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Conserved domains on  [gi|499282689|ref|WP_010975749|]
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glucose-1-phosphate thymidylyltransferase RfbA [Sinorhizobium meliloti]

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];
1-289 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 502.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  81 PEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEE 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDED-GRVVSLEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRT 240
Cdd:COG1209  160 KPKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLT 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499282689 241 IEHRQGVKIMCPEEIALELGYVSADQVLQRADLLGKNDYAIYLRRRVRE 289
Cdd:COG1209  240 IEKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 502.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  81 PEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEE 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDED-GRVVSLEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRT 240
Cdd:COG1209  160 KPKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLT 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499282689 241 IEHRQGVKIMCPEEIALELGYVSADQVLQRADLLGKNDYAIYLRRRVRE 289
Cdd:COG1209  240 IEKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-285 9.83e-176

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: 486.51  E-value: 9.83e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689    2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   82 EPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEEK 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSN-GRAISIEEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  162 PELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRTI 241
Cdd:TIGR01207 160 PAQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTI 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 499282689  242 EHRQGVKIMCPEEIALELGYVSADQVLQRADLLGKNDYAIYLRR 285
Cdd:TIGR01207 240 EKRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLR 283
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-241 8.43e-155

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: 431.61  E-value: 8.43e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  81 PEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDgETGRAETIEE 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFD-ENGRVLSIEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRT 240
Cdd:cd02538  160 KPKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQT 239

                 .
gi 499282689 241 I 241
Cdd:cd02538  240 I 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-290 2.71e-137

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 389.42  E-value: 2.71e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  82 EPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDgETGRAETIEEK 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFD-QNGTAISLEEK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 162 PELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRTI 241
Cdd:PRK15480 164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499282689 242 EHRQGVKIMCPEEIALELGYVSADQVLQRADLLGKNDYAIYLRRRVREL 290
Cdd:PRK15480 244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 1.01e-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: 294.93  E-value: 1.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689    2 KGIILAGGRGTRLYPVTISVSKQLLPVHDK-PMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   81 PEPNGLAEAFIIGRDFIGNSSV-ALILGDNIFYGAGLPELCSDAAARPS--GATIFAYRVDDPERYGVVSFDgETGRAET 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFD-DNGRVIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  158 IEEKPELAR-SSWAVTGLYFYENSVLE-IASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAA 235
Cdd:pfam00483 160 FVEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEAN 239

                  ...
gi 499282689  236 SFV 238
Cdd:pfam00483 240 LFL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 502.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  81 PEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEE 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDED-GRVVSLEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRT 240
Cdd:COG1209  160 KPKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLT 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499282689 241 IEHRQGVKIMCPEEIALELGYVSADQVLQRADLLGKNDYAIYLRRRVRE 289
Cdd:COG1209  240 IEKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-285 9.83e-176

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: 486.51  E-value: 9.83e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689    2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   82 EPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEEK 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSN-GRAISIEEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  162 PELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRTI 241
Cdd:TIGR01207 160 PAQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTI 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 499282689  242 EHRQGVKIMCPEEIALELGYVSADQVLQRADLLGKNDYAIYLRR 285
Cdd:TIGR01207 240 EKRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLR 283
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-241 8.43e-155

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: 431.61  E-value: 8.43e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  81 PEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDgETGRAETIEE 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFD-ENGRVLSIEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRT 240
Cdd:cd02538  160 KPKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQT 239

                 .
gi 499282689 241 I 241
Cdd:cd02538  240 I 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-290 2.71e-137

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 389.42  E-value: 2.71e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  82 EPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDgETGRAETIEEK 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFD-QNGTAISLEEK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 162 PELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAASFVRTI 241
Cdd:PRK15480 164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499282689 242 EHRQGVKIMCPEEIALELGYVSADQVLQRADLLGKNDYAIYLRRRVREL 290
Cdd:PRK15480 244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKGY 292
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 1.01e-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: 294.93  E-value: 1.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689    2 KGIILAGGRGTRLYPVTISVSKQLLPVHDK-PMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   81 PEPNGLAEAFIIGRDFIGNSSV-ALILGDNIFYGAGLPELCSDAAARPS--GATIFAYRVDDPERYGVVSFDgETGRAET 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFD-DNGRVIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  158 IEEKPELAR-SSWAVTGLYFYENSVLE-IASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYAWLDTGTHDSLHDAA 235
Cdd:pfam00483 160 FVEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEAN 239

                  ...
gi 499282689  236 SFV 238
Cdd:pfam00483 240 LFL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-234 1.83e-67

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: 210.12  E-value: 1.83e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRdRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  81 PEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGaGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGetGRAETIEE 160
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD--GRIVRLVE 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282689 161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYaWLDTGTHDSLHDA 234
Cdd:cd04189  157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEA 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-226 6.68e-63

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 197.80  E-value: 6.68e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   3 GIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRpLFEELLGDGSQFGLAISYAEQPE 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGE-QIEEYFGDGSKFGVNIEYVVQEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  83 PNGLAEAFIIGRDFIGNSSVALILGDNIFYgAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEEKP 162
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTD-LDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDD-GRVTRFVEKP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282689 163 ELARSSWAVTGLYFYENSVLEIASSIKPsaRGELEITDVNRAYLERGDLHVCRLgRGYaWLDTG 226
Cdd:cd04181  158 TLPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV-DGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-234 3.01e-56

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


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 184.91  E-value: 3.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689    2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   82 EPNGLAEAFIIGRDFIGNSSVALILGDNIFYGaGLPELCSDAAARPSGATIFAYRVDDPERYGVVSF-DGEtgRAETIEE 160
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLeDGK--RILKLVE 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282689  161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGYaWLDTGTHDSLHDA 234
Cdd:TIGR01208 158 KPKEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-226 1.34e-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: 163.53  E-value: 1.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689    1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLfEELLGDGSQFGLAISYAEQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKV-REYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   81 PEPNGLAEAFIIGRDFIgNSSVALILGDNIFYGAGLPELCsdaaaRPSGATIFAYRVDDPERYGVVSFDGetGRAETIEE 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETDG--GRVTGIVE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282689  161 KPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLHVCRLGRGyaWLDTG 226
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-250 1.91e-47

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


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 158.78  E-value: 1.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRdRPLFEELLGDGSQFGLAISYAEQP 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYL-AEQIEEYFGDGSRFGVRITYVDEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  82 EPNGLAEAFIIGRDFIGNSSVALILGDnIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEEK 161
Cdd:COG1208   80 EPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFVEK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 162 PELARSSWAVTGLYFYENSVLEIAssikpSARGELEITDVNRAYLERGDLHVCRLgRGYaWLDTGTHDSLHDAASFVRti 241
Cdd:COG1208  158 PEEPPSNLINAGIYVLEPEIFDYI-----PEGEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANALLL-- 228

                 ....*....
gi 499282689 242 EHRQGVKIM 250
Cdd:COG1208  229 SGKAPVVIW 237
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-227 1.76e-33

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


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 123.03  E-value: 1.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMP----------RDRPLFEELLGDGSQ 70
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdRSYELEETLEKKGKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  71 FGLA----------ISYAEQPEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGA--GLPELCsDAAARPSGATIFAYRVD 138
Cdd:cd02541   81 DLLEevriisdlanIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepCLKQLI-EAYEKTGASVIAVEEVP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 139 DPE--RYGVV---SFDGETGRAETIEEKP--ELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDL 211
Cdd:cd02541  160 PEDvsKYGIVkgeKIDGDVFKVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239
                        250
                 ....*....|....*..
gi 499282689 212 HVCRL-GRGYawlDTGT 227
Cdd:cd02541  240 YAYVFeGKRY---DCGN 253
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-227 1.72e-27

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 107.81  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPL---F---------------EE 63
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIedhFdrsyeleatleakgkEE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  64 LLG--DGSQFGLAISYAEQPEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGA--GLPELCsDAAARPSGATIFAYRVDD 139
Cdd:COG1210   85 LLEevRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkpCLKQMI-EVYEETGGSVIAVQEVPP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 140 PE--RYGVVS---FDGETGRAETIEEKP--ELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNRAYLERGDLH 212
Cdd:COG1210  164 EEvsKYGIVDgeeIEGGVYRVTGLVEKPapEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEPVY 243
                        250
                 ....*....|....*.
gi 499282689 213 VCRL-GRGYawlDTGT 227
Cdd:COG1210  244 AYEFeGKRY---DCGD 256
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-234 5.34e-25

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


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 99.51  E-value: 5.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVIT--MPRdrpLFEELLGDGSQFGLAISYAEQP 81
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVnyLAE---MIEDYFGDGSKFGVNISYVRED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  82 EPNGLAEAFIIGRDFIgNSSVALILGDnIFYGAGLPELCSDAAARPSGATIFA--YRVDDPerYGVVSFDGetGRAETIE 159
Cdd:cd06426   79 KPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETEG--GRITSIE 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282689 160 EKPELarsSWAV-TGLYFYENSVLEiasSIKPSARgeLEITDVNRAYLERGDLHVCRLGRGYaWLDTGTHDSLHDA 234
Cdd:cd06426  153 EKPTH---SFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-227 1.93e-24

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: 98.44  E-value: 1.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAEQ 80
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  81 PEPNGLAEAFIIGRDFI-GNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGETGRAETIE 159
Cdd:cd06425   81 TEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282689 160 EKPELARSSWAVTGLYFYENSVLEiassikpsaRGELEITDVNR----AYLERGDLHVCRLgRGYaWLDTGT 227
Cdd:cd06425  161 EKPKVFVGNKINAGIYILNPSVLD---------RIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WMDIGQ 221
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-234 1.90e-21

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: 89.92  E-value: 1.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRdRPLFEELLGDGSQFGLAISYAEQPEP 83
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYL-AEQIEEYFGDGYRGGIRIYYVIEPEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  84 NGLAEAFIIGRDFIGNSSVALILGDNiFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGEtGRAETIEEKPE 163
Cdd:cd06915   81 LGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGD-GRVIAFVEKGP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499282689 164 LARSSWAVTGLYFYENSVLEIASSIKPSargeLEiTDVNRAYLERGDLhVCRLGRGYaWLDTGTHDSLHDA 234
Cdd:cd06915  159 GAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL-YGFEVDGY-FIDIGIPEDYARA 222
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-141 5.42e-17

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: 77.70  E-value: 5.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPL----FEELLGDGSQFGLAIS 76
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEistyLRSFPLNLKQKLDEVT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  77 YAEQpEPNGLAEAF-----IIGRDFIgnssvalILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPE 141
Cdd:cd04198   81 IVLD-EDMGTADSLrhirkKIKKDFL-------VLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSS 142
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-234 3.83e-16

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: 75.69  E-value: 3.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVIT--MPRdrpLFEELLGDgSQFGLAISYae 79
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNThhLAD---QIEAHLGD-SRFGLRITI-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  80 QPEPN-------GLAEAfiigRDFIGNSSVALILGDnIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFD-GE 151
Cdd:cd06422   75 SDEPDelletggGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSlDA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 152 TGRaetIEEKPELARSSWAVTGLYFYENSVLeiaSSIKPsarGELEITDVNRAYLERGDLHVCRLgRGYaWLDTGTHDSL 231
Cdd:cd06422  150 DGR---LRRGGGGAVAPFTFTGIQILSPELF---AGIPP---GKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERL 218

                 ...
gi 499282689 232 HDA 234
Cdd:cd06422  219 LAA 221
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-231 6.77e-14

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 70.71  E-value: 6.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPR----------------------DRP 59
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSknsienhfdtsfeleamlekrvKRQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  60 LFEELLGDGSQfGLAISYAEQPEPNGLAEAFIIGRDFIGNSSVALILGDNIfygagLPELCSDAAA----------RPSG 129
Cdd:PRK13389  90 LLDEVQSICPP-HVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVI-----LDEYESDLSQdnlaemirrfDETG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 130 AT-IFAYRVDDPERYGVVSFD------GETGRAETIEEKP--ELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITD 200
Cdd:PRK13389 164 HSqIMVEPVADVTAYGVVDCKgvelapGESVPMVGVVEKPkaDVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 499282689 201 ---------VNRAYLERGDLHVC--RLGRGYAWLDTGT-HDSL 231
Cdd:PRK13389 244 aidmliekeTVEAYHMKGKSHDCgnKLGYMQAFVEYGIrHNTL 286
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-203 1.28e-13

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: 69.20  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   3 GIILAGG--RGTRLYPVTISVSKQLLPVHDKPMIYYPLGML-MLAGIREILVITMPRDRPLFEELLGDGSQFGLAISYAE 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  80 QPEPNGLAEAFIIGRDFI--GNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRV--DDPERYGVVSFDGETGRA 155
Cdd:cd06428   81 EYKPLGTAGGLYHFRDQIlaGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGCIVEDPSTGEV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499282689 156 ETIEEKPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITDVNR 203
Cdd:cd06428  161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNN 208
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-200 1.70e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 69.15  E-value: 1.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRD-------------RPLFE----- 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKnavenhfdtsyelESLLEqrvkr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  63 ELLGDGSQF---GLAISYAEQPEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAA------RPSGATIF 133
Cdd:PRK10122  84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAmiarfnETGRSQVL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282689 134 AYRV-DDPERYGVVS------FDGETGR-AETIE--EKPELARSSWAVTGLYFYENSVLEIASSIKPSARGELEITD 200
Cdd:PRK10122 164 AKRMpGDLSEYSVIQtkepldREGKVSRiVEFIEkpDQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-54 2.35e-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: 67.66  E-value: 2.35e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITM 54
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCC 54
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-213 4.25e-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: 64.18  E-value: 4.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRdRPLFEELLGDgsqfGLAISYAEQPEP 83
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYK-KEQIEELLKK----YPNIKFVYNPDY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  84 N--GLAEAFIIGRDFIGNSSVaLILGDNIFYGAGLPELCSDaaarPSGATIFAYRVDDPERYGVVSFDGETGRAETIEEK 161
Cdd:cd02523   77 AetNNIYSLYLARDFLDEDFL-LLEGDVVFDPSILERLLSS----PADNAILVDKKTKEWEDEYVKDLDDAGVLLGIISK 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499282689 162 PE-LARSSWAVTGLYFYENS----VLEIASSIKPSARGELEITDVNRAYLERGDLHV 213
Cdd:cd02523  152 AKnLEEIQGEYVGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKV 208
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-234 1.71e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 63.94  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   3 GIILAGGRGTRLYPVTISVSkqllpvhdKPMIYY---------PLGMLMLAGIREILVIT--MPRdrplfeEL---LGDG 68
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRA--------KPAVPFggkyriidfPLSNCVNSGIRRVGVLTqyKSH------SLndhIGSG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  69 SQFGLAISY-------AEQPEPN-----GLAEAFIIGRDFIGNSSV--ALIL-GDNIF---YGAGLpelcsdAAARPSGA 130
Cdd:COG0448   70 KPWDLDRKRggvfilpPYQQREGedwyqGTADAVYQNLDFIERSDPdyVLILsGDHIYkmdYRQML------DFHIESGA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 131 --TIFAYRVDDPE--RYGVVSFDgETGRAETIEEKPELARSSWAVTGLYFYENSVL--EIASSIKPSAR--GEleitDVN 202
Cdd:COG0448  144 diTVACIEVPREEasRFGVMEVD-EDGRITEFEEKPKDPKSALASMGIYVFNKDVLieLLEEDAPNSSHdfGK----DII 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 499282689 203 RAYLERGDLHVCRLgRGYaWLDTGTHDSLHDA 234
Cdd:COG0448  219 PRLLDRGKVYAYEF-DGY-WRDVGTIDSYYEA 248
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-201 8.30e-11

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 60.61  E-value: 8.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPvtiSVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITmPRDRPLFEELLGDGSqfglaISYAEQPEP 83
Cdd:cd02540    2 VILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVV-GHGAEQVKKALANPN-----VEFVLQEEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  84 NGLAEAFIIGRDFIGN-SSVALILgdnifYG-------AGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGETGRA 155
Cdd:cd02540   73 LGTGHAVKQALPALKDfEGDVLVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVL 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499282689 156 ETIEEK---PELARSSWAVTGLYFYENSVLEIA-SSIKPS-ARGELEITDV 201
Cdd:cd02540  148 RIVEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI 198
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
4-258 1.07e-10

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 61.92  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPvtiSVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGsqfglaISYAEQPEP 83
Cdd:PRK14358  11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG------VAFARQEQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  84 NGLAEAFIIGRDFI--GNSSVALILGDN-IFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVsFDGETGRAETIEE 160
Cdd:PRK14358  82 LGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRI-VRGADGAVERIVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 161 KPELARSSWAV----TGLYFYENSVLEIASSI-KPSARGELEITDVNRAYLERG-DLHVCRLGRGYAWLDTGTHDSLHDA 234
Cdd:PRK14358 161 QKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGGaQVRAFKLSDPDEVLGANDRAGLAQL 240
                        250       260
                 ....*....|....*....|....*...
gi 499282689 235 ASFVR----TIEHRQGVKIMCPEEIALE 258
Cdd:PRK14358 241 EATLRrrinEAHMKAGVTLQDPGTILIE 268
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 2.13e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 59.48  E-value: 2.13e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499282689   2 KGIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVIT 53
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-201 7.00e-10

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 59.39  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRL---YPvtisvsKQLLPVHDKPMIYYPLGmLMLAGIREILVItMPRDRPLFEELLGDGsqfglaISY 77
Cdd:PRK14357   1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVID-TAKKVAQKVGVV-LGHEAELVKKLLPEW------VKI 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  78 AEQPEPNGLAEAFIIGRDFIGNSSVALIL-GDNIFYGAG-LPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGetGRA 155
Cdd:PRK14357  67 FLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENtLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDG--GKY 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499282689 156 ETIEEK---PELARSSWAVTGLYFYE-NSVLEIASSIKP-SARGELEITDV 201
Cdd:PRK14357 145 RIVEDKdapEEEKKIKEINTGIYVFSgDFLLEVLPKIKNeNAKGEYYLTDA 195
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-209 1.19e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 55.52  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPVTISVskqLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSqfglaISYAEQPEP 83
Cdd:PRK14355   7 IILAAGKGTRMKSDLVKV---MHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEEQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  84 NGLAEAFIIGRDFI-GNSSVALIL-GDN-IFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGETGRAETIEE 160
Cdd:PRK14355  79 LGTGHAVACAAPALdGFSGTVLILcGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIVEE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499282689 161 K---PELARSSWAVTGLYFYENSVLEIA-SSIK-PSARGELEITDVNRAYLERG 209
Cdd:PRK14355 159 KdatPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEG 212
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-201 3.70e-08

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: 53.88  E-value: 3.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYpvtISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPrDRPLFEELLGDgsqfgLAISYAEQPEP 83
Cdd:COG1207    6 VILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGH-GAEQVRAALAD-----LDVEFVLQEEQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  84 NGLAEAFIIGRDFIGN-SSVALILgdnifYG-------AGLPELCSDAAARPSGATIFAYRVDDPERYGVVsFDGETGRA 155
Cdd:COG1207   77 LGTGHAVQQALPALPGdDGTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTGYGRI-VRDEDGRV 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499282689 156 ETI-EEK---PELARSSWAVTGLYFYENSVLEIA-SSIKPS-ARGELEITDV 201
Cdd:COG1207  151 LRIvEEKdatEEQRAIREINTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-67 7.58e-08

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 52.05  E-value: 7.58e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499282689   4 IILAGGRGTRLypvTISVSKQLLPVHDKPMIYYPL-GMLMLAGIREILVITMPRDRPLFEELLGD 67
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLeAFLAHPRIDEIVVVVPPDDIEYFEELLAK 62
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 6.13e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 49.36  E-value: 6.13e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282689   4 IILAGGRGTRLYPvtiSVSKQLLPVHDKPMIYYPLGMLMLAG-IREILVITMPRDRPLFEELL 65
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-111 6.97e-07

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: 48.69  E-value: 6.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   3 GIILAGGRGTRLYPVTISVSKQLLPVHDK-PMIYYPLGMLMLAGIREILVITMPRDRPLFEEL------LGDGSQFGLAI 75
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLgsgkewDLDRKNGGLFI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499282689  76 SYAEQ-PEPN---GLAEAFIIGRDFIGNSSV--ALIL-GDNIF 111
Cdd:cd02508   81 LPPQQrKGGDwyrGTADAIYQNLDYIERSDPeyVLILsGDHIY 123
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-68 1.17e-06

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: 48.29  E-value: 1.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282689   4 IILAGGRGTRLypvTISVSKQLLPVHDKPMIYYPLGMLM-LAGIREILVITMPRDRPLFEELLGDG 68
Cdd:cd02516    4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-201 1.71e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.06  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTR----LYPVtisvskqLLPVHDKPMIYYPLGMLMLAGIREILVItMPRDRPLFEELLGDGSQfglaisYAE 79
Cdd:PRK14354   6 IILAAGKGTRmkskLPKV-------LHKVCGKPMVEHVVDSVKKAGIDKIVTV-VGHGAEEVKEVLGDRSE------FAL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  80 QPEPNGLAEAFIIGRDFIGNSS--VALILGDN-IFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDgETGRAE 156
Cdd:PRK14354  72 QEEQLGTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRN-ENGEVE 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499282689 157 TI-EEK---PELARSSWAVTGLYFYENSVL-EIASSIKP-SARGELEITDV 201
Cdd:PRK14354 151 KIvEQKdatEEEKQIKEINTGTYCFDNKALfEALKKISNdNAQGEYYLTDV 201
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-68 7.14e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 45.92  E-value: 7.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282689   3 GIILAGGRGTRLypvtiSVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDG 68
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLG 66
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-68 2.74e-05

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 44.87  E-value: 2.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499282689   1 MKGIILAGGRGTRLYPV-TISVSKQLLPV-HDKPMIYYPLGMLM-LAGIREILVITMPRDRPLFEELLGDG 68
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDRLKgLVPPDRILVVTNEEYRFLVREQLPEG 71
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-65 3.27e-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: 3.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   6 LAGGRGTRLYpvtiSVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDrPLFEELL 65
Cdd:COG2266    1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNT-PKTREYL 55
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-177 3.74e-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: 44.17  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYplGMLMLAGIREilvitmprDRPLFEELLGDGSQFGLAISYAE---- 79
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFD--------SRFIFICRDEHNTKFHLDESLKLlapn 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  80 ------QPEPNGLAEAFIIGRDFIGNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPeRYGVVSFDGETG 153
Cdd:cd04183   72 atvvelDGETLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGR 150
                        170       180
                 ....*....|....*....|....
gi 499282689 154 RAETIEEKPelaRSSWAVTGLYFY 177
Cdd:cd04183  151 VIETAEKEP---ISDLATAGLYYF 171
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-161 6.36e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.08  E-value: 6.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   4 IILAGGRGTRLYPvtiSVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPrDRPLFEELLgdgSQFGLAISYAEQPEP 83
Cdd:PRK14353   9 IILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAA---AKIAPDAEIFVQKER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  84 NGLAEAFIIGRDFI--GNSSVALILGDNIFYGAGLPELCSDAAARPSGATIFAYRVDDPERYGVVSFDGetGRAETI-EE 160
Cdd:PRK14353  82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGRLIVKG--GRLVAIvEE 159

                 .
gi 499282689 161 K 161
Cdd:PRK14353 160 K 160
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-68 1.02e-04

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: 41.80  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282689    3 GIILAGGRGTRLypvtiSVSKQLLPVHDKPMIYYPLGMLMLAGiREILVITmpRDRPLFEELLGDG 68
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVA--NDEEVLAALAGLG 58
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
3-53 1.14e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 43.34  E-value: 1.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499282689   3 GIILAGGRGTRLYPVTISVSKQLLPVHDK-PMIYYPLGMLMLAGIREILVIT 53
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-234 1.26e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.93  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPVTISVSKQLLPVHDK-PMIYYPLGMLMLAGIREILVITmpRDRPLfeEL---LGDGSQFGL--- 73
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT--QYQPL--ELnnhIGIGSPWDLdri 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  74 ----AI--SYAEQPEPN---GLAEAFIIGRDFIG--NSSVALIL-GDNIF---YGAGLPELCSDAAArpsgATIFAYRV- 137
Cdd:PRK05293  80 nggvTIlpPYSESEGGKwykGTAHAIYQNIDYIDqyDPEYVLILsGDHIYkmdYDKMLDYHKEKEAD----VTIAVIEVp 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689 138 -DDPERYGVVSFDgETGRAETIEEKPELARSSWAVTGLYFYENSVLE---IASSIKPSAR---GEleitDVNRAYLERGD 210
Cdd:PRK05293 156 wEEASRFGIMNTD-ENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKeylIEDEKNPNSShdfGK----NVIPLYLEEGE 230
                        250       260
                 ....*....|....*....|....
gi 499282689 211 LHVCRLGRGYaWLDTGTHDSLHDA 234
Cdd:PRK05293 231 KLYAYPFKGY-WKDVGTIESLWEA 253
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-134 1.30e-04

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: 41.78  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   3 GIILAGGRGTRLypvtiSVSKQLLPVHDKPMIYYPLGMLMLAGIREILVITMPRDRPLFEELLGDGSQFGlaisYAEQPE 82
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVV----INPDWE 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689  83 pNGLAEAFIIGRDFIGNSS--VALILGDnifygagLPELCSD------AAARPSGATIFA 134
Cdd:cd04182   74 -EGMSSSLAAGLEALPADAdaVLILLAD-------QPLVTAEtlraliDAFREDGAGIVA 125
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-64 1.76e-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: 41.72  E-value: 1.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282689   1 MKGIILAGGRGTRLYpvtisVSKQLLPVHDKPMIYYPLGMLMLAgIREILVITmpRDRPLFEEL 64
Cdd:COG0746    5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVA--NRPERYAAL 60
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-52 6.14e-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: 40.28  E-value: 6.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 499282689   3 GIILAGGRGTRLYPVTISVSKQLLPVHDKPMIYYPLGMLMLAGIREILVI 52
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
4-53 7.03e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 40.59  E-value: 7.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499282689   4 IILAGGRGTRLYPVTISVSKQLLPVHDK-PMIYYPLGMLMLAGIREILVIT 53
Cdd:PRK00725  19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLT 69
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 7.78e-04

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.43  E-value: 7.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282689   1 MKGIILAGGRGTRLYPvtisVS-----KQLLP-VHDKPMIYYPLGMLM-LAGIREILVIT 53
Cdd:COG0836    3 IYPVILAGGSGTRLWP----LSresypKQFLPlLGEKSLLQQTVERLAgLVPPENILVVT 58
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-66 2.42e-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: 37.94  E-value: 2.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282689   1 MKGIILAGGRGTRL-YPvtisvsKQLLPVHDKPMIYYPLGMLMLAgIREILVITmpRDRPLFEELLG 66
Cdd:cd02503    1 ITGVILAGGKSRRMgGD------KALLELGGKPLLEHVLERLKPL-VDEVVISA--NRDQERYALLG 58
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
4-69 5.68e-03

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


Pssm-ID: 460075  Cd Length: 219  Bit Score: 37.43  E-value: 5.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282689    4 IILAGGRGTRLypvTISVSKQLLPVHDKPMIYYPL-GMLMLAGIREILVITMPRDRPLFEELLGDGS 69
Cdd:pfam01128   2 VIPAAGSGKRM---GAGVPKQFLQLLGQPLLEHTVdAFLASPVVDRIVVAVSPDDTPEFRQLLGDPS 65
 
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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