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Conserved domains on  [gi|1473965910|ref|WP_118388873|]
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MULTISPECIES: glucose-1-phosphate thymidylyltransferase RfbA [Collinsella]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

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

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

Graphical summary

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List of domain hits

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

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 530.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVQNAESgrATVFGYHVDDPERFGVVEFDGEGRAVSIE 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESG--ATIFGYKVEDPERYGVVEFDEDGRVVSLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 161 EKPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVR 240
Cdd:COG1209   159 EKPKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1473965910 241 AVEHSQDLPVSVPEEIAWENGWITTAELEEAAKAYGKSVYGQHLKKVAAGEIV 293
Cdd:COG1209   239 TIEKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRA 291
 
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: 530.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVQNAESgrATVFGYHVDDPERFGVVEFDGEGRAVSIE 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESG--ATIFGYKVEDPERYGVVEFDEDGRVVSLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 161 EKPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVR 240
Cdd:COG1209   159 EKPKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1473965910 241 AVEHSQDLPVSVPEEIAWENGWITTAELEEAAKAYGKSVYGQHLKKVAAGEIV 293
Cdd:COG1209   239 TIEKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRA 291
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-288 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: 502.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  82 SPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAvqNAESGRATVFGYHVDDPERFGVVEFDGEGRAVSIEE 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRA--AARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 162 KPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVRA 241
Cdd:TIGR01207 159 KPAQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQT 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1473965910 242 VEHSQDLPVSVPEEIAWENGWITTAELEEAAKAYGKSVYGQHLKKVA 288
Cdd:TIGR01207 239 IEKRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-242 7.57e-163

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: 452.41  E-value: 7.57e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVQNaeSGRATVFGYHVDDPERFGVVEFDGEGRAVSIE 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQ--KEGATVFGYEVNDPERYGVVEFDENGRVLSIE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 161 EKPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVR 240
Cdd:cd02538   159 EKPKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQ 238


                  ..
gi 1473965910 241 AV 242
Cdd:cd02538   239 TI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-290 2.94e-138

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 392.11  E-value: 2.94e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  82 SPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVqNAESGrATVFGYHVDDPERFGVVEFDGEGRAVSIEE 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAV-NKESG-ATVFAYHVNDPERYGVVEFDQNGTAISLEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 162 KPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVRA 241
Cdd:PRK15480  163 KPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIAT 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1473965910 242 VEHSQDLPVSVPEEIAWENGWITTAELEEAAKAYGKSVYGQHLKKVAAG 290
Cdd:PRK15480  243 IEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKG 291
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-239 7.57e-96

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: 282.60  E-value: 7.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDK-PMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPC-ALVLGDNIFYGNGLSRHLTRAVQNAESGRATVFGYHVDDPERFGVVEFDGEGRAVSI 159
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 160 EEKPAEPK-SSYAVTGLYFYPGDVAAK-AHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAE 237
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1473965910 238 FV 239
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: 530.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVQNAESgrATVFGYHVDDPERFGVVEFDGEGRAVSIE 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESG--ATIFGYKVEDPERYGVVEFDEDGRVVSLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 161 EKPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVR 240
Cdd:COG1209   159 EKPKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1473965910 241 AVEHSQDLPVSVPEEIAWENGWITTAELEEAAKAYGKSVYGQHLKKVAAGEIV 293
Cdd:COG1209   239 TIEKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRA 291
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-288 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: 502.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  82 SPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAvqNAESGRATVFGYHVDDPERFGVVEFDGEGRAVSIEE 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRA--AARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 162 KPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVRA 241
Cdd:TIGR01207 159 KPAQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQT 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1473965910 242 VEHSQDLPVSVPEEIAWENGWITTAELEEAAKAYGKSVYGQHLKKVA 288
Cdd:TIGR01207 239 IEKRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-242 7.57e-163

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: 452.41  E-value: 7.57e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVQNaeSGRATVFGYHVDDPERFGVVEFDGEGRAVSIE 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQ--KEGATVFGYEVNDPERYGVVEFDENGRVLSIE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 161 EKPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVR 240
Cdd:cd02538   159 EKPKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQ 238


                  ..
gi 1473965910 241 AV 242
Cdd:cd02538   239 TI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-290 2.94e-138

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 392.11  E-value: 2.94e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  82 SPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVqNAESGrATVFGYHVDDPERFGVVEFDGEGRAVSIEE 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAV-NKESG-ATVFAYHVNDPERYGVVEFDQNGTAISLEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 162 KPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAEFVRA 241
Cdd:PRK15480  163 KPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIAT 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1473965910 242 VEHSQDLPVSVPEEIAWENGWITTAELEEAAKAYGKSVYGQHLKKVAAG 290
Cdd:PRK15480  243 IEERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKG 291
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-239 7.57e-96

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: 282.60  E-value: 7.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDK-PMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPC-ALVLGDNIFYGNGLSRHLTRAVQNAESGRATVFGYHVDDPERFGVVEFDGEGRAVSI 159
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 160 EEKPAEPK-SSYAVTGLYFYPGDVAAK-AHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYAWLDTGTMESLHEAAE 237
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 1473965910 238 FV 239
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-239 1.17e-72

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: 223.60  E-value: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDlPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEPCALVLGDNIFyGNGLSRHltraVQNAESGR--ATVFGYHVDDPERFGVVEFDGeGRAVS 158
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLI-QEGISPL----VRDFLEEDadASILLAEVEDPRRFGVAVVDD-GRIVR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 159 IEEKPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYaWLDTGTMESLHEAAEF 238
Cdd:cd04189   154 LVEKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRL 232


                  .
gi 1473965910 239 V 239
Cdd:cd04189   233 L 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-227 1.78e-64

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: 202.04  E-value: 1.78e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPtdLPN-FERLLGDGSRYGVNLSYAEQP 81
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGY--LGEqIEEYFGDGSKFGVNIEYVVQE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  82 SPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNgLSRHLtrAVQNAESGRATVFGYHVDDPERFGVVEFDGEGRAVSIEE 161
Cdd:cd04181    79 EPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD-LSELL--RFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1473965910 162 KPAEPKSSYAVTGLYFYPGDVAAKAHEVKPsaRGELEITTLNQMYLEEGTLSVVTLgRGYaWLDTG 227
Cdd:cd04181   156 KPTLPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV-DGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-235 6.92e-57

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: 186.84  E-value: 6.92e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  82 SPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGnGLSRHLTRAvqNAESGRATVFGYHVDDPERFGVVEFDGEGRAVSIEE 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSF--EEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVE 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1473965910 162 KPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGYaWLDTGTMESLHEA 235
Cdd:TIGR01208 158 KPKEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-227 8.00e-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: 164.30  E-value: 8.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDlPNFERLLGDGSRYGVNLSYAEQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSPDGLAQAFTIGEEFIDGEpcALVL-GDNIFYGNGLsRHLTRAVQNAesgratVFGYHVDDPERFGVVEFDGeGRAVSI 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDDE--FLVLnGDVLLDSDLL-ERLIRAEAPA------IAVVEVDDPSDYGVVETDG-GRVTGI 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1473965910 160 EEKPAEPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYLEEGTLSVVTLGRGyaWLDTG 227
Cdd:TIGR03992 150 VEKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-241 1.01e-46

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: 156.85  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDIlVISTPtDLPN-FERLLGDGSRYGVNLSYAEQ 80
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVG-YLAEqIEEYFGDGSRFGVRITYVDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  81 PSP----DGLAQAftigEEFIDGEPCALVLGDNIFygnglSRHLTRAVQNAESGR--ATVFGYHVDDPERFGVVEFDGEG 154
Cdd:COG1208    79 GEPlgtgGALKRA----LPLLGDEPFLVLNGDILT-----DLDLAALLAFHREKGadATLALVPVPDPSRYGVVELDGDG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 155 RAVSIEEKPAEPKSSYAVTGLYFYPGDVAAKAHEvkpsaRGELEITTLNQMYLEEGTLSVVTLgRGYaWLDTGTMESLHE 234
Cdd:COG1208   150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLE 222


                  ....*..
gi 1473965910 235 AAEFVRA 241
Cdd:COG1208   223 ANALLLS 229
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-235 6.56e-30

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: 113.78  E-value: 6.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPT--------DlPNFE---RLLGDGS 69
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfD-RSYEleeTLEKKGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  70 R----------YGVNLSYAEQPSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYG-NGLSRHLTRAVQnaESGRATVFGYH 138
Cdd:cd02541    80 TdlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSkEPCLKQLIEAYE--KTGASVIAVEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 139 VDDPE--RFGVVE-FDGEGRAVSIE---EKPA--EPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEIT-TLNQMYLEE 209
Cdd:cd02541   158 VPPEDvsKYGIVKgEKIDGDVFKVKglvEKPKpeEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTdAIAKLLEEE 237

                         250       260
                  ....*....|....*....|....*.
gi 1473965910 210 GTLSVVTLGRGYawlDTGTMESLHEA 235
Cdd:cd02541   238 PVYAYVFEGKRY---DCGNKLGYLKA 260
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-235 6.83e-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: 6.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDIlVISTptdlpNF-----ERLLGDGSRYGVNLSYA 78
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISV-----NYlaemiEDYFGDGSKFGVNISYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  79 EQPSPDGLAQAFTIGEEFIDgEPCALVLGD---NIFYGNGLSRHLTravQNAEsgrATVFG--YHVDDPerFGVVEFDGe 153
Cdd:cd06426    76 REDKPLGTAGALSLLPEKPT-DPFLVMNGDiltNLNYEHLLDFHKE---NNAD---ATVCVreYEVQVP--YGVVETEG- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 154 GRAVSIEEKPAEpkSSYAVTGLYFypgdvaakaheVKPSARGELE------ITTLNQMYLEEGTLSVVTLGRGYaWLDTG 227
Cdd:cd06426   146 GRITSIEEKPTH--SFLVNAGIYV-----------LEPEVLDLIPkneffdMPDLIEKLIKEGKKVGVFPIHEY-WLDIG 211


                  ....*...
gi 1473965910 228 TMESLHEA 235
Cdd:cd06426   212 RPEDYEKA 219
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-176 1.48e-20

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: 88.04  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRD-ILVIS-TPTDLPNFERLLGDgsRYGVNLSYA 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  79 EQPSPDGLAQAFTIGEEFI-DGEPCALVLGDNIF----YGNGLSRHltravqNAESGRATVFGYHVDDPERFGVVEFD-G 152
Cdd:cd06425    79 IETEPLGTAGPLALARDLLgDDDEPFFVLNSDVIcdfpLAELLDFH------KKHGAEGTILVTKVEDPSKYGVVVHDeN 152

                         170       180
                  ....*....|....*....|....
gi 1473965910 153 EGRAVSIEEKPAEPKSSYAVTGLY 176
Cdd:cd06425   153 TGRIERFVEKPKVFVGNKINAGIY 176
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-228 2.23e-18

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 83.16  E-value: 2.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPT--------DL-PNFERLL---GDGS 69
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGkraiedhfDRsYELEATLeakGKEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  70 RY--------GVNLSYAEQPSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNglSRHLTRAVQNAESGRATVFG-YHVD 140
Cdd:COG1210    85 LLeevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQMIEVYEETGGSVIAvQEVP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 141 DPE--RFGVVEFDG-EGRAVSIE---EKPA--EPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITT-LNQMYLEEGT 211
Cdd:COG1210   163 PEEvsKYGIVDGEEiEGGVYRVTglvEKPApeEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDaIAALAKEEPV 242

                         250
                  ....*....|....*..
gi 1473965910 212 LSVVTLGRGYawlDTGT 228
Cdd:COG1210   243 YAYEFEGKRY---DCGD 256
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-176 2.44e-18

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: 81.83  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDIL--------VIstptdlpnfERLLGDGSRYGVNL 75
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVlsvgylaeQI---------EEYFGDGYRGGIRI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  76 SYAEQPSPDGLAQAFTIGEEFIDGEPCALVLGDNIFYGNgLSRhLTRAVQNAeSGRATVFGYHVDDPERFGVVEFDGEGR 155
Cdd:cd06915    73 YYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD-LLA-LLAALRAS-GADATMALRRVPDASRYGNVTVDGDGR 149

                         170       180
                  ....*....|....*....|.
gi 1473965910 156 AVSIEEKPAEPKSSYAVTGLY 176
Cdd:cd06915   150 VIAFVEKGPGAAPGLINGGVY 170
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-178 1.66e-16

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 78.96  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGGSGTRLYPLTLVTSKqllpvydkPMIYY---------PLSTLMLAGIRDILVIsTPTdlpNFERL---LGDGSR 70
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVL-TQY---KSHSLndhIGSGKP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  71 YGVN--------LSYAEQPSPD----GLAQAFTIGEEFIDGEPCALVL---GDNIF---YGNGLSRHLTRavqNAEsgrA 132
Cdd:COG0448    72 WDLDrkrggvfiLPPYQQREGEdwyqGTADAVYQNLDFIERSDPDYVLilsGDHIYkmdYRQMLDFHIES---GAD---I 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1473965910 133 TVFGYHVDDPE--RFGVVEFDGEGRAVSIEEKPAEPKSSYAVTGLYFY 178
Cdd:COG0448   146 TVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVF 193
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-57 3.98e-16

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: 75.39  E-value: 3.98e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTD 57
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-235 1.14e-15

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: 74.14  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVistptdlpN-------FERLLGDgSRYGVN 74
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV--------NthhladqIEAHLGD-SRFGLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  75 LSYAEQP-----SPDGLAQAftigEEFIDGEPCALVLGDnIFYGNGLSRHLTRAVQNAESGRATVFGYHVDDPERFGVVE 149
Cdd:cd06422    72 ITISDEPdelleTGGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 150 FDGEGRavsIEEKPAEPKSSYAVTGLYFYpgdvaakahevKPS--ARGELEITTLNQMY---LEEGTLSVVtLGRGYaWL 224
Cdd:cd06422   147 LDADGR---LRRGGGGAVAPFTFTGIQIL-----------SPElfAGIPPGKFSLNPLWdraIAAGRLFGL-VYDGL-WF 210

                         250
                  ....*....|.
gi 1473965910 225 DTGTMESLHEA 235
Cdd:cd06422   211 DVGTPERLLAA 221
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-200 5.51e-14

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 70.69  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVI--STPTDLPN-------FERLLGDGSRY 71
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthASKNAVENhfdtsyeLESLLEQRVKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  72 ------------GVNLSYAEQPSPDGLAQAFTIGEEFIDGEPCALVLGDnIFYGNGLSRHL-----TRAVQNAESGRATV 134
Cdd:PRK10122   84 qllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPD-VVIDDASADPLrynlaAMIARFNETGRSQV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1473965910 135 FGYHV-DDPERFGVVE----FDGEG---RAVSIEEKPAEPK---SSYAVTGLYFYPGDVAAKAHEVKPSARGELEIT 200
Cdd:PRK10122  163 LAKRMpGDLSEYSVIQtkepLDREGkvsRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-212 1.94e-13

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 69.16  E-value: 1.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVI--STPTDLPN-----FE-----------R 63
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthSSKNSIENhfdtsFEleamlekrvkrQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  64 LLGDGSRY---GVNLSYAEQPSPDGLAQAFTIGEEFIDGEPCALVLGDNIF--YGNGLSR-HLTRAVQN-AESGRATVFG 136
Cdd:PRK13389   90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQdNLAEMIRRfDETGHSQIMV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 137 YHVDDPERFGVVEFDGEGRA-------VSIEEKPA--EPKSSYAVTGLYFYPGDVAAKAHEVKPSARGELEITTLNQMYL 207
Cdd:PRK13389  170 EPVADVTAYGVVDCKGVELApgesvpmVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLI 249


                  ....*
gi 1473965910 208 EEGTL 212
Cdd:PRK13389  250 EKETV 254
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-52 2.11e-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: 68.05  E-value: 2.11e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVI 52
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-235 1.67e-11

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: 62.64  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVI----STptdlpNFERLLGDgsRYGVNLSYAE 79
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVtgykKE-----QIEELLKK--YPNIKFVYNP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  80 QPSPDGLAQAFTIGEEFIDgEPCALVLGDNIFYGNGLSRHLtravqnAESGRATVFgyhVDDPERFGVVEFD----GEGR 155
Cdd:cd02523    75 DYAETNNIYSLYLARDFLD-EDFLLLEGDVVFDPSILERLL------SSPADNAIL---VDKKTKEWEDEYVkdldDAGV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 156 AVSIEEKPAEPKSSYAVT-GLYFYPGDVAAKAH----EVKPSARGELEITTLNQMYLEEGTLSVVTLGrGYAWLDTGTME 230
Cdd:cd02523   145 LLGIISKAKNLEEIQGEYvGISKFSPEDADRLAealeELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLE 223


                  ....*
gi 1473965910 231 SLHEA 235
Cdd:cd02523   224 DLERA 228
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-240 1.04e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 60.64  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   2 KGIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVIstpT----DLpnFERLLGdgsRYGVNLSY 77
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV---TgykaEL--IEEALA---RPGPDVTF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  78 AEQPSPDGLAQAFT--IGEEFIDgEPCALVLGDnIFYGnglSRHLTRAVQNAESGRATV--FGYHVDDPERFgvVEFDGE 153
Cdd:COG1213    73 VYNPDYDETNNIYSlwLAREALD-EDFLLLNGD-VVFD---PAILKRLLASDGDIVLLVdrKWEKPLDEEVK--VRVDED 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 154 GRAVSIEEKPAEPKSSYAVTGLYFYPGDVAAKAHEvkpsARGELEITTLNQMYLEEG---------TLSVVTLGrGYAWL 224
Cdd:COG1213   146 GRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALRE----ALEALIDEGGPNLYYEDAlqelideggPVKAVDIG-GLPWV 220

                         250
                  ....*....|....*.
gi 1473965910 225 DTGTMESLHEAAEFVR 240
Cdd:COG1213   221 EIDTPEDLERAEELFA 236
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-235 8.16e-10

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 59.11  E-value: 8.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRLYPLTLVTSKQLLPVYDK-PMIYYPLSTLMLAGIRDILVIST--PTDLPNFerlLGDGSRYGVN--- 74
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQyqPLELNNH---IGIGSPWDLDrin 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  75 -----LS-YAEQPSPD---GLAQAFTIGEEFIDG-EP-CALVL-GDNIF---YGNGLSRHltraVQNAESGRATVFGYHV 139
Cdd:PRK05293   81 ggvtiLPpYSESEGGKwykGTAHAIYQNIDYIDQyDPeYVLILsGDHIYkmdYDKMLDYH----KEKEADVTIAVIEVPW 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 140 DDPERFGVVEFDGEGRAVSIEEKPAEPKSSYAVTGLYFY---------------PGDVAAKAHEVKPSargeleittlnq 204
Cdd:PRK05293  157 EEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL------------ 224

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1473965910 205 mYLEEGTLSVVTLGRGYaWLDTGTMESLHEA 235
Cdd:PRK05293  225 -YLEEGEKLYAYPFKGY-WKDVGTIESLWEA 253
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-87 1.46e-08

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 54.57  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGG--SGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTL-MLAGIRDILVISTPTDLPnFERLLGDGSR-YGVNLSYA 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQQeFNVPIRYL 79


                  ....*....
gi 1473965910  79 EQPSPDGLA 87
Cdd:cd06428    80 QEYKPLGTA 88
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-53 1.70e-08

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: 53.70  E-value: 1.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1473965910   3 GIILAGGSGTRLYPLTLVTSKQLLPV---YDkpMIYYPLSTLMLAGIRDILVIS 53
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT 52
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-210 3.79e-07

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: 49.82  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLY-PLtlvtSKQLLPVYDKPMIYYPLSTLMLAGIRDI-LVISTPTDLpnFERLLGDGsrygvNLSYAEQP 81
Cdd:cd02540     2 VILAAGKGTRMKsDL----PKVLHPLAGKPMLEHVLDAARALGPDRIvVVVGHGAEQ--VKKALANP-----NVEFVLQE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  82 SPDGLAQAFTIGEEFIDGEpCALVLgdnIFYG-------NGLSRhLTRAVQNAESGrATVFGYHVDDPERFGVVEFDGEG 154
Cdd:cd02540    71 EQLGTGHAVKQALPALKDF-EGDVL---VLYGdvplitpETLQR-LLEAHREAGAD-VTVLTAELEDPTGYGRIIRDGNG 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1473965910 155 RAVSI-EEK---PAEPKSSYAVTGLYFYPGDVAAKA-HEVKPS-ARGELEITTLNQMYLEEG 210
Cdd:cd02540   145 KVLRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDIIALAVADG 206
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-169 9.13e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 49.84  E-value: 9.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLYPLTLVTSKQLLPVYDK-PMIYYPLSTLMLAGIRDILVIST-----------------PTDLPNFERLL 65
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQykahslirhiqrgwsffREELGEFVDLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  66 GDGSRYGVNLSYaeQPSPDGLAQAFTI----GEEFIdgepcaLVL-GDNIF---YGNGLSRHltravqnAESG-RATVFG 136
Cdd:PRK00725   99 PAQQRVDEENWY--RGTADAVYQNLDIirryDPKYV------VILaGDHIYkmdYSRMLADH-------VESGaDCTVAC 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1473965910 137 YHVDDPE--RFGVVEFDGEGRAVSIEEKPAEPKSS 169
Cdd:PRK00725  164 LEVPREEasAFGVMAVDENDRITAFVEKPANPPAM 198
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 1.14e-06

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: 48.59  E-value: 1.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1473965910   4 IILAGGSGTRLyplTLVTSKQLLPVYDKPMIYYPLSTLMLAG-IRDILVISTPTDLPNFERLLGD 67
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-165 1.56e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 49.11  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MK---GIILAGGSGTRLYPLTLVTSKQLLPVYDK-PMIYYPLSTLMLAGIRDILV------------ISTPTDLPNFerl 64
Cdd:PRK02862    1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVltqfnsaslnrhISQTYNFDGF--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  65 lGDGSrygVNLSYAEQP--SPD---GLAQA-----FTIGEEFIDGepcALVL-GDNIF---YGNGLSRHLTravQNAEsg 130
Cdd:PRK02862   78 -SGGF---VEVLAAQQTpeNPSwfqGTADAvrkylWHFQEWDVDE---YLILsGDQLYrmdYRLFVQHHRE---TGAD-- 145

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1473965910 131 rATVFGYHVD--DPERFGVVEFDGEGRAVSIEEKPAE 165
Cdd:PRK02862  146 -ITLAVLPVDekDASGFGLMKTDDDGRITEFSEKPKG 181
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 2.89e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 47.44  E-value: 2.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1473965910   4 IILAGGSGTRL---YPltlvtsKQLLPVYDKPMIYYPLSTLMLAG-IRDILVISTPTDLPNFERLL 65
Cdd:PRK00155    7 IIPAAGKGSRMgadRP------KQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-73 3.51e-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: 47.13  E-value: 3.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473965910   4 IILAGGSGTRlypLTLVTSKQLLPVYDKPMIYYPLSTLM-LAGIRDILVISTPTDLPNFERLLGDGSRYGV 73
Cdd:cd02516     4 IILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVV 71
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-200 4.67e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 47.84  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   1 MKGIILAGGSGTRL---YPltlvtsKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLpnFERLLGDgsrygvNLSY 77
Cdd:PRK14357    1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPE------WVKI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  78 AEQPSPDGLAQAFTIGEEFIDGEPCALVL-GDNIFYGNGLSRHLTRAvQNAESGRATVFGYHVDDPERFGVVEFDGeGRA 156
Cdd:PRK14357   67 FLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEE-HNRKGADVTILVADLEDPTGYGRIIRDG-GKY 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1473965910 157 VSIEEKPAEPKSSYAV---TGLYFYPGDVAAKA-HEVKP-SARGELEIT 200
Cdd:PRK14357  145 RIVEDKDAPEEEKKIKeinTGIYVFSGDFLLEVlPKIKNeNAKGEYYLT 193
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-168 1.81e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.59  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGGSGTRLYPLTLVTSKQLLP---VYDkpMIYYPLSTLMLAGIRDILV------------------ISTPTD---- 57
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhisqtwrLSGLLGnyit 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  58 -LPNFERLlgdGSRYgvnlsYaeQPSPDGLAQAFTIGEefiDGEP-CALVLG-DNIF---YGNGLSRHLtravqnaESG- 130
Cdd:PRK00844   86 pVPAQQRL---GKRW-----Y--LGSADAIYQSLNLIE---DEDPdYVVVFGaDHVYrmdPRQMVDFHI-------ESGa 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1473965910 131 RATVFGYHVDDPE--RFGVVEFDGEGRAVSIEEKPAEPKS 168
Cdd:PRK00844  146 GVTVAAIRVPREEasAFGVIEVDPDGRIRGFLEKPADPPG 185
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-52 2.53e-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: 2.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1473965910   1 MKGIILAGGSGTRLYPLtlvtS-----KQLLPVY-DKPMIYYPLSTLM-LAGIRDILVI 52
Cdd:cd02509     1 IYPVILAGGSGTRLWPL----SresypKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVV 55
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-52 5.59e-05

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 43.90  E-value: 5.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1473965910   1 MKGIILAGGSGTRLYPLtlvtS-----KQLLPVY-DKPMIYyplSTLM----LAGIRDILVI 52
Cdd:COG0836     3 IYPVILAGGSGTRLWPL----SresypKQFLPLLgEKSLLQ---QTVErlagLVPPENILVV 57
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-52 1.48e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 42.92  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1473965910   3 GIILAGGSGTRLYPLTLVTSKQLLPV---YDkpMIYYPLSTLMLAGIRDILVI 52
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-128 2.38e-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: 40.64  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGGSGTRLYpltlvTSKQLLPVYDKPMIYYPLSTlmLAGIRDILVISTptdlpNFERLLGDGSRYGVnlSYAEQPS 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLER--LRPAGDEVVVVA-----NDEEVLAALAGLGV--PVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1473965910  83 PD-----GLAQAFtigEEFIDGEPCALVLGDNIFYGNGLSRHLTRAVQNAE 128
Cdd:pfam12804  67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPELLRRLLAAAEESG 114
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-52 4.98e-04

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 40.14  E-value: 4.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGGSGTRLypltlVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVI 52
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV 50
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-210 5.50e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 41.12  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLYPltlVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVIStptdlpnferllGDGSRY------GVNLSY 77
Cdd:PRK14358   11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVT------------GHGAEQveaalqGSGVAF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  78 AEQPSPDGLAQAFTIGEEFI-DGEPCALVL-GDNIFYGNGLSRHLTrAVQNAESGRATVFGYHVDDPERFGVVEFDGEGR 155
Cdd:PRK14358   76 ARQEQQLGTGDAFLSGASALtEGDADILVLyGDTPLLRPDTLRALV-ADHRAQGSAMTILTGELPDATGYGRIVRGADGA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910 156 AVSIEEKPAEPKSSYAV----TGLYFYPGDVAAKAHEV-KPSARGELEITTLNQMYLEEG 210
Cdd:PRK14358  155 VERIVEQKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-108 5.92e-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: 39.85  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGGSGTRLYpltlvTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPTDLPNFERLLGDGSRYGVNLSYAEqps 82
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE--- 74

                          90       100
                  ....*....|....*....|....*...
gi 1473965910  83 pdGLAQAFTIGEEFI--DGEPCALVLGD 108
Cdd:cd04182    75 --GMSSSLAAGLEALpaDADAVLILLAD 100
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-65 8.33e-04

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 39.49  E-value: 8.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   6 LAGGSGTRLYPltlvTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVISTPtDLPNFERLL 65
Cdd:COG2266     1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREYL 55
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-167 1.27e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLYPlTLVtsKQLLPVYDKPMIYYPLSTLMLAGI-RDILVISTPTDLPNfERLLGDGsrygvNLSYAEQPS 82
Cdd:PRK14355    7 IILAAGKGTRMKS-DLV--KVMHPLAGRPMVSWPVAAAREAGAgRIVLVVGHQAEKVR-EHFAGDG-----DVSFALQEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  83 PDGLAQAFTIGEEFIDGEPCALVL--GDN-IFYGNGLSRHLTravQNAESGRA-TVFGYHVDDPERFGVVEFDGEGRAVS 158
Cdd:PRK14355   78 QLGTGHAVACAAPALDGFSGTVLIlcGDVpLLRAETLQGMLA---AHRATGAAvTVLTARLENPFGYGRIVRDADGRVLR 154

                         170
                  ....*....|
gi 1473965910 159 I-EEKPAEPK 167
Cdd:PRK14355  155 IvEEKDATPE 164
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-52 2.71e-03

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 38.36  E-value: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473965910   3 GIILAGGSGTRLYPLTLVTSKQLLPVYDKPMIYYPLSTLMLAGIRDILVI 52
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-164 2.80e-03

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: 38.85  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910   4 IILAGGSGTRLY---PltlvtsKQLLPVYDKPMIYYPLSTLMLAGIRDILVIStptdlpNFER-----LLGDgsrygVNL 75
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVV------GHGAeqvraALAD-----LDV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473965910  76 SYAEQPSPDGLAQAFTIGEEFIDGEPcALVLgdnIFYGNG--LS----RHLTRAVQNAESGrATVFGYHVDDPERFGVVE 149
Cdd:COG1207    69 EFVLQEEQLGTGHAVQQALPALPGDD-GTVL---VLYGDVplIRaetlKALLAAHRAAGAA-ATVLTAELDDPTGYGRIV 143

                         170
                  ....*....|....*.
gi 1473965910 150 FDGEGRAVSI-EEKPA 164
Cdd:COG1207   144 RDEDGRVLRIvEEKDA 159
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-57 4.66e-03

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: 37.48  E-value: 4.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1473965910   1 MKGIILAGGSGTRLYpltlvTSKQLLPVYDKPMIYYPLSTlmLAGIRDILVISTPTD 57
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP 54
 
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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