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Conserved domains on  [gi|1210348224|gb|ASD68130|]
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glucose-1-phosphate thymidylyltransferase [Pseudoalteromonas piscicida]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

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

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 161 PSQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1210348224 241 ERRQGLMVACLEEIAWNKGWLTLESLEKQSNLLAKTTYGDYLKALVtKEKRVR 293
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL-DSNRAR 292
 
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: 547.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 161 PSQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1210348224 241 ERRQGLMVACLEEIAWNKGWLTLESLEKQSNLLAKTTYGDYLKALVtKEKRVR 293
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL-DSNRAR 292
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: 525.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQE 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 KPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 162 SQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1210348224 242 RRQGLMVACLEEIAWNKGWLTLESLEKQSNLLAKTTYGDYLKALVT 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 4.46e-172

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: 475.53  E-value: 4.46e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 161 PSQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-286 6.58e-133

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 378.63  E-value: 6.58e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 KPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 162 SQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1210348224 242 RRQGLMVACLEEIAWNKGWLTLESLEKQSNLLAKTTYGDYLKALV 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 7.53e-100

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 292.62  E-value: 7.53e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNK-PMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESV-CLVLGDNIFYGQAFSPYLNNAAQLTHGAMV--FGYPVADPERFGVVEFNEAGKVTSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADATVtfGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 158 EEKPSQPK-SNFAVTGLYFYDNQVVD-IAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASH 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1210348224 236 FV 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 161 PSQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1210348224 241 ERRQGLMVACLEEIAWNKGWLTLESLEKQSNLLAKTTYGDYLKALVtKEKRVR 293
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL-DSNRAR 292
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: 525.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQE 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 KPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 162 SQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1210348224 242 RRQGLMVACLEEIAWNKGWLTLESLEKQSNLLAKTTYGDYLKALVT 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 4.46e-172

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: 475.53  E-value: 4.46e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 161 PSQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-286 6.58e-133

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 378.63  E-value: 6.58e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 KPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 162 SQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASHFVQTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1210348224 242 RRQGLMVACLEEIAWNKGWLTLESLEKQSNLLAKTTYGDYLKALV 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 7.53e-100

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 292.62  E-value: 7.53e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNK-PMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESV-CLVLGDNIFYGQAFSPYLNNAAQLTHGAMV--FGYPVADPERFGVVEFNEAGKVTSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADATVtfGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 158 EEKPSQPK-SNFAVTGLYFYDNQVVD-IAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFAWLDTGTHDSMLEASH 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1210348224 236 FV 237
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-237 9.92e-76

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: 230.92  E-value: 9.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQlFKNLLGDGTQFGVKLEYAVQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEE-IKEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGqAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFnEAGKVTSIEEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVV-DDGRIVRLVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210348224 161 PSQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEIT-CINRaYLERGQLQVSVLGRGFaWLDTGTHDSMLEASHFV 237
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITdAIQW-LIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-249 8.75e-66

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: 209.57  E-value: 8.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQE 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 KPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAfSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGI-SRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 162 SQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGFaWLDTGTHDSMLEASHFV--QT 239
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIldEV 238

                         250
                  ....*....|
gi 1210348224 240 IERRQGLMVA 249
Cdd:TIGR01208 239 EREVQGVDDE 248
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 4.65e-62

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 195.49  E-value: 4.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   3 GIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQlFKNLLGDGTQFGVKLEYAVQEK 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQ-IEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  83 PEGLAQAFVIAETFIGNESVCLVLGDNIFYGqAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEKPS 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1210348224 163 QPKSNFAVTGLYFYDNQVVDIAKTVKPssRGELEITCINRAYLERGQLQVsVLGRGFaWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-234 1.24e-48

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 166.23  E-value: 1.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLfKNLLGDGTQFGVKLEYAVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKV-REYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNEsvCLVL-GDNIFYgqafSPYLNNAAqLTHGAMVFGYPVADPERFGVVEFnEAGKVTSIEE 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDDE--FLVLnGDVLLD----SDLLERLI-RAEAPAIAVVEVDDPSDYGVVET-DGGRVTGIVE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1210348224 160 KPSQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGRGfaWLDTGTHDSMLEAS 234
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDAN 224
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 1.23e-47

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


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 159.16  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDIlVITTAQEQQLFKNLLGDGTQFGVKLEYAVQE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 KPEGLAQAFVIAETFIGNESVCLVLGDnIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAGKVTSIEEKP 161
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEKP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1210348224 162 SQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELeitcINRAyLERGQLQVSVLgRGFaWLDTGTHDSMLEA 233
Cdd:COG1208   159 EEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDL----LPRL-IAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-234 5.92e-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: 116.48  E-value: 5.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQ--------------EQQLF---KN 63
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfdrsyelEETLEkkgKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  64 LLGDGTQ---FGVKLEYAVQEKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAF-SPYLNNAAQLTHGAMVFGYPVAD 139
Cdd:cd02541    81 DLLEEVRiisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYEKTGASVIAVEEVPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 140 PE--RFGVVEFNEAG----KVTSIEEKPSQ--PKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYLERGQlq 211
Cdd:cd02541   161 EDvsKYGIVKGEKIDgdvfKVKGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP-- 238

                         250       260
                  ....*....|....*....|....*
gi 1210348224 212 vsVLGRGF--AWLDTGTHDSMLEAS 234
Cdd:cd02541   239 --VYAYVFegKRYDCGNKLGYLKAT 261
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-233 4.76e-26

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: 102.20  E-value: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLfKNLLGDGTQFGVKLEYAVQEKP 83
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMI-EDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  84 EGLAQAFVIAETFIgNESVCLVLGD---NIFYGQAFSPYLNNAAQLTHGAMVFGYPVAdperFGVVEFNEaGKVTSIEEK 160
Cdd:cd06426    81 LGTAGALSLLPEKP-TDPFLVMNGDiltNLNYEHLLDFHKENNADATVCVREYEVQVP----YGVVETEG-GRITSIEEK 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1210348224 161 PSQpkSNFAVTGLYFYDNQVVDIaktVKPSSRgeLEITCINRAYLERGQLQVSVLGRGFaWLDTGTHDSMLEA 233
Cdd:cd06426   155 PTH--SFLVNAGIYVLEPEVLDL---IPKNEF--FDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-226 3.91e-25

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: 100.36  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQ 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNESVC-LVLGDNIF----YGQAFSPYLNNAAQLThgamVFGYPVADPERFGVVEFNEA-GKV 154
Cdd:cd06425    81 TEPLGTAGPLALARDLLGDDDEPfFVLNSDVIcdfpLAELLDFHKKHGAEGT----ILVTKVEDPSKYGVVVHDENtGRI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210348224 155 TSIEEKPSQPKSNFAVTGLYFYDNQVVDiaktvkpssRGELEITCINR----AYLERGQLQVSVLgRGFaWLDTGT 226
Cdd:cd06425   157 ERFVEKPKVFVGNKINAGIYILNPSVLD---------RIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WMDIGQ 221
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 4.95e-24

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 98.57  E-value: 4.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYplSV--LMLAGIRDILVIT------------TAQ--EQQLFKN-- 63
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTgrgkraiedhfdRSYelEATLEAKgk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  64 --LLG--DGTQFGVKLEYAVQEKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAfspylNNAAQL------THGAMVF 133
Cdd:COG1210    83 eeLLEevRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEK-----PCLKQMievyeeTGGSVIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 134 GYPVADPE--RFGVVEFNEAG----KVTSIEEKPSQPK--SNFAVTGLYFYDNQVVDIAKTVKPSSRGELEITCINRAYL 205
Cdd:COG1210   158 VQEVPPEEvsKYGIVDGEEIEggvyRVTGLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALA 237

                         250       260       270
                  ....*....|....*....|....*....|
gi 1210348224 206 ERGQlqvsVLGRGFA--WLDTGTHDSMLEA 233
Cdd:COG1210   238 KEEP----VYAYEFEgkRYDCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-174 6.12e-23

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: 94.16  E-value: 6.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDIlVITTAQEQQLFKNLLGDGTQFGVKLEYAVQEKP 83
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  84 EGLAQAFVIAETFIGNESVcLVL-GDNIF---YGQAFSPYLNNAAQLThgaMVfGYPVADPERFGVVEFNEAGKVTSIEE 159
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQF-LVLnGDTYFdvdLLALLAALRASGADAT---MA-LRRVPDASRYGNVTVDGDGRVIAFVE 155

                         170
                  ....*....|....*
gi 1210348224 160 KPSQPKSNFAVTGLY 174
Cdd:cd06915   156 KGPGAAPGLINGGVY 170
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-60 6.27e-20

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: 85.79  E-value: 6.27e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQL 60
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAE 60
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-60 1.21e-16

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: 76.91  E-value: 1.21e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQL 60
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAI 60
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-177 8.71e-16

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 76.65  E-value: 8.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   3 GIILAGGSGTRLYPVTQGVSKqllpiynkPMIYY---------PLSVLMLAGIRDILVITtaqeQQLFKNL---LGDGT- 69
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT----QYKSHSLndhIGSGKp 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  70 -QFGVKLEY-----AVQEKP-----EGLAQAFVIAETFI--GNESVCLVL-GDNIF---YGQAFSPYLNNAAQLTHGAMV 132
Cdd:COG0448    72 wDLDRKRGGvfilpPYQQREgedwyQGTADAVYQNLDFIerSDPDYVLILsGDHIYkmdYRQMLDFHIESGADITVACIE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1210348224 133 fgYPVADPERFGVVEFNEAGKVTSIEEKPSQPKSNFAVTGLYFYD 177
Cdd:COG0448   152 --VPREEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-198 5.95e-15

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 73.40  E-value: 5.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLfKNLLGDGTQFGVKLEYAVQE 81
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSI-ENHFDTSFELEAMLEKRVKR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 K----------------------PEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQL------THGAMVF 133
Cdd:PRK13389   89 QlldevqsicpphvtimqvrqglAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMirrfdeTGHSQIM 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1210348224 134 GYPVADPERFGVVEFN-------EAGKVTSIEEKP--SQPKSNFAVTGLYFYDNQVVDIAKTVKPSSRGELEIT 198
Cdd:PRK13389  169 VEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 1.28e-14

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 72.61  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQ------------------EQQLFK 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASknavenhfdtsyelesllEQRVKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  63 NLLGDGTQF---GVKLEYAVQEKPEGLAQAFVIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQL------THGAMVF 133
Cdd:PRK10122   84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMiarfneTGRSQVL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210348224 134 GYPV-ADPERFGVVEFNEA----GKVTSIE---EKPSQPK---SNFAVTGLYFYDNQVVDIAKTVKPSSRGELEIT 198
Cdd:PRK10122  164 AKRMpGDLSEYSVIQTKEPldreGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-233 4.03e-13

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: 67.21  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLfKNLLGDgTQFGVKLEYaVQE 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQI-EAHLGD-SRFGLRITI-SDE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  82 KPE------GLAQafviAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVfgYPVAD-PERFGVVEF--NEAG 152
Cdd:cd06422    78 PDElletggGIKK----ALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLL--LPLVRnPGHNGVGDFslDADG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 153 KVTSIEEKPSQPksnFAVTGLYFYDNQVVDIAKtvkpssRGELEITCINRAYLERGQLQVSVLgRGFaWLDTGTHDSMLE 232
Cdd:cd06422   152 RLRRGGGGAVAP---FTFTGIQILSPELFAGIP------PGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLA 220


                  .
gi 1210348224 233 A 233
Cdd:cd06422   221 A 221
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-223 3.06e-12

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 64.95  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQlFKNLLGDgtqfGVKLEYAVQEKP 83
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQ-IEELLKK----YPNIKFVYNPDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  84 E--GLAQAFVIAETFIgNESVCLVLGDNIFYGQAFSPYLNNAAqlthGAMVFGYPVADPERFGVVE-FNEAGKVTSIEEK 160
Cdd:cd02523    77 AetNNIYSLYLARDFL-DEDFLLLEGDVVFDPSILERLLSSPA----DNAILVDKKTKEWEDEYVKdLDDAGVLLGIISK 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210348224 161 PSQPKSNFAVT-GLYFYDNQ----VVDIAKTVKPSSRGELEITCINRAYLERGQLQVSVLGrGFAWLD 223
Cdd:cd02523   152 AKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 1.85e-11

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 62.57  E-value: 1.85e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1210348224   2 KGIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVIT 53
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-234 3.37e-10

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 60.27  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPVTQGVSKQLLPIYNK-PMIYYPLSVLMLAGIRDILVITtaQEQQLFKNL-LGDGTQF------- 71
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT--QYQPLELNNhIGIGSPWdldring 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  72 GVKL--EYAVQEKP---EGLAQAFVIAETFIGN---ESVcLVL-GDNIF---YGQAFSPYLNNAAQLTHGamVFGYPVAD 139
Cdd:PRK05293   82 GVTIlpPYSESEGGkwyKGTAHAIYQNIDYIDQydpEYV-LILsGDHIYkmdYDKMLDYHKEKEADVTIA--VIEVPWEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224 140 PERFGVVEFNEAGKVTSIEEKPSQPKSNFAVTGLYFY---------------DNQVVDIAKTVKPSsrgeleitcinraY 204
Cdd:PRK05293  159 ASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL-------------Y 225

                         250       260       270
                  ....*....|....*....|....*....|
gi 1210348224 205 LERGQLQVSVLGRGFaWLDTGTHDSMLEAS 234
Cdd:PRK05293  226 LEEGEKLYAYPFKGY-WKDVGTIESLWEAN 254
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-166 1.37e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 58.31  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLYPVTQGVSKQLLPIYNK-PMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLgDG-----TQFGvklEY 77
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQ-RGwsffrEELG---EF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  78 -----AVQEKPE-----GLA----QAFVIAETFigNESVCLVL-GDNIF---YGQAFSPYLNNAAQLTHGAM-VfgyPVA 138
Cdd:PRK00725   95 vdllpAQQRVDEenwyrGTAdavyQNLDIIRRY--DPKYVVILaGDHIYkmdYSRMLADHVESGADCTVACLeV---PRE 169

                         170       180
                  ....*....|....*....|....*...
gi 1210348224 139 DPERFGVVEFNEAGKVTSIEEKPSQPKS 166
Cdd:PRK00725  170 EASAFGVMAVDENDRITAFVEKPANPPA 197
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-90 2.05e-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: 56.01  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   3 GIILAGGSGTRLYPVTQGVSKQLLPI---YNkpMIYYPLSVLMLAGIRDILVITTAQEQQLF------KNLLGDGTQFGV 73
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLTQYKSRSLNdhlgsgKEWDLDRKNGGL 78

                          90       100
                  ....*....|....*....|.
gi 1210348224  74 KLEYAVQEKP----EGLAQAF 90
Cdd:cd02508    79 FILPPQQRKGgdwyRGTADAI 99
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-181 2.59e-09

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: 56.37  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRL---YPvtqgvsKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFgvkleyAVQ 80
Cdd:cd02540     2 VILAAGKGTRMksdLP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEF------VLQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGN-ESVCLVLgdnifYG-------QAFSPYLNNAAQLTHGAMVFGYPVADPERFGVVEFNEAG 152
Cdd:cd02540    70 EEQLGTGHAVKQALPALKDfEGDVLVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNG 144

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1210348224 153 KVTSI-EEK---PSQPKSNFAVTGLYFYDNQVV 181
Cdd:cd02540   145 KVLRIvEEKdatEEEKAIREVNAGIYAFDAEFL 177
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 1.43e-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: 53.98  E-value: 1.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1210348224   4 IILAGGSGTRLypvTQGVSKQLLPIYNKPMIYYPLSVLMLAG-IRDILVITTAQEQQLFKNLLGD 67
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-188 2.54e-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: 53.80  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   3 GIILAGG--SGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVL-MLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAV 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  80 QEKPEGLA---------------QAFviaetFIGNESVC--LVLGDNI-FYGQAFSPYL---NNAAQLThgAMVFGYPVA 138
Cdd:cd06428    81 EYKPLGTAgglyhfrdqilagnpSAF-----FVLNADVCcdFPLQELLeFHKKHGASGTilgTEASREQ--ASNYGCIVE 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1210348224 139 DPerfgvvefnEAGKVTSIEEKPSQPKSNFAVTGLYFYDNQVVD-IAKTVK 188
Cdd:cd06428   154 DP---------STGEVLHYVEKPETFVSDLINCGVYLFSPEIFDtIKKAFQ 195
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-165 7.25e-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: 52.58  E-value: 7.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLYPV-TQGVSKQLLPIY-NKPMIYYPLS-VLMLAGIRDILVITTAQEQQLFKNLLGDGtqfgvKLEY 77
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVTNEEYRFLVREQLPEG-----LPEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  78 AVQEKPEG--------LAQAFVIAEtfiGNESVCLVL------GDNifygQAFSPYLNNAAQLT-HGAMV-FGYPVADPE 141
Cdd:cd02509    76 NIILEPEGrntapaiaLAALYLAKR---DPDAVLLVLpsdhliEDV----EAFLKAVKKAVEAAeEGYLVtFGIKPTRPE 148

                         170       180       190
                  ....*....|....*....|....*....|
gi 1210348224 142 -RFGVVEFNE-----AGKVTSIEEKPSQPK 165
Cdd:cd02509   149 tGYGYIEAGEklgggVYRVKRFVEKPDLET 178
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-166 9.39e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 52.91  E-value: 9.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   3 GIILAGGSGTRLYPVTQGVSKQLLP---IYNkpMIYYPLSVLMLAGIRDILVITTAQEQQLFK---------NLLGdgtQ 70
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLTQYKSHSLDRhisqtwrlsGLLG---N 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  71 FgvkleyaVQEKP----------EGLAQAFVIAETFIGNES---VCLVLGDNIF---YGQAFSPYLNNAAQLTHGAMVFg 134
Cdd:PRK00844   83 Y-------ITPVPaqqrlgkrwyLGSADAIYQSLNLIEDEDpdyVVVFGADHVYrmdPRQMVDFHIESGAGVTVAAIRV- 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1210348224 135 yPVADPERFGVVEFNEAGKVTSIEEKPSQPKS 166
Cdd:PRK00844  155 -PREEASAFGVIEVDPDGRIRGFLEKPADPPG 185
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-108 1.80e-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: 50.25  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   3 GIILAGGSGTRLypvtqGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAvqek 82
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWE---- 73

                          90       100
                  ....*....|....*....|....*...
gi 1210348224  83 pEGLAQAFVIA-ETFIGNESVCLV-LGD 108
Cdd:cd04182    74 -EGMSSSLAAGlEALPADADAVLIlLAD 100
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-198 2.17e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 51.90  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLypvTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFgvkleyAVQEKP 83
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAF------ARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  84 EGLAQAFVIAETFI--GNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAM-VFGYPVADPERFGVVEFNEAGKVTSIEEK 160
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTPLLRPDTLRALVADHRAQGSAMtILTGELPDATGYGRIVRGADGAVERIVEQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1210348224 161 PSQPKSNFAV----TGLYFYDNQVVDIAKTVKPSSR-GELEIT 198
Cdd:PRK14358  162 KDATDAEKAIgefnSGVYVFDARAPELARRIGNDNKaGEYYLT 204
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-68 2.41e-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: 2.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210348224   4 IILAGGSGTRLypvTQGVSKQLLPIYNKPMIYYPLSVLM-LAGIRDILVITTAQEQQLFKNLLGDG 68
Cdd:cd02516     4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-71 5.14e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.00  E-value: 5.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1210348224   3 GIILAGGSGTRLypvtqGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQF 71
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRV 69
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 6.95e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 48.98  E-value: 6.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1210348224   4 IILAGGSGTRLYPvtqGVSKQLLPIYNKPMIYYPLSVLMLAG-IRDILVITTAQEQQLFKNLL 65
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-180 5.73e-06

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: 47.33  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLY---PvtqgvsKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLfKNLLGDgtqfgVKLEYAVQ 80
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQV-RAALAD-----LDVEFVLQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  81 EKPEGLAQAFVIAETFIGNES-VCLVLgdnifYG-----------QAFSPYLNNAAQLTHGAMVfgypVADPERFGVVEF 148
Cdd:COG1207    74 EEQLGTGHAVQQALPALPGDDgTVLVL-----YGdvpliraetlkALLAAHRAAGAAATVLTAE----LDDPTGYGRIVR 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1210348224 149 NEAGKVTSI-EEK---PSQPKSNFAVTGLYFYDNQV 180
Cdd:COG1207   145 DEDGRVLRIvEEKdatEEQRAIREINTGIYAFDAAA 180
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 9.04e-06

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 46.60  E-value: 9.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1210348224   1 MKGIILAGGSGTRLYPV-TQGVSKQLLPIY-NKPMIYypLSVLMLAGI---RDILVIT 53
Cdd:COG0836     3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLLQ--QTVERLAGLvppENILVVT 58
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-53 9.59e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 46.42  E-value: 9.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1210348224   1 MK---GIILAGGSGTRLYPVTQGVSKQLLPIYNK-PMIYYPLSVLMLAGIRDILVIT 53
Cdd:PRK02862    1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-165 1.27e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 46.28  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLypvTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLLGDGtqfgvKLEYAVQEKP 83
Cdd:PRK14355    7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG-----DVSFALQEEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  84 EGLAQAFVIAET----FIGneSVCLVLGDNIFYGQAFSPYLNNAAQLTHGAM-VFGYPVADPERFGVVEFNEAGKVTSI- 157
Cdd:PRK14355   79 LGTGHAVACAAPaldgFSG--TVLILCGDVPLLRAETLQGMLAAHRATGAAVtVLTARLENPFGYGRIVRDADGRVLRIv 156


                  ....*...
gi 1210348224 158 EEKPSQPK 165
Cdd:PRK14355  157 EEKDATPE 164
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-53 1.71e-05

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 46.00  E-value: 1.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1210348224   3 GIILAGGSGTRLYPVTQGVSKQLLPI---YNkpMIYYPLSVLMLAGIRDILVIT 53
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLT 57
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-180 2.81e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.21  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTR----LYPVtqgvskqLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLfKNLLGDGTqfgvklEYAV 79
Cdd:PRK14354    6 IILAAGKGTRmkskLPKV-------LHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEV-KEVLGDRS------EFAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  80 QEKPEGLAQAFVIAETFIGNES-VCLVL-GDN-IFYGQAFSPYL----NNAAQLThgamVFGYPVADPERFGVVEFNEAG 152
Cdd:PRK14354   72 QEEQLGTGHAVMQAEEFLADKEgTTLVIcGDTpLITAETLKNLIdfheEHKAAAT----ILTAIAENPTGYGRIIRNENG 147

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1210348224 153 KVTSI-EEK---PSQPKSNFAVTGLYFYDNQV 180
Cdd:PRK14354  148 EVEKIvEQKdatEEEKQIKEINTGTYCFDNKA 179
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-54 3.59e-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: 43.72  E-value: 3.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1210348224   6 LAGGSGTRLypvtQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITT 54
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVS 45
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-53 3.87e-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: 3.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1210348224   3 GIILAGGSGTRLypvtqGVSKQLLPIYNKPMIYYPLSVLMLAGiRDILVIT 53
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVA 45
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-208 5.94e-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: 43.40  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYplSVLMLAGIRDILVITTAQEQQLFKNLLGDGTQFGVKLEYAVQEKP 83
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDSRFIFICRDEHNTKFHLDESLKLLAPNATVVELDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  84 EGLAQAF--VIAETFIGNESVCLVLGDNIFYGQAFSPYLNNAAQLTHGAMVFGYPVADPeRFGVVEFNEAGKVTSIEEKp 161
Cdd:cd04183    80 ETLGAACtvLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVIETAEK- 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1210348224 162 sQPKSNFAVTGLYFYDN--QVVDIAKTVKP---SSRGELEITCINRAYLERG 208
Cdd:cd04183   158 -EPISDLATAGLYYFKSgsLFVEAAKKMIRkddSVNGEFYISPLYNELILDG 208
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-60 1.05e-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: 42.10  E-value: 1.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRLypvtqGVSKQLLPIYNKPMIYYPLSVlmLAGIRDILVITTAQEQQL 60
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRPERY 57
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-60 1.43e-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: 42.21  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1210348224   3 GIILAGGSGTRLYPVTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQL 60
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQI 60
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-160 1.89e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.54  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   4 IILAGGSGTRLypvTQGVSKQLLPIYNKPMIYYPLSVLMLAGIRDILVITTAQEQQLFKNLlgdgTQFGVKLEYAVQEKP 83
Cdd:PRK14353    9 IILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAA----AKIAPDAEIFVQKER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  84 EGLAQAFVIAETFI--GNESVCLVLGDNIFYGQAfsPYLNNAAQLTHGA--MVFGYPVADPERFG-VVEfnEAGKVTSI- 157
Cdd:PRK14353   82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAE--TLARLRERLADGAdvVVLGFRAADPTGYGrLIV--KGGRLVAIv 157


                  ...
gi 1210348224 158 EEK 160
Cdd:PRK14353  158 EEK 160
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-67 1.00e-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: 40.22  E-value: 1.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1210348224   4 IILAGGSGTRLypvTQGVSKQLLPIYNKPMIYYPLSVLMLAG-IRDILVITTAQEQQLFKNLLGD 67
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-198 1.41e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 39.75  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224   1 MKGIILAGGSGTRL---YPvtqgvsKQLLPIYNKPMIYYplsVLMLAG-IRDILVITTAQEQQLFKNLLGDgtqfgvKLE 76
Cdd:PRK14357    1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINW---VIDTAKkVAQKVGVVLGHEAELVKKLLPE------WVK 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210348224  77 YAVQEKPEGLAQAFVIAETFIG-NESVCLVLGDNIFYGQAFSPYLNNAAQLTHG-AMVFGYPVADPERFGVVeFNEAGKV 154
Cdd:PRK14357   66 IFLQEEQLGTAHAVMCARDFIEpGDDLLILYGDVPLISENTLKRLIEEHNRKGAdVTILVADLEDPTGYGRI-IRDGGKY 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1210348224 155 TSIEEKPSQPKSNFAV---TGLYFYD-NQVVDIAKTVKP-SSRGELEIT 198
Cdd:PRK14357  145 RIVEDKDAPEEEKKIKeinTGIYVFSgDFLLEVLPKIKNeNAKGEYYLT 193
 
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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