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Conserved domains on  [gi|2796359215|ref|WP_373092871|]
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glucose-1-phosphate thymidylyltransferase RfbA [Zhongshania sp.]

Protein Classification

glucose-1-phosphate thymidylyltransferase( domain architecture ID 11492097)

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

EC:  2.7.7.24
Gene Ontology:  GO:0008879|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
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 6-290 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: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQTVE 245
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2796359215 246 HRQGLKVACLEEIAYRQGWISTEQLLQQGEALKKTGYGEYLLRVA 290
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
 
Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 6-290 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: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQTVE 245
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2796359215 246 HRQGLKVACLEEIAYRQGWISTEQLLQQGEALKKTGYGEYLLRVA 290
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-290 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 552.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQTVE 245
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2796359215 246 HRQGLKVACLEEIAYRQGWISTEQLLQQGEALKKTGYGEYLLRVA 290
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-244 4.68e-170

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: 470.13  E-value: 4.68e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQTV 244
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-293 1.04e-151

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 426.01  E-value: 1.04e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   3 KKYKGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYA 82
Cdd:PRK15480    2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  83 EQPSPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIE 162
Cdd:PRK15480   82 VQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 163 EKPAKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQ 242
Cdd:PRK15480  162 EKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIA 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2796359215 243 TVEHRQGLKVACLEEIAYRQGWISTEQLLQQGEALKKTGYGEYLLRVAAGY 293
Cdd:PRK15480  242 TIEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-241 4.38e-102

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: 298.40  E-value: 4.38e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDK-PMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQ 84
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  85 PSPDGLAQAFTIGADFIGNDNVS-LVLGDNIFYGQRFSDNLKSAVAKES--GATVFGYHVTDPERFGVVEFGDDGKAISI 161
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSDvLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 162 EEKPAKPKSP-YAVTGLYFYDNDVVE-IARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQ 239
Cdd:pfam00483 161 VEKPKLPKASnYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2796359215 240 FV 241
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 6-290 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: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQTVE 245
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2796359215 246 HRQGLKVACLEEIAYRQGWISTEQLLQQGEALKKTGYGEYLLRVA 290
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-290 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 552.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:COG1209    82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQTVE 245
Cdd:COG1209   162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2796359215 246 HRQGLKVACLEEIAYRQGWISTEQLLQQGEALKKTGYGEYLLRVA 290
Cdd:COG1209   242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-244 4.68e-170

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: 470.13  E-value: 4.68e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:cd02538    82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQTV 244
Cdd:cd02538   162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-293 1.04e-151

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 426.01  E-value: 1.04e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   3 KKYKGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYA 82
Cdd:PRK15480    2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  83 EQPSPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIE 162
Cdd:PRK15480   82 VQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 163 EKPAKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQFVQ 242
Cdd:PRK15480  162 EKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIA 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2796359215 243 TVEHRQGLKVACLEEIAYRQGWISTEQLLQQGEALKKTGYGEYLLRVAAGY 293
Cdd:PRK15480  242 TIEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-241 4.38e-102

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: 298.40  E-value: 4.38e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDK-PMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQ 84
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  85 PSPDGLAQAFTIGADFIGNDNVS-LVLGDNIFYGQRFSDNLKSAVAKES--GATVFGYHVTDPERFGVVEFGDDGKAISI 161
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSDvLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 162 EEKPAKPKSP-YAVTGLYFYDNDVVE-IARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFAWLDTGTHDSLIDAGQ 239
Cdd:pfam00483 161 VEKPKLPKASnYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2796359215 240 FV 241
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-241 2.40e-66

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: 207.04  E-value: 2.40e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDlPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQrFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFgDDGKAISIEEKP 165
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG-ISPLVRDFLEEDADASILLAEVEDPRRFGVAVV-DDGRIVRLVEKP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFaWLDTGTHDSLIDAGQFV 241
Cdd:cd04189   159 KEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 7-229 3.11e-58

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: 185.86  E-value: 3.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPtdLPG-FQRLLGDGSQFGTNIAYAEQP 85
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGY--LGEqIEEYFGDGSKFGVNIEYVVQE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQrFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:cd04181    79 EPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKpsPRGELEITDVNLAYLQRGDLSVeVLGRGFaWLDTG 229
Cdd:cd04181   158 TLPESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 6-241 2.33e-56

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: 185.30  E-value: 2.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQrFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEKP 165
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDG-ISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGFaWLDTGTHDSLIDAGQFV 241
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLI 234
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 6-237 3.56e-43

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: 151.98  E-value: 3.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDlPGFQRLLGDGSQFGTNIAYAEQP 85
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIgNDNVSLVLGDNIFygqrfSDNLKSAVAKESGATVFGYHVTDPERFGVVEFgDDGKAISIEEKP 165
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVET-DGGRVTGIVEKP 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796359215 166 AKPKSPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGRGfaWLDTGTHDSLIDA 237
Cdd:TIGR03992 154 ENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDA 223
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 6-237 1.04e-40

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 141.06  E-value: 1.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDIlVISTptdlpG-----FQRLLGDGSQFGTNIA 80
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINV-----GylaeqIEEYFGDGSRFGVRIT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  81 YAEQPSP----DGLAQAftigADFIGNDNVSLVLGDnIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDG 156
Cdd:COG1208    75 YVDEGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 157 KAISIEEKPAKPKSPYAVTGLYFYDNDVVEIArnikpsPRGE-LEITDVNLAYLQRGDLSVEVLgRGFaWLDTGTHDSLI 235
Cdd:COG1208   150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLL 221


                  ..
gi 2796359215 236 DA 237
Cdd:COG1208   222 EA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-237 2.11e-27

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: 107.23  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTP------------------------TD 61
Cdd:cd02541     2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdrsyeleetlekkgkTD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  62 LPGFQRLLGDGSqfgtNIAYAEQPSPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQrfSDNLKS--AVAKESGATVFGY 139
Cdd:cd02541    82 LLEEVRIISDLA----NIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSK--EPCLKQliEAYEKTGASVIAV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 140 HVTDPE---RFGVVE-FGDDGKAISIE---EKPaKPK---SPYAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLAYL 209
Cdd:cd02541   156 EEVPPEdvsKYGIVKgEKIDGDVFKVKglvEKP-KPEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLL 234

                         250       260
                  ....*....|....*....|....*....
gi 2796359215 210 QRGD-LSVEVLGRgfaWLDTGTHDSLIDA 237
Cdd:cd02541   235 EEEPvYAYVFEGK---RYDCGNKLGYLKA 260
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 8-234 4.26e-20

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


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 86.41  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDIlVISTptdlpGFQR-----LLGDGSQFGTNIAYA 82
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISV-----NYLAemiedYFGDGSKFGVNISYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  83 EQPSPDGLAQAFTIGADFIgnDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFG--YHVTDPerFGVVEfGDDGKAIS 160
Cdd:cd06426    76 REDKPLGTAGALSLLPEKP--TDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVE-TEGGRITS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796359215 161 IEEkpaKPKSPYAV-TGLYFYDNDVVE-IARNIKpsprgeLEITDVNLAYLQRGD-LSVEVLgRGFaWLDTGTHDSL 234
Cdd:cd06426   151 IEE---KPTHSFLVnAGIYVLEPEVLDlIPKNEF------FDMPDLIEKLIKEGKkVGVFPI-HEY-WLDIGRPEDY 216
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 8-237 1.12e-19

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: 85.30  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDIlVISTptdlpGF-----QRLLGDGSQFGTNIAYA 82
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSV-----GYlaeqiEEYFGDGYRGGIRIYYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  83 EQPSPDGLAQAFTIGADFIGNDNVsLVL-GDNIFYGQrFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISI 161
Cdd:cd06915    76 IEPEPLGTGGAIKNALPKLPEDQF-LVLnGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAF 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796359215 162 EEKPAKPKSPYAVTGLYFYDNDVVEIARNIKPSprgeLEiTDVNLAYLQRGDLSV-EVLGRgfaWLDTGTHDSLIDA 237
Cdd:cd06915   154 VEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRLYGfEVDGY---FIDIGIPEDYARA 222
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-230 9.53e-17

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 78.54  E-value: 9.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYplSV--LMLSGIKDILVISTP------------------------ 59
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiedhfdrsyeleatleakgk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  60 TD-LPGFQRLLGDGsqfgtNIAYAEQPSPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQRfsDNLKS--AVAKESGATV 136
Cdd:COG1210    83 EElLEEVRSISPLA-----NIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEK--PCLKQmiEVYEETGGSV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 137 FGYHVTDPE---RFGVVEFGDDGKAI----SIEEKPAKPKSP--YAVTGLYFYDNDVVEIARNIKPSPRGELEITDVNLA 207
Cdd:COG1210   156 IAVQEVPPEevsKYGIVDGEEIEGGVyrvtGLVEKPAPEEAPsnLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAA 235

                         250       260
                  ....*....|....*....|....
gi 2796359215 208 YLQRGD-LSVEVLGRgfaWLDTGT 230
Cdd:COG1210   236 LAKEEPvYAYEFEGK---RYDCGD 256
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 6-185 4.93e-15

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: 72.63  E-value: 4.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKD-ILVIS-TPTDLPGFQRLLGDgsQFGTNIAYAE 83
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  84 QPSPDGLAQAFTIGADFI-GNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAI-SI 161
Cdd:cd06425    80 ETEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIeRF 159

                         170       180
                  ....*....|....*....|....
gi 2796359215 162 EEKPAKPKSPYAVTGLYFYDNDVV 185
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVL 183
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 7-184 7.33e-15

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 73.96  E-value: 7.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGGSGTRLHPITMGCSKqllpiydkPMIYY---------PLSVLMLSGIKDILVistptdLPGFQ-----RLLGDG 72
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKshslnDHIGSG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  73 SQFGTNI---------AYAEQPSPD---GLAQAFTIGADFIGNDNVSLVL---GDNIfYGQRFSDNLKSAVAKESGATVF 137
Cdd:COG0448    70 KPWDLDRkrggvfilpPYQQREGEDwyqGTADAVYQNLDFIERSDPDYVLilsGDHI-YKMDYRQMLDFHIESGADITVA 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2796359215 138 GYHVTDPE--RFGVVEFGDDGKAISIEEKPAKPKSPYAVTGLYFYDNDV 184
Cdd:COG0448   149 CIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 5-61 1.63e-13

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: 68.07  E-value: 1.63e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2796359215   5 YKGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTD 61
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-237 1.68e-12

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: 65.28  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDIlVISTpTDLPG-FQRLLGDgSQFGTNIAYAEQ 84
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNT-HHLADqIEAHLGD-SRFGLRITISDE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  85 P-----SPDGLAQAftigADFIGNDNVSLVLGDnIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAI 159
Cdd:cd06422    78 PdelleTGGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDADGR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796359215 160 sIEEKPAKPKSPYAVTGLYFYDNDVVeiaRNIKPSPrgeLEITDVNLAYLQRGDLSVEVLgRGFaWLDTGTHDSLIDA 237
Cdd:cd06422   153 -LRRGGGGAVAPFTFTGIQILSPELF---AGIPPGK---FSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-203 1.54e-11

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 63.77  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   2 TKKYKGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVIS------------TPTDLPGF---- 65
Cdd:PRK13389    6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEAMlekr 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  66 -QRLLGDGSQF----GTNIAYAEQPSPDGLAQAFTIGADFIGNDNVSLVLGDNIF--YG------------QRFSDNLKS 126
Cdd:PRK13389   86 vKRQLLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYEsdlsqdnlaemiRRFDETGHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 127 AVAKESGATVFGYHVTDPErfGV-VEFGDDGKAISIEEKPAKPKSP--YAVTGLYFYDNDVVEIARNIKPSPRGELEITD 203
Cdd:PRK13389  166 QIMVEPVADVTAYGVVDCK--GVeLAPGESVPMVGVVEKPKADVAPsnLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
4-213 8.17e-11

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 61.44  E-value: 8.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   4 KYKGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVIS------------TPTDLPGF------ 65
Cdd:PRK10122    3 NLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  66 QRLLGDGSQF---GTNIAYAEQPSPDGLAQAFTIGADFIGNDNVSLVLGDNIFYGQ-----RFsdNLKSAVAK--ESG-A 134
Cdd:PRK10122   83 RQLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplRY--NLAAMIARfnETGrS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 135 TVFGYHVT-DPERFGVVEF-------GDDGKAISIEEKPAKPK---SPYAVTGLYFYDNDVVEIARNIKPSPRGELEITD 203
Cdd:PRK10122  161 QVLAKRMPgDLSEYSVIQTkepldreGKVSRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240

                         250
                  ....*....|..
gi 2796359215 204 --VNLAYLQRGD 213
Cdd:PRK10122  241 aiAELAKKQSVD 252
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 5-56 1.04e-10

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: 60.34  E-value: 1.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2796359215   5 YKGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVI 56
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 8-212 1.80e-09

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 58.07  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLHPitmGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPtdlpGFQRLlgDGSQFGTNIAYAEQPSP 87
Cdd:PRK14358   11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGH----GAEQV--EAALQGSGVAFARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  88 DGLAQAFTIGADFI--GNDNVSLVLGDN-IFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKAISIEEK 164
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2796359215 165 PAKPKSPYAV----TGLYFYDNDVVEIARNI-KPSPRGELEITDVNLAYLQRG 212
Cdd:PRK14358  162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-69 3.63e-09

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 55.91  E-value: 3.63e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215   8 IILAGGSGTRlhpitMG--CSKQLLPIYDKPMIYYPLSVLMLSG-IKDILVISTPTDLPGFQRLL 69
Cdd:PRK00155    7 IIPAAGKGSR-----MGadRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-56 5.14e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 55.63  E-value: 5.14e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2796359215   6 KGIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVI 56
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-227 5.42e-09

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 55.32  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVIStptdlpGFQrllgdGSQF------GTNIAY 81
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT------GYK-----KEQIeellkkYPNIKF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  82 AEQPSPD--GLAQAFTIGADFIGNDnvSLVL-GDNIFYgqrfSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKA 158
Cdd:cd02523    71 VYNPDYAetNNIYSLYLARDFLDED--FLLLeGDVVFD----PSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGV 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215 159 -ISIEEKPAKPKSPYAVT-GLYFYDND----VVEIARNIKPSPRGELEITDVNLAYLQRGDLSVEVLGrGFAWLD 227
Cdd:cd02523   145 lLGIISKAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 7-91 7.77e-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: 55.34  E-value: 7.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGG--SGTRLHPITMGCSKQLLPIYDKPMIYYPLSVL-MLSGIKDILVISTPTDLPgFQRLLGDGSQ-FGTNIAYA 82
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQQeFNVPIRYL 79


                  ....*....
gi 2796359215  83 EQPSPDGLA 91
Cdd:cd06428    80 QEYKPLGTA 88
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 1-237 2.22e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 54.45  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   1 MTKKYKGIILAGGSGTRLHPITMGCSKQLLP---IYDkpMIYYPLSVLMLSGIKDILV------------------ISTP 59
Cdd:PRK00844    2 AMPKVLAIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhisqtwrLSGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  60 TD-----LPGFQRLlgdGSQF--GT--------NIAYAEQPspdglaqaftigadfignDNVSLVLGDNIfYGQRFSDNL 124
Cdd:PRK00844   80 LGnyitpVPAQQRL---GKRWylGSadaiyqslNLIEDEDP------------------DYVVVFGADHV-YRMDPRQMV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 125 KSAVAKESGATVFGYHVTDPE--RFGVVEFGDDGKAISIEEKPAKPK----SP---YAVTGLYFYDNDV-VEIARNIKPS 194
Cdd:PRK00844  138 DFHIESGAGVTVAAIRVPREEasAFGVIEVDPDGRIRGFLEKPADPPglpdDPdeaLASMGNYVFTTDAlVDALRRDAAD 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215 195 PRGELEI-TDVNLAYLQRGDLSV------EVLG-----RGFaWLDTGTHDSLIDA 237
Cdd:PRK00844  218 EDSSHDMgGDIIPRLVERGRAYVydfstnEVPGaterdRGY-WRDVGTIDAYYDA 271
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 8-71 3.00e-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: 53.21  E-value: 3.00e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215   8 IILAGGSGTRLHpitMGCSKQLLPIYDKPMIYYPLSVLMLSG-IKDILVISTPTDLPGFQRLLGD 71
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 7-178 4.27e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 53.72  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGGSGTRLHPITMGCSKQLLPIYDK-PMIYYPLSVLMLSGIKDILVIST--PTDLpgfQRLLGDGSQFGTNIA--- 80
Cdd:PRK05293    6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQyqPLEL---NNHIGIGSPWDLDRIngg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  81 ------YAEQPSPD---GLAQAFTIGADFIGNDNVSLVL---GDNIfYGQRFSDNLKSAVAKESGATVFGYHVTDPE--R 146
Cdd:PRK05293   83 vtilppYSESEGGKwykGTAHAIYQNIDYIDQYDPEYVLilsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEVPWEEasR 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2796359215 147 FGVVEFGDDGKAISIEEKPAKPKSPYAVTGLY 178
Cdd:PRK05293  162 FGIMNTDENMRIVEFEEKPKNPKSNLASMGIY 193
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-219 5.51e-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: 52.52  E-value: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLH---PitmgcsKQLLPIYDKPMIYYPL-SVLMLSGIKDILVISTPTDLpgFQRLLGDgsqfgTNIAYAE 83
Cdd:cd02540     2 VILAAGKGTRMKsdlP------KVLHPLAGKPMLEHVLdAARALGPDRIVVVVGHGAEQ--VKKALAN-----PNVEFVL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  84 QPSPDGLAQAFTIGADFIGNDNvSLVLgdnIFYG----------QRFSDNLKSAVAkesGATVFGYHVTDPERFGVVEFG 153
Cdd:cd02540    69 QEEQLGTGHAVKQALPALKDFE-GDVL---VLYGdvplitpetlQRLLEAHREAGA---DVTVLTAELEDPTGYGRIIRD 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796359215 154 DDGKAISI-EEKPAKP--KSPYAV-TGLYFYDNDVVEIA-RNIKPSP-RGELEITDVnLAYLQRGDLSVEVL 219
Cdd:cd02540   142 GNGKVLRIvEEKDATEeeKAIREVnAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDI-IALAVADGLKVAAV 212
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-61 3.80e-07

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: 49.42  E-value: 3.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796359215   1 MTKKYKGIILAGGSGTRlhpitMGCSKQLLPIYDKPMIYYPLSVlmLSGIKDILVISTPTD 61
Cdd:COG0746     1 MTMPITGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP 54
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-72 5.23e-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: 5.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796359215   8 IILAGGSGTRLHPitmGCSKQLLPIYDKPMIYYPLSVLM-LSGIKDILVISTPTDLPGFQRLLGDG 72
Cdd:cd02516     4 IILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 7-112 7.31e-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: 48.71  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGGSGTRlhpitMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLPGFQRLLGDGSQFGTNIAYAEqps 86
Cdd:cd04182     3 AIILAAGRSSR-----MGGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE--- 74

                          90       100
                  ....*....|....*....|....*...
gi 2796359215  87 pdGLAQAFTIGADFIGN--DNVSLVLGD 112
Cdd:cd04182    75 --GMSSSLAAGLEALPAdaDAVLILLAD 100
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 8-170 2.18e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 48.68  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLHPITMGCSKQLLPIYDK-PMIYYPLSVLMLSGIKDILVIstpTD------------------------- 61
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVL---TQykahslirhiqrgwsffreelgefv 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  62 --LPGFQRLLGDGSQFGTniayaeqpspdglAQAFTIGADFIGNDNVSLVL---GDNIF---YGQRFSDNlksavaKESG 133
Cdd:PRK00725   96 dlLPAQQRVDEENWYRGT-------------ADAVYQNLDIIRRYDPKYVVilaGDHIYkmdYSRMLADH------VESG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2796359215 134 A--TVFGYHVTDPE--RFGVVEFGDDGKAISIEEKPAKPKS 170
Cdd:PRK00725  157 AdcTVACLEVPREEasAFGVMAVDENDRITAFVEKPANPPA 197
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 7-141 2.39e-06

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 47.15  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGGSGTRLHPITMGCSKQLLPI---YDkpMIYYPLSVLMLSGIKDILVI------STPTDLPGFQRLLGDGSQFGT 77
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLtqyksrSLNDHLGSGKEWDLDRKNGGL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796359215  78 NIAYAEQ-PSPD---GLAQAFTIGADFIGNDNVSLVL---GDNIfYGQRFSDNLKSAVAKESGATVfGYHV 141
Cdd:cd02508    79 FILPPQQrKGGDwyrGTADAIYQNLDYIERSDPEYVLilsGDHI-YNMDYREMLDFHIESGADITV-VYKA 147
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-204 7.55e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 47.07  E-value: 7.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPitmGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTPTDLpgFQRLLGDgsqfgtNIAYAEQP 85
Cdd:PRK14357    2 RALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPE------WVKIFLQE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  86 SPDGLAQAFTIGADFIG-NDNVSLVLGDNIFYGQRFSDNL-KSAVAKESGATVFGYHVTDPERFGVVeFGDDGKAISIEE 163
Cdd:PRK14357   71 EQLGTAHAVMCARDFIEpGDDLLILYGDVPLISENTLKRLiEEHNRKGADVTILVADLEDPTGYGRI-IRDGGKYRIVED 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2796359215 164 KPAKPKSPYAV---TGLYFYDND-VVEIARNIKP-SPRGELEITDV 204
Cdd:PRK14357  150 KDAPEEEKKIKeinTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
7-56 7.74e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 45.54  E-value: 7.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGGSGTRlhpitMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVI 56
Cdd:COG2068     6 AIILAAGASSR-----MGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV 50
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 7-68 1.25e-05

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: 44.87  E-value: 1.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796359215   7 GIILAGGSGTRlhpitMGCSKQLLPIYDKPMIYYPLSvlMLSGIKDILVISTPTDLPGFQRL 68
Cdd:cd02503     3 GVILAGGKSRR-----MGGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 7-61 2.53e-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: 43.72  E-value: 2.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215   7 GIILAGGSGTRlhpitMGCSKQLLPIYDKPMIYYplSVLMLSGIKDILVISTPTD 61
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLER--VLERLRPAGDEVVVVANDE 48
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-234 4.64e-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: 44.10  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   6 KGIILAGGSGTRLHPI-TMGCSKQLLPIY-DKPMIYYPLS-VLMLSGIKDILVIstpTDLPGFQRLLGDGSQFGTNIAYA 82
Cdd:cd02509     2 YPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVV---TNEEYRFLVREQLPEGLPEENII 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  83 EQPSPDGLAQAFTIGADFI---GNDNVSLVL------GDNifygQRFSDNLKSAV--AKESGATVFGYHVTDPE-RFGVV 150
Cdd:cd02509    79 LEPEGRNTAPAIALAALYLakrDPDAVLLVLpsdhliEDV----EAFLKAVKKAVeaAEEGYLVTFGIKPTRPEtGYGYI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 151 EFGD--DGKAISIE---EKP--AKPKSpYAVTGLYF-------------------YDNDVVEIARNIKPSPRGELEITDV 204
Cdd:cd02509   155 EAGEklGGGVYRVKrfvEKPdlETAKE-YLESGNYLwnsgiflfraktfleelkkHAPDIYEALEKALAAAGTDDFLRLL 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2796359215 205 NLAYLQRGDLSVE-----------VLGRGFAWLDTGTHDSL 234
Cdd:cd02509   234 EEAFAKIPSISIDyavmektkkvaVVPADFGWSDLGSWDAL 274
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 10-59 7.73e-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: 42.57  E-value: 7.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2796359215  10 LAGGSGTRLHpitmGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTP 59
Cdd:COG2266     1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-220 3.73e-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: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLH---PitmgcsKQLLPIYDKPMIYYPLSVLMLSGIKDILVIStptdlpGFQR-----LLGDgsqfgTNI 79
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVV------GHGAeqvraALAD-----LDV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  80 AYAEQPSPDGLAQAFTIGADFIGNDN-VSLVLgdnifYG----------QRFsdnLKSAVAKESGATVFGYHVTDPERFG 148
Cdd:COG1207    69 EFVLQEEQLGTGHAVQQALPALPGDDgTVLVL-----YGdvpliraetlKAL---LAAHRAAGAAATVLTAELDDPTGYG 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 149 VVEFGDDGKAISI-EEKPAKP--KspyAV----TGLYFYDNDVVEIA-RNIKPS-PRGELEITDVnLAYLQRGDLSV--- 216
Cdd:COG1207   141 RIVRDEDGRVLRIvEEKDATEeqR---AIreinTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV-IAIARADGLKVaav 216

                         250
                  ....*....|
gi 2796359215 217 ------EVLG 220
Cdd:COG1207   217 qpedpwEVLG 226
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
3-56 1.01e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.05  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215   3 KKYKGIILAGGSGTRL-------HPitmgcsKQLLPIY-DKPMIYypLSVLMLSGI---KDILVI 56
Cdd:COG0836     1 SMIYPVILAGGSGTRLwplsresYP------KQFLPLLgEKSLLQ--QTVERLAGLvppENILVV 57
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-189 1.04e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.23  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLHPITmgcSKQLLPIYDKPMIYYPLSVLMLSGIKDILVISTptdlPGFQRLLGDGSQFGTNIAYAEQPSP 87
Cdd:PRK14353    9 IILAAGEGTRMKSSL---PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVG----PGAEAVAAAAAKIAPDAEIFVQKER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  88 DGLAQAFTIGADFI--GNDNVSLVLGDNIFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFG-VVEfgDDGKAISI-EE 163
Cdd:PRK14353   82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrLIV--KGGRLVAIvEE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2796359215 164 KPAKPKSpYAVT----GLY----------------------FYDNDVVEIAR 189
Cdd:PRK14353  160 KDASDEE-RAITlcnsGVMaadgadalalldrvgndnakgeYYLTDIVAIAR 210
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-204 1.13e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRL---HPitmgcsKQLLPIYDKPMIYYPLSVLMLSGIKDILVIStptdlpGF-----QRLLGDGSQfgtni 79
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVV------GHgaeevKEVLGDRSE----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  80 aYAEQPSPDGLAQAFTIGADFIGN-DNVSLVL-GDN-IFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDG 156
Cdd:PRK14354   69 -FALQEEQLGTGHAVMQAEEFLADkEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215 157 KAISI-EEKPAKPKSpYAV----TGLYFYDNDV-VEIARNIKP-SPRGELEITDV 204
Cdd:PRK14354  148 EVEKIvEQKDATEEE-KQIkeinTGTYCFDNKAlFEALKKISNdNAQGEYYLTDV 201
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-165 1.29e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 39.87  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   3 KKYKGIILAGGSGTRLHPITMGCSKQLLPIYDK-PMIYYPLSVLMLSGIKDILV------------ISTPTDLPGFqrll 69
Cdd:PRK02862    2 KRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVltqfnsaslnrhISQTYNFDGF---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  70 gdgSQFGTNIAYAEQP--SPD---GLAQAFTIGADFIGNDNVSLVL---GDNIfYGQRFSDNLKSAVAKESGATVFGYHV 141
Cdd:PRK02862   78 ---SGGFVEVLAAQQTpeNPSwfqGTADAVRKYLWHFQEWDVDEYLilsGDQL-YRMDYRLFVQHHRETGADITLAVLPV 153

                         170       180
                  ....*....|....*....|....*.
gi 2796359215 142 T--DPERFGVVEFGDDGKAISIEEKP 165
Cdd:PRK02862  154 DekDASGFGLMKTDDDGRITEFSEKP 179
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 7-56 1.32e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 39.84  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2796359215   7 GIILAGGSGTRLHPITMGCSKQLLPI---YDkpMIYYPLSVLMLSGIKDILVI 56
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-212 3.54e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.57  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215   8 IILAGGSGTRLHPitmGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVIStptdlpGFQ------RLLGDGsqfgtNIAY 81
Cdd:PRK14355    7 IILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVV------GHQaekvreHFAGDG-----DVSF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215  82 AEQPSPDGLAQAFTIGADFI--GNDNVSLVLGDN-IFYGQRFSDNLKSAVAKESGATVFGYHVTDPERFGVVEFGDDGKA 158
Cdd:PRK14355   73 ALQEEQLGTGHAVACAAPALdgFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRV 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796359215 159 ISI-EEKPAKPKSPYAV---TGLYFYDNDVVE--IARNIKPSPRGELEITDVNLAYLQRG 212
Cdd:PRK14355  153 LRIvEEKDATPEERSIRevnSGIYCVEAAFLFdaIGRLGNDNAQGEYYLTDIVAMAAAEG 212
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 8-71 7.25e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 37.52  E-value: 7.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796359215   8 IILAGGSGTRLHPitmGCSKQLLPIYDKPMIYYPLSVLM-LSGIKDILVISTPTDLPGFQRLLGD 71
Cdd:PRK09382    9 VIVAAGRSTRFSA---EVKKQWLRIGGKPLWLHVLENLSsAPAFKEIVVVIHPDDIAYMKKALPE 70
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 7-56 8.70e-03

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: 36.82  E-value: 8.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2796359215   7 GIILAGGSGTRLHPITMGCSKQLLPIYDKPMIYYPLSVLMLSGIKDILVI 56
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
 
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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