELIDEGgPVKAVDIGGLP-WVEIDTPEDLERA 231


                  ....
gi 2272037971 235 SQYV 238
Cdd:COG1213   232 EELF 235
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-53 1.85e-11

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 62.27  E-value: 1.85e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2272037971   3 KGIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI 53
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-68 5.58e-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: 55.14  E-value: 5.58e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2272037971   5 IVLAGGSGTRLHpitLGVSKQLLPIYDKPMIYYPISVLMLAG-IREILLISTPQDLPQYRQLFGD 68
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-215 9.31e-09

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 54.95  E-value: 9.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGG--SGTRLHPITLGVSKQLLPIYDKPMIYYPISVL-MLAGIREILLISTPQDLpQYRQLFGDGSQ-FGIQLHYA 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPES-VFSDFISDAQQeFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  80 EQPSPDGLAQAF-----LIGEefiGDDSVCLILGDNIFHGQGFSEqLLRAIDR-PSGATVFGYWV--KDPERFGVVDFDA 151
Cdd:cd06428    80 QEYKPLGTAGGLyhfrdQILA---GNPSAFFVLNADVCCDFPLQE-LLEFHKKhGASGTILGTEAsrEQASNYGCIVEDP 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2272037971 152 Q-GRALSIEEKPSQPKSNYAVTGLYFYDNDVIEIAKGVKPSARGELEITDITNAYLKRGDLRVER 215
Cdd:cd06428   156 StGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQ 220
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-214 2.18e-08

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: 53.67  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTR--------LHPItLGvskqllpiydKPMIYYPISVLMLAGIREILLIsTPQDLPQYRQLFGDgsqfgIQL 76
Cdd:cd02540     2 VILAAGKGTRmksdlpkvLHPL-AG----------KPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALAN-----PNV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  77 HYAEQPSPDGLAQAFLIGEEFI-GDDSVCLIL-GDN--IfhgqgfSEQLLRAI-----DRPSGATVFGYWVKDPERFGVV 147
Cdd:cd02540    65 EFVLQEEQLGTGHAVKQALPALkDFEGDVLVLyGDVplI------TPETLQRLleahrEAGADVTVLTAELEDPTGYGRI 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2272037971 148 DFDAQGRALSI-EEK---PSQPKSNYAVTGLYFYDNDVIEIA-KGVKPS-ARGELEITDITnAYLKRGDLRVE 214
Cdd:cd02540   139 IRDGNGKVLRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDII-ALAVADGLKVA 210
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 4-234 4.84e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 53.68  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLHPITLGVSKQLLP---IYDkpMIYYPISVLMLAGIREILListpqdLPQYRqlfgdgSQ--------- 71
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYV------LTQYK------SHsldrhisqt 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  72 ---FGIQLHYAEqPSP----------DGLAQAFLIGEEFIGD---DSVCLILGDNIFHGQgfSEQLLRA-IDRPSGATVF 134
Cdd:PRK00844   74 wrlSGLLGNYIT-PVPaqqrlgkrwyLGSADAIYQSLNLIEDedpDYVVVFGADHVYRMD--PRQMVDFhIESGAGVTVA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 135 GYWV--KDPERFGVVDFDAQGRALSIEEKPSQPKS-------NYAVTGLYFYDNDVIEIAkgVKPSARGELEITD----I 201
Cdd:PRK00844  151 AIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDALVDA--LRRDAADEDSSHDmggdI 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2272037971 202 TNAYLKRGDLRVERF-----------GRGFaWLDTGTHDSLLEA 234
Cdd:PRK00844  229 IPRLVERGRAYVYDFstnevpgaterDRGY-WRDVGTIDAYYDA 271
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-65 2.12e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 50.52  E-value: 2.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2272037971   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAG-IREILLISTPQDLPQYRQL 65
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAEL 65
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-65 5.52e-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: 5.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2272037971   5 IVLAGGSGTRLHpitLGVSKQLLPIYDKPMIYYPISVLM-LAGIREILLISTPQDLPQYRQL 65
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKEL 62
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 5-209 1.47e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 49.21  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFgiqlhyAEQPSP 84
Cdd:PRK14358   11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAF------ARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  85 DGLAQAFLIGEEFI--GDDSVCLILGDNIFhgqgFSEQLLRAI-----DRPSGATVFGYWVKDPERFGVVDFDAQGRALS 157
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTPL----LRPDTLRALvadhrAQGSAMTILTGELPDATGYGRIVRGADGAVER 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2272037971 158 IEEKPSQPKSNYAV----TGLYFYDNDVIEIAKGV-KPSARGELEITDITNAYLKRG 209
Cdd:PRK14358  158 IVEQKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-209 1.51e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.97  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDlPQYRQLFGDGSQFGIQLHyAEQ--- 81
Cdd:PRK14355    7 IILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQA-EKVREHFAGDGDVSFALQ-EEQlgt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  82 --------PSPDGLAQAFLIgeeFIGDdsVCLILGDNIfhgqgfseQLLRAIDRPSGA--TVFGYWVKDPERFGVVDFDA 151
Cdd:PRK14355   82 ghavacaaPALDGFSGTVLI---LCGD--VPLLRAETL--------QGMLAAHRATGAavTVLTARLENPFGYGRIVRDA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2272037971 152 QGRALSI-EEKPSQPKS---NYAVTGLYFYDNDVIEIA-KGVK-PSARGELEITDITNAYLKRG 209
Cdd:PRK14355  149 DGRVLRIvEEKDATPEErsiREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEG 212
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 4-137 1.33e-05

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: 44.86  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLhpitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLFGDGSQFGIQLHYAEqps 83
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE--- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2272037971  84 pdGLAQAFLIGEEFIGDD-SVCLI-LGDNIFHGQGFSEQLLRAIDRPSGATVFGYW 137
Cdd:cd04182    75 --GMSSSLAAGLEALPADaDAVLIlLADQPLVTAETLRALIDAFREDGAGIVAPVY 128
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 4-133 1.67e-05

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 44.11  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRlhpitLGVSKQLLPIYDKPMIYYPISVLMLAGiREILLISTPQDLPQYRQLFGdgsqfgiqLHYAEQPS 83
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2272037971  84 PD-GLAQAFLIGEEFIGDDSVCLIL-GDNIFHGQGFSEQLLRAIDRPSGATV 133
Cdd:pfam12804  67 PGqGPLAGLLAALRAAPGADAVLVLaCDMPFLTPELLRRLLAAAEESGADIV 118
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-65 4.38e-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: 4.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2272037971   1 MTK---GIVLAGGSGTRlhpitLGVSKQLLPIYDKPMIYYPISVLMLAGIReiLLISTPQDlPQYRQL 65
Cdd:COG0746     1 MTMpitGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQVDE--VVIVANRP-ERYAAL 60
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-109 4.62e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 43.23  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   1 MTKGIVLAGGSGTRLhpitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLIsTPQDLPQYRQLFgdgSQFGIQLHYAE 80
Cdd:COG2068     3 KVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LGADAEEVAAAL---AGLGVRVVVNP 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2272037971  81 QPSpDGLAQAFLIGEEFIGD--DSVCLILGD 109
Cdd:COG2068    74 DWE-EGMSSSLRAGLAALPAdaDAVLVLLGD 103
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 4-91 7.06e-05

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: 42.91  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLHPITLGVSKQLLPI---YDkpMIYYPISVLMLAGIREILLIsTPQdlpQYRQLF----------GDGS 70
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVL-TQY---KSRSLNdhlgsgkewdLDRK 74

                          90       100
                  ....*....|....*....|....*
gi 2272037971  71 QFGIQLHYAEQ-PSPD---GLAQAF 91
Cdd:cd02508    75 NGGLFILPPQQrKGGDwyrGTADAI 99
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-210 7.68e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 43.67  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTRL---HPitlgvsKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQDLPQYRQLfGDGSQFGIQlhyAEQ 81
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVL-GDRSEFALQ---EEQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  82 PspdGLAQAFLIGEEFIGD-DSVCLIL-GDN-IFHGQGFSEQLLRAIDRPSGATVFGYWVKDPERFGVVDFDAQGRALSI 158
Cdd:PRK14354   76 L---GTGHAVMQAEEFLADkEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEKI 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2272037971 159 -EEK---PSQPKSNYAVTGLYFYDNDVI-EIAKGVKP-SARGELEITDITNAYLKRGD 210
Cdd:PRK14354  153 vEQKdatEEEKQIKEINTGTYCFDNKALfEALKKISNdNAQGEYYLTDVIEILKNEGE 210
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-203 9.81e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.60  E-value: 9.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   3 KGIVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTPQD-----LPQYRQLFGDGSQFGIqlh 77
Cdd:PRK14357    2 RALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAElvkklLPEWVKIFLQEEQLGT--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  78 yaeqpspdglAQAFLIGEEFIGDDSVCLIL-GDNIFHGQGFSEQLLRA-IDRPSGATVFGYWVKDPERFGVVDFDaQGRA 155
Cdd:PRK14357   76 ----------AHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEhNRKGADVTILVADLEDPTGYGRIIRD-GGKY 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2272037971 156 LSIEEKPSQPKSNYAV---TGLYFYDND-VIEIAKGVKP-SARGELEITDITN 203
Cdd:PRK14357  145 RIVEDKDAPEEEKKIKeinTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAVN 197
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 143-235 1.51e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.93  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971 143 RFGVVDFDAQGRALSIEEKPSQPKSNYAVTGLYFYD----NDVIEIAKGVKPSAR--GEleitDITNAYLKRGD-LRVER 215
Cdd:PRK05293  161 RFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNwkrlKEYLIEDEKNPNSSHdfGK----NVIPLYLEEGEkLYAYP 236

                          90       100
                  ....*....|....*....|
gi 2272037971 216 FgRGFaWLDTGTHDSLLEAS 235
Cdd:PRK05293  237 F-KGY-WKDVGTIESLWEAN 254
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 7-56 1.72e-04

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 41.41  E-value: 1.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2272037971   7 LAGGSGTRLHpitlGVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTP 56
Cdd:COG2266     1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-53 3.72e-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: 41.05  E-value: 3.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLHPITLGVSKQLLPIYDKPMIYYPISVLMLAGIREILLI 53
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-201 3.99e-04

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: 41.55  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   5 IVLAGGSGTR--------LHPItLGvskqllpiydKPMIYYPISVLMLAGIREILLISTPQ-DlpQYRQLFGDgsqfgIQ 75
Cdd:COG1207     6 VILAAGKGTRmksklpkvLHPL-AG----------KPMLEHVLDAARALGPDRIVVVVGHGaE--QVRAALAD-----LD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  76 LHYAEQPSPDGLAQAFLIGEEFI-GDDSVCLIL-GDN--IfhgqgfSEQLLRA-----IDRPSGATVFGYWVKDPERFGV 146
Cdd:COG1207    68 VEFVLQEEQLGTGHAVQQALPALpGDDGTVLVLyGDVplI------RAETLKAllaahRAAGAAATVLTAELDDPTGYGR 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2272037971 147 VDFDAQGRALSI-EEK---PSQPKSNYAVTGLYFYDNDVIEIA-KGVKPS-ARGELEITDI 201
Cdd:COG1207   142 IVRDEDGRVLRIvEEKdatEEQRAIREINTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-68 1.17e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 39.01  E-value: 1.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   1 MTKGIVLAGGSGTRLHpitlGVSKQLLPIYDKPMIYYPISVL--MLAGIreilLISTPQDLPQYRQlFGD 68
Cdd:PRK00317    3 PITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERLapQVDEI----VINANRNLARYAA-FGL 63
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-127 2.54e-03

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


Pssm-ID: 396773  Cd Length: 217  Bit Score: 38.47  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLhpitlgVSKQLLPIYDKPMIYYPISVLMLAGIREILLISTpqDLPQYRQlfgDGSQFGIQLHYAEQPS 83
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT--DSEEIAD---VAKEFGAGVVMTSGSL 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2272037971  84 PDGLAQAFLIGEEFIG--DDSVCLILGDNIFHgqgFSEQLLRAIDR 127
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNdhDDIIVNIQGDNPLL---QPEVILKAIET 113
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-35 3.68e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 38.51  E-value: 3.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2272037971   1 MTKGIVLAGGSGTRLHPitlgVS-----KQLLPIY-DKPMI 35
Cdd:COG0836     2 MIYPVILAGGSGTRLWP----LSresypKQFLPLLgEKSLL 38
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 4-163 3.93e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 38.33  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLHPITLGVSKQLLPIYDK-PMIYYPISVLMLAGIREILListpqdLPQY------RQL--------FGD 68
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYV------LTQFnsaslnRHIsqtynfdgFSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2272037971  69 GsqFgIQLHYAEQP--SPD---GLAQA-----FLIGEEFIgdDSVcLIL-GDNIFHgQGFSEQLLRAIDRPSGATVFGYW 137
Cdd:PRK02862   80 G--F-VEVLAAQQTpeNPSwfqGTADAvrkylWHFQEWDV--DEY-LILsGDQLYR-MDYRLFVQHHRETGADITLAVLP 152

                         170       180
                  ....*....|....*....|....*...
gi 2272037971 138 V--KDPERFGVVDFDAQGRALSIEEKPS 163
Cdd:PRK02862  153 VdeKDASGFGLMKTDDDGRITEFSEKPK 180
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 5-70 5.41e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 37.43  E-value: 5.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2272037971   5 IVLAGGSGTRLHPitlGVSKQLLPIYDKPMIYYPISVLMLAG-IREILLISTPQDLPQYRQLFGDGS 70
Cdd:pfam01128   2 VIPAAGSGKRMGA---GVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAVSPDDTPEFRQLLGDPS 65
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 4-50 5.42e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 37.91  E-value: 5.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2272037971   4 GIVLAGGSGTRLHPITLGVSKQLLPI---YDkpMIYYPISVLMLAGIREI 50
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKI 53
 
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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