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Conserved domains on  [gi|503409858|ref|WP_013644519|]
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glucose-1-phosphate thymidylyltransferase RfbA [Methanobacterium lacus]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 521.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  81 DEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 161 PENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAI 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503409858 241 QKRQGFYIACLEEISFNNGWIDEDIVLKSAESLEKTDYSKYLVELVKRNGNDI 293
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRARV 293
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 521.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  81 DEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 161 PENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAI 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503409858 241 QKRQGFYIACLEEISFNNGWIDEDIVLKSAESLEKTDYSKYLVELVKRNGNDI 293
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRARV 293
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-287 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 512.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQD 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   82 EPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  162 ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAIQ 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 503409858  242 KRQGFYIACLEEISFNNGWIDEDIVLKSAESLEKTDYSKYLVELVK 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-240 6.46e-165

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: 457.42  E-value: 6.46e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  81 DEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 161 PENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAI 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-287 6.10e-131

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 373.63  E-value: 6.10e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQD 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  82 EPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 162 ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAIQ 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 503409858 242 KRQGFYIACLEEISFNNGWIDEDIVLKSAESLEKTDYSKYLVELVK 287
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 6.09e-93

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: 274.90  E-value: 6.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    2 KGIILAGGSGTRLYPITKAVSKQLLPIYDK-PMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   81 DEPRGLADAFIVGEDFIGEESV-ALVLGDNIFHGHRFSEILKRAASL--DKGAVIFGYYVKNPRPFGVVEFDEEGNVLSV 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKaaDATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  158 EEKPENPK-SNYVVPGLYFYDNSVID-IAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASN 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 503409858  236 YVE 238
Cdd:pfam00483 241 FLL 243
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 521.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  81 DEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 161 PENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAI 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503409858 241 QKRQGFYIACLEEISFNNGWIDEDIVLKSAESLEKTDYSKYLVELVKRNGNDI 293
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRARV 293
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-287 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 512.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQD 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   82 EPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  162 ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAIQ 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 503409858  242 KRQGFYIACLEEISFNNGWIDEDIVLKSAESLEKTDYSKYLVELVK 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-240 6.46e-165

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: 457.42  E-value: 6.46e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  81 DEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 161 PENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAI 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-287 6.10e-131

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 373.63  E-value: 6.10e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQD 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  82 EPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 162 ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASNYVEAIQ 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 503409858 242 KRQGFYIACLEEISFNNGWIDEDIVLKSAESLEKTDYSKYLVELVK 287
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 6.09e-93

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: 274.90  E-value: 6.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    2 KGIILAGGSGTRLYPITKAVSKQLLPIYDK-PMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   81 DEPRGLADAFIVGEDFIGEESV-ALVLGDNIFHGHRFSEILKRAASL--DKGAVIFGYYVKNPRPFGVVEFDEEGNVLSV 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKaaDATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  158 EEKPENPK-SNYVVPGLYFYDNSVID-IAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGMAWLDTGTHIGLLEASN 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 503409858  236 YVE 238
Cdd:pfam00483 241 FLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-237 6.46e-64

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: 200.87  E-value: 6.46e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDlPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  81 DEPRGLADAFIVGEDFIGEESVALVLGDNIFHGhRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDeEGNVLSVEEK 160
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVEK 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503409858 161 PENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYL--KRKELKVELLGrgmAWLDTGTHIGLLEASNYV 237
Cdd:cd04189  158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIdrGRRVGYSIVTG---WWKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-225 1.00e-60

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 192.02  E-value: 1.00e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPtdLPRY-KELLGDGTDLGVEFSYRVQD 81
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGY--LGEQiEEYFGDGSKFGVNIEYVVQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  82 EPRGLADAFIVGEDFIGEESVALVLGDNIFHGHrFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEKP 161
Cdd:cd04181   79 EPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503409858 162 ENPKSNYVVPGLYFYDNSVIDIAKNIapSDRGEIEITSVNDEYLKRKELKVELLgrGMAWLDTG 225
Cdd:cd04181  158 TLPESNLANAGIYIFEPEILDYIPEI--LPRGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-233 1.07e-55

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: 183.37  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRVQD 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   82 EPRGLADAFIVGEDFIGEESVALVLGDNIFHGHrFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDG-ISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503409858  162 ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVnDEYLKRKELKVELLGRGMAWLDTGTHIGLLEA 233
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDA-IQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-237 8.03e-47

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: 161.61  E-value: 8.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDlPRYKELLGDGTDLGVEFSYRVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   81 DEPRGLADAFIVGEDFIgEESVALVLGDNIFHghrfSEILKRAASLDkGAVIFGYYVKNPRPFGVVEFDEeGNVLSVEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLD----SDLLERLIRAE-APAIAVVEVDDPSDYGVVETDG-GRVTGIVEK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503409858  161 PENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYLKRKELKVELLGRGmaWLDTGTHIGLLEASNYV 237
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-239 2.66e-41

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


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 142.60  E-value: 2.66e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREIlIISTptdlpRYK-----ELLGDGTDLGVEFS 76
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINV-----GYLaeqieEYFGDGSRFGVRIT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  77 YRVQDEPRGLADAFIVGEDFIGEESVALVLGDNIFhGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLS 156
Cdd:COG1208   75 YVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 157 VEEKPENPKSNYVVPGLYFYDNSVIDIAKniapsDRGEIEITSVNDEYLKRKELKVELLgRGmAWLDTGTHIGLLEASNY 236
Cdd:COG1208  154 FVEKPEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVYGYVH-DG-YWLDIGTPEDLLEANAL 226

                 ...
gi 503409858 237 VEA 239
Cdd:COG1208  227 LLS 229
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-234 3.04e-31

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: 117.25  E-value: 3.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTP------------------------T 56
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdrsyeleetlekkgkT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  57 DLPRYKELLGDgtdlGVEFSYRVQDEPRGLADAFIVGEDFIGEESVALVLGDNIFHGhrFSEILKRAASL--DKGAVIFG 134
Cdd:cd02541   81 DLLEEVRIISD----LANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDS--KEPCLKQLIEAyeKTGASVIA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 135 Y---YVKNPRPFGVVEFDE-EGNVLSVE---EKP--ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEYL 205
Cdd:cd02541  155 VeevPPEDVSKYGIVKGEKiDGDVFKVKglvEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLL 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 503409858 206 KRKE-LKVELLGRgmaWLDTGTHIGLLEAS 234
Cdd:cd02541  235 EEEPvYAYVFEGK---RYDCGNKLGYLKAT 261
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 1.51e-25

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 102.42  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTptdlpRYK---------------ELLG 66
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTG-----RGKraiedhfdrsyeleaTLEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  67 DG-TDL---------GVEFSYRVQDEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHRfsEILKR---AASLDKGAVI- 132
Cdd:COG1210   80 KGkEELleevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEK--PCLKQmieVYEETGGSVIa 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 133 --------FGYYvknprpfGVVEFDE-EGNVLSVE---EKP--ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEIT 198
Cdd:COG1210  158 vqevppeeVSKY-------GIVDGEEiEGGVYRVTglvEKPapEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLT 230
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 503409858 199 SVNDEYLKRKE-LKVELLGRgmaWLDTGTHIGLLEA 233
Cdd:COG1210  231 DAIAALAKEEPvYAYEFEGK---RYDCGDKLGYLKA 263
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-182 2.02e-23

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 95.74  E-value: 2.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIRE-ILIIS-TPTDLPRYKELLGDgtDLGVEFSYR 78
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  79 VQDEPRGLADAFIVGEDFIGEESVA-LVLGDNIFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEE-GNVLS 156
Cdd:cd06425   79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIER 158
                        170       180
                 ....*....|....*....|....*.
gi 503409858 157 VEEKPENPKSNYVVPGLYFYDNSVID 182
Cdd:cd06425  159 FVEKPKVFVGNKINAGIYILNPSVLD 184
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-191 2.52e-22

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: 92.23  E-value: 2.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREIlIISTPtdlprYK-----ELLGDGTDLGVEFSYR 78
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVG-----YLaeqieEYFGDGYRGGIRIYYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  79 VQDEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHrFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLSVE 158
Cdd:cd06915   76 IEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFV 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 503409858 159 EKPENPKSNYVVPGLYFYDNSVIDIAKNIAPSD 191
Cdd:cd06915  155 EKGPGAAPGLINGGVYLLRKEILAEIPADAFSL 187
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-233 5.75e-19

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: 83.33  E-value: 5.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREIlIISTptdlpRY-----KELLGDGTDLGVEFSYR 78
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISV-----NYlaemiEDYFGDGSKFGVNISYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  79 VQDEPRGLADAFIVGEDFIgEESVALVLGDnIFHGHRFSEIL----KRAASLDKGAVIFGYYVknprPFGVVEFDeEGNV 154
Cdd:cd06426   76 REDKPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLdfhkENNADATVCVREYEVQV----PYGVVETE-GGRI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 155 LSVEEKPENpkSNYVVPGLYFYDNSVID-IAKNIapsdrgEIEITSVNDEYLKRKElKV---ELLGRgmaWLDTGTHIGL 230
Cdd:cd06426  149 TSIEEKPTH--SFLVNAGIYVLEPEVLDlIPKNE------FFDMPDLIEKLIKEGK-KVgvfPIHEY---WLDIGRPEDY 216

                 ...
gi 503409858 231 LEA 233
Cdd:cd06426  217 EKA 219
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-57 1.35e-15

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 73.85  E-value: 1.35e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTD 57
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-242 6.94e-14

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 70.30  E-value: 6.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIS------------TPTDLP-----RYK- 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELEslleqRVKr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  63 ELLGDGTDL---GVEFSYRVQDEPRGLADAFIVGEDFIGEESVALVLGDNIFHG-------HRFSEILKRAASLDKGAVI 132
Cdd:PRK10122  84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplrYNLAAMIARFNETGRSQVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 133 FGYYVKNPRPFGVVE----FDEEGNVLSVE---EKPENPK---SNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVND 202
Cdd:PRK10122 164 AKRMPGDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 503409858 203 EYLKRKELKVELL-------GRGMAWLDTGTHIGL---LEASNYVEAIQK 242
Cdd:PRK10122 244 ELAKKQSVDAMLMtgdsydcGKKMGYMQAFVKYGLrnlKEGAKFRKGIEK 293
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-52 3.52e-13

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: 67.28  E-value: 3.52e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILII 52
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-233 1.30e-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: 65.67  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREIlIISTpTDLP-RYKELLGD-GTDLGVEFSyrv 79
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNT-HHLAdQIEAHLGDsRFGLRITIS--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  80 qDEPR-------GLADAfivgEDFIGEESVALVLGDNIFHGHRFSEILKRAASLDkGAVIFGYYVKNPR--PFGVVEFDE 150
Cdd:cd06422   76 -DEPDelletggGIKKA----LPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMD-ALLLLLPLVRNPGhnGVGDFSLDA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 151 EGNVLSveeKPENPKSNYVVPGLYFYDNSVIDiakNIAPsdrGEIEITSVNDEYLKRKELKVELL-GRgmaWLDTGTHIG 229
Cdd:cd06422  150 DGRLRR---GGGGAVAPFTFTGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAGRLFGLVYdGL---WFDVGTPER 217

                 ....
gi 503409858 230 LLEA 233
Cdd:cd06422  218 LLAA 221
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-238 2.96e-12

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 65.70  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIS------------TPTDL-----PRYK-E 63
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELeamleKRVKrQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  64 LLGDGTDL---GVEFSYRVQDEPRGLADAFIVGEDFIGEESVALVLGDNIFHGHR-------FSEILKRAASLDKGAVIF 133
Cdd:PRK13389  90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYEsdlsqdnLAEMIRRFDETGHSQIMV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 134 gYYVKNPRPFGVVEFD-------EEGNVLSVEEKP--ENPKSNYVVPGLYFYDNSVIDIAKNIAPSDRGEIEITSVNDEY 204
Cdd:PRK13389 170 -EPVADVTAYGVVDCKgvelapgESVPMVGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDML 248
                        250       260       270
                 ....*....|....*....|....*....|....
gi 503409858 205 LKRKELKVELLgRGMAWlDTGTHIGLLEAsnYVE 238
Cdd:PRK13389 249 IEKETVEAYHM-KGKSH-DCGNKLGYMQA--FVE 278
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-177 5.27e-12

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 65.48  E-value: 5.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGGSGTRLYPITKAVSKqllpiydkPMIYY---------PLSVLMLAGIREILIistptdLPRYK--EL---LGDG 68
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKshSLndhIGSG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  69 T--DL-----GVE-FSYRVQDEP----RGLADAFIVGEDFIGEESVALVL---GDNIFhghR--FSEILKRAasLDKGA- 130
Cdd:COG0448   70 KpwDLdrkrgGVFiLPPYQQREGedwyQGTADAVYQNLDFIERSDPDYVLilsGDHIY---KmdYRQMLDFH--IESGAd 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503409858 131 --VIfgyYVKNPRP----FGVVEFDEEGNVLSVEEKPENPKSNYVVPGLYFYD 177
Cdd:COG0448  145 itVA---CIEVPREeasrFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-52 4.91e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 55.63  E-value: 4.91e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503409858   2 KGIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILII 52
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-112 9.46e-09

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 54.09  E-value: 9.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGGSGTRLYPITKAVSKQLLPI---YDkpMIYYPLSVLMLAGIREILII------STPTDLPRYKELLGDGTDLGV 73
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLtqyksrSLNDHLGSGKEWDLDRKNGGL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503409858  74 EFSYRVQDEP----RGLADAFIVGEDFIGEESVALVL---GDNIFH 112
Cdd:cd02508   79 FILPPQQRKGgdwyRGTADAIYQNLDYIERSDPEYVLilsGDHIYN 124
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-67 1.12e-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: 54.37  E-value: 1.12e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503409858   4 IILAGGSGTRLypiTKAVSKQLLPIYDKPMIYYPLSVLMLAG-IREILIISTPTDLPRYKELLGD 67
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-52 1.35e-08

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: 54.16  E-value: 1.35e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 503409858   4 IILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILII 52
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIV 50
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-187 1.44e-08

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 54.57  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGG--SGTRLYPITKAVSKQLLPIYDKPMIYYPLSVL-MLAGIREILIISTPTDLPRYKELLGDGTDLGVEFSYRV 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  80 QDEPRGLADAFIVGEDFIGEE--SVALVLGDNIFHGHRFSEILKRAASLDKGAVIFGyyVKNPRP----FG-VVEFDEEG 152
Cdd:cd06428   81 EYKPLGTAGGLYHFRDQILAGnpSAFFVLNADVCCDFPLQELLEFHKKHGASGTILG--TEASREqasnYGcIVEDPSTG 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 503409858 153 NVLSVEEKPENPKSNYVVPGLYFYDNSVIDIAKNI 187
Cdd:cd06428  159 EVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKA 193
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 3.46e-08

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 52.83  E-value: 3.46e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503409858   4 IILAGGSGTRLypitKA-VSKQLLPIYDKPMIYYPLSVLMLAG-IREILIISTPTDLPRYKELL 65
Cdd:PRK00155   7 IIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
4-190 5.45e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 53.31  E-value: 5.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLYPITKAVSKQLLPIYDK-PMIYYPLSVLMLAGIREILIIStptdlpRYKEL-----LGDG-----TDLG 72
Cdd:PRK00725  19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLT------QYKAHslirhIQRGwsffrEELG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  73 vEF------SYRVQDEP--RGLADAFIVGEDFIGEESVALVL---GDNIFHGHrFSEILkrAASLDKGAVIFGYYVKNPR 141
Cdd:PRK00725  93 -EFvdllpaQQRVDEENwyRGTADAVYQNLDIIRRYDPKYVVilaGDHIYKMD-YSRML--ADHVESGADCTVACLEVPR 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503409858 142 P----FGVVEFDEEGNVLSVEEKPENPKS-------------NYVVPGLYFYD---------NSVIDIAKNIAPS 190
Cdd:PRK00725 169 EeasaFGVMAVDENDRITAFVEKPANPPAmpgdpdkslasmgIYVFNADYLYElleedaedpNSSHDFGKDIIPK 243
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-161 9.16e-08

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: 52.19  E-value: 9.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPI-TKAVSKQLLPIY-DKPMIYYPLS-VLMLAGIREILIISTPTDLPRYKELLGDGTDlgvefSY 77
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVTNEEYRFLVREQLPEGLP-----EE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  78 RVQDEPRG--------LADAFIVGEDfigEESVALVL-------GDNIFHghrfsEILKRAASL-DKGA-VIFGyyVKNP 140
Cdd:cd02509   76 NIILEPEGrntapaiaLAALYLAKRD---PDAVLLVLpsdhlieDVEAFL-----KAVKKAVEAaEEGYlVTFG--IKPT 145
                        170       180
                 ....*....|....*....|....*....
gi 503409858 141 RP---FGVVEFDE--EGNVLSVE---EKP 161
Cdd:cd02509  146 RPetgYGYIEAGEklGGGVYRVKrfvEKP 174
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-75 2.62e-07

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 50.21  E-value: 2.62e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503409858   4 IILAGGSGTRLypiTKAVSKQLLPIYDKPMIYYPLSVLM-LAGIREILIISTPTDLPRYKELLGDGTDLGVEF 75
Cdd:cd02516    4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-164 1.62e-06

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: 47.90  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLYpitKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIsTPTDLPRYKELLGdgtDLGVEFSYrvQDEP 83
Cdd:cd02540    2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALA---NPNVEFVL--QEEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  84 RGLADAFIVGEDFIGE-ESVALVL-GDNIF-HGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLS-VEE 159
Cdd:cd02540   73 LGTGHAVKQALPALKDfEGDVLVLyGDVPLiTPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRiVEE 152

                 ....*
gi 503409858 160 KPENP 164
Cdd:cd02540  153 KDATE 157
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-178 6.77e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.13  E-value: 6.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRlypITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREI-LIISTPTDLprYKELLGDGTdlgvefSYRVQDE 82
Cdd:PRK14354   6 IILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIvTVVGHGAEE--VKEVLGDRS------EFALQEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  83 PRGLADAFIVGEDFIGEES--VALVLGDN-IFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLS-VE 158
Cdd:PRK14354  75 QLGTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEKiVE 154
                        170       180
                 ....*....|....*....|...
gi 503409858 159 EK---PENPKSNYVVPGLYFYDN 178
Cdd:PRK14354 155 QKdatEEEKQIKEINTGTYCFDN 177
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-207 1.94e-05

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 44.94  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYplSVLMLAGIRE---ILIIS----TPTDLPRYKELLGDGTDLgvefs 76
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFICRdehnTKFHLDESLKLLAPNATV----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  77 YRVQDEPRGLADAFIVGEDFI-GEESVALVLGDNIFHGhRFSEILKRAASLDKGAVIFGYYVKNPRpFGVVEFDEEGNVL 155
Cdd:cd04183   75 VELDGETLGAACTVLLAADLIdNDDPLLIFNCDQIVES-DLLAFLAAFRERDLDGGVLTFFSSHPR-WSYVKLDENGRVI 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503409858 156 SVEEKpeNPKSNYVVPGLYFYDNS--VIDIAKN-IAPSDR--GEIEITSVNDEYLKR 207
Cdd:cd04183  153 ETAEK--EPISDLATAGLYYFKSGslFVEAAKKmIRKDDSvnGEFYISPLYNELILD 207
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-160 2.34e-05

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: 45.40  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLYpitKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIstptdlprY-------KELLGdgtDLGVEFS 76
Cdd:COG1207    6 VILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV--------VghgaeqvRAALA---DLDVEFV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  77 yrVQDEPRGLADAFIVGEDFI-GEESVALVL-GDN-IFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGN 153
Cdd:COG1207   72 --LQEEQLGTGHAVQQALPALpGDDGTVLVLyGDVpLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGR 149

                 ....*...
gi 503409858 154 VLS-VEEK 160
Cdd:COG1207  150 VLRiVEEK 157
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
4-204 2.44e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 45.36  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLypiTKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDgtdlGVEFSYrvQDEP 83
Cdd:PRK14358  11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGS----GVAFAR--QEQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  84 RGLADAFIVGEDFIGEESV-ALVL-GDN-IFHGHRFSEILKRAASLDKGAVIFGYYVKNPRPFGVVEFDEEGNVLS-VEE 159
Cdd:PRK14358  82 LGTGDAFLSGASALTEGDAdILVLyGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERiVEQ 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503409858 160 KPENPKSNYV---VPGLYFYDNSVIDIAKNIAPSDR-GEIEITSVNDEY 204
Cdd:PRK14358 162 KDATDAEKAIgefNSGVYVFDARAPELARRIGNDNKaGEYYLTDLLGLY 210
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-190 3.43e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 44.86  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPITKAVSKQLLPIYDK-PMIYYPLSVLMLAGIREILI--------------ISTPTDLprykell 65
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVltqyqplelnnhigIGSPWDL------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  66 gDGTDLGVEF--SYRVQDEPR---GLADAFIVGEDFIGEESVALVL---GDNIFHgHRFSEILKraASLDKGA-----VI 132
Cdd:PRK05293  77 -DRINGGVTIlpPYSESEGGKwykGTAHAIYQNIDYIDQYDPEYVLilsGDHIYK-MDYDKMLD--YHKEKEAdvtiaVI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503409858 133 FGYYVKNPRpFGVVEFDEEGNVLSVEEKPENPKSNYVVPGLYFY---------------DNSVIDIAKNIAPS 190
Cdd:PRK05293 153 EVPWEEASR-FGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL 224
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
3-52 3.50e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 44.88  E-value: 3.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503409858   3 GIILAGGSGTRLYPITKAVSKQLLPIYDK-PMIYYPLSVLMLAGIREILII 52
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-108 4.21e-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: 42.95  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    3 GIILAGGSGTRLypitkAVSKQLLPIYDKPMIYYPLSVLMLAGiREILIIStptdlpRYKELLGDGTDLGVEFsyrVQDE 82
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVA------NDEEVLAALAGLGVPV---VPDP 65
                          90       100
                  ....*....|....*....|....*....
gi 503409858   83 P--RGLADAFIVGEDFIGE-ESVALVLGD 108
Cdd:pfam12804  66 DpgQGPLAGLLAALRAAPGaDAVLVLACD 94
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-161 6.77e-05

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 43.90  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLYPI-TKAVSKQLLPIY-DKPMIYypLSVLMLAGI---REILIIStptdlprykellgdgtdlGVEF 75
Cdd:COG0836    3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLLQ--QTVERLAGLvppENILVVT------------------NEEH 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  76 SYRVQDEPRGLADAFIVGEDF-----------------IGEESVALVL------GDNifhgHRFSEILKRAASL-DKGA- 130
Cdd:COG0836   63 RFLVAEQLPELGPANILLEPVgrntapaialaalliakRDPDAVLLVLpadhliEDE----EAFREAVRAAVEAaEAGKl 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 503409858 131 VIFGyyVKnP-RP---FGVVEFDEE---GNVLSVE---EKP 161
Cdd:COG0836  139 VTFG--IK-PtRPetgYGYIEAGEAlggAGAYKVKrfvEKP 176
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-166 1.33e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 42.89  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGGSGTRLYPITKAVSKQLLP---IYDkpMIYYPLSVLMLAGIREILIistptdLPRYKE---------------L 64
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYV------LTQYKShsldrhisqtwrlsgL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  65 LGdgtdlgvEFSYRVQDEPR-------GLADAFIVGEDFIGEES---VALVLGDNIFhghR--FSEILkrAASLDKGAVI 132
Cdd:PRK00844  80 LG-------NYITPVPAQQRlgkrwylGSADAIYQSLNLIEDEDpdyVVVFGADHVY---RmdPRQMV--DFHIESGAGV 147
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 503409858 133 FGYYVKNPR----PFGVVEFDEEGNVLSVEEKPENPKS 166
Cdd:PRK00844 148 TVAAIRVPReeasAFGVIEVDPDGRIRGFLEKPADPPG 185
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-183 1.72e-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: 41.82  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGGSGTRLYPITKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTptdlpRYKELL------GDGTDLGVE-F 75
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCC-----SHSDQIkeyiekSKWSKPKSSlM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  76 SYRVQ---------DEPRGLADAFIVGEDFIgeesvaLVLGD---NIfhghRFSEIL---KRAASLDKGA----VIF--- 133
Cdd:cd04197   78 IVIIImsedcrslgDALRDLDAKGLIRGDFI------LVSGDvvsNI----DLKEILeehKERRKKDKNAimtmVLKeas 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503409858 134 -GYYVKNPRPFGVVEFDEE-GNVLSVEEKP-ENPKSNYVVPGLYFYDNSVIDI 183
Cdd:cd04197  148 pPHRTRRTGEEFVIAVDPKtSRLLHYEELPgSKYRSITDLPSELLGSNSEVEI 200
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
3-52 1.90e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 42.53  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503409858   3 GIILAGGSGTRLYPITKAVSKQLLPI---YDkpMIYYPLSVLMLAGIREILII 52
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-85 3.65e-04

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 40.56  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRLypitkAVSKQLLPIYDKPMIYYPLSVLMLAGIReiLIISTPTDlPRYKellgdgtDLGVEFsyrVQ 80
Cdd:COG0746    5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQVDE--VVIVANRP-ERYA-------ALGVPV---VP 66

                 ....*
gi 503409858  81 DEPRG 85
Cdd:COG0746   67 DDPPG 71
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-55 4.32e-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: 40.26  E-value: 4.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 503409858   6 LAGGSGTRLypitKAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTP 55
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
3-170 5.32e-04

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: 40.40  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858    3 GIILAGGSGTRLypitkaVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIStpTDLPRYKELLgdgTDLGVEFSYRVQDE 82
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVA--TDSEEIADVA---KEFGAGVVMTSGSL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   83 PRGLADAFIVGEDFIGEES--VALVLGDNIFhghRFSEILKRAASldkgavifgYYVKNPRPFgvveFDEEGNVLSVEEK 160
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNDHDdiIVNIQGDNPL---LQPEVILKAIE---------TLLNNGEPY----MSTLVVPVGSAEE 134
                         170
                  ....*....|
gi 503409858  161 PENPKSNYVV 170
Cdd:pfam02348 135 VLNANALKVV 144
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-108 1.05e-03

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 39.37  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGGSGTRLypitkAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIsTPtdlPRYKELLGDGTDLGVEFSYrVQDE 82
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LG---ADAEEVAAALAGLGVRVVV-NPDW 75
                         90       100
                 ....*....|....*....|....*...
gi 503409858  83 PRGLADAFIVGEDFIGEES--VALVLGD 108
Cdd:COG2068   76 EEGMSSSLRAGLAALPADAdaVLVLLGD 103
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-226 1.09e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.13  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRL---YPitkavsKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLprYKELLGDGTDLgvefsy 77
Cdd:PRK14357   1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPEWVKI------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  78 RVQDEPRGLADAFIVGEDFIGEESVALVL-GDNIFHGHRFSEILKRAASLDKGAV-IFGYYVKNPRPFGVVeFDEEGNVL 155
Cdd:PRK14357  67 FLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEHNRKGADVtILVADLEDPTGYGRI-IRDGGKYR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858 156 SVEEK--PENPKS-NYVVPGLYFYD-NSVIDIAKNIAPSD-RGE---------------------IEITSVND------- 202
Cdd:PRK14357 146 IVEDKdaPEEEKKiKEINTGIYVFSgDFLLEVLPKIKNENaKGEyyltdavnfaekvrvvktedlLEITGVNTriqlawl 225
                        250       260
                 ....*....|....*....|....
gi 503409858 203 EYLKRKELKVELLGRGMAWLDTGT 226
Cdd:PRK14357 226 EKQLRMRILEELMENGVTILDPNT 249
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-108 1.32e-03

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: 39.08  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   3 GIILAGGSGTRLypitkAVSKQLLPIYDKPMIYYPLSVLMLAGIREILIISTPTDLPRYKELLGDGTDLgvefsYRVQDE 82
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVV-----VINPDW 72
                         90       100
                 ....*....|....*....|....*...
gi 503409858  83 PRGLADAFIVGEDFIGEESVALV--LGD 108
Cdd:cd04182   73 EEGMSSSLAAGLEALPADADAVLilLAD 100
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-86 5.45e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 37.17  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   1 MKGIILAGGSGTRL-YPitkavsKQLLPIYDKPMIYYPLSvlMLAGIREILIISTPTDLPRYKellgdgtDLGVEFsyrV 79
Cdd:cd02503    1 ITGVILAGGKSRRMgGD------KALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYA-------LLGVPV---I 62

                 ....*..
gi 503409858  80 QDEPRGL 86
Cdd:cd02503   63 PDEPPGK 69
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-165 5.68e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.19  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858   4 IILAGGSGTRLypiTKAVSKQLLPIYDKPMIYYPLSVLMLAGI-REILIISTPTDLPRyKELLGDGtdlgvEFSYRVQDE 82
Cdd:PRK14355   7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAgRIVLVVGHQAEKVR-EHFAGDG-----DVSFALQEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503409858  83 PRGLADAFIVGEDFIGEES--VALVLGDNIFHGhrfSEILKR--AASLDKGAVIFGYYVKNPRPFG---VVEfDEEGNVL 155
Cdd:PRK14355  78 QLGTGHAVACAAPALDGFSgtVLILCGDVPLLR---AETLQGmlAAHRATGAAVTVLTARLENPFGygrIVR-DADGRVL 153
                        170
                 ....*....|.
gi 503409858 156 S-VEEKPENPK 165
Cdd:PRK14355 154 RiVEEKDATPE 164
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
4-67 5.72e-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: 37.90  E-value: 5.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503409858   4 IILAGGSGTRLypiTKAVSKQLLPIYDKPMIYYPLSVLMLAG-IREILIISTPTDLPRYKELLGD 67
Cdd:PRK09382   9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-64 6.83e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 36.70  E-value: 6.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503409858   1 MKGIILAGGSGTRLYPITKAvskqLLPIYDKPMIYYplsVLM-LAGIREILIISTPTDLPRYKEL 64
Cdd:PRK00317   4 ITGVILAGGRSRRMGGVDKG----LQELNGKPLIQH---VIErLAPQVDEIVINANRNLARYAAF 61
 
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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