NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2647439292|ref|WP_324207332|]
View 

glucose-1-phosphate thymidylyltransferase RfbA [Sediminibacterium sp.]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-284 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 535.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDVN-GAAVFAYEVNDPERYGVVEFNEQKQAISIEEK 159
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAAREsGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 160 PKQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVI 239
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2647439292 240 EKRQSQKVGCIEEVAYRMGFIDRAQLMLLGEKYAKSGYGEYLKRL 284
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRL 285
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-284 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 535.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDVN-GAAVFAYEVNDPERYGVVEFNEQKQAISIEEK 159
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAAREsGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 160 PKQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVI 239
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2647439292 240 EKRQSQKVGCIEEVAYRMGFIDRAQLMLLGEKYAKSGYGEYLKRL 284
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRL 285
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-284 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: 501.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQH 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  82 EPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDV-NGAAVFAYEVNDPERYGVVEFNEQKQAISIEEKP 160
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARtEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 161 KQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVIE 240
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2647439292 241 KRQSQKVGCIEEVAYRMGFIDRAQLMLLGEKYAKSGYGEYLKRL 284
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-239 5.93e-162

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: 449.33  E-value: 5.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDV-NGAAVFAYEVNDPERYGVVEFNEQKQAISIEEK 159
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQkEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 160 PKQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVI 239
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-284 2.58e-134

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 381.71  E-value: 2.58e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQH 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  82 EPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQS-FNDVNGAAVFAYEVNDPERYGVVEFNEQKQAISIEEKP 160
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAaVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 161 KQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVIE 240
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2647439292 241 KRQSQKVGCIEEVAYRMGFIDRAQLMLLGEKYAKSGYGEYLKRL 284
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-236 4.96e-93

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 274.90  E-value: 4.96e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDK-PMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKV-CLILGDNIFYGAGFSKLVQSFNDVN---GAAVFAYEVNDPERYGVVEFNEQKQAISI 156
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAadaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 157 EEKPKQPK-SNYAVPGLYFYDNSVVE-IAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACE 234
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2647439292 235 FV 236
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-284 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 535.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDVN-GAAVFAYEVNDPERYGVVEFNEQKQAISIEEK 159
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAAREsGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 160 PKQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVI 239
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2647439292 240 EKRQSQKVGCIEEVAYRMGFIDRAQLMLLGEKYAKSGYGEYLKRL 284
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRL 285
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-284 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: 501.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQH 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  82 EPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDV-NGAAVFAYEVNDPERYGVVEFNEQKQAISIEEKP 160
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARtEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 161 KQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVIE 240
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2647439292 241 KRQSQKVGCIEEVAYRMGFIDRAQLMLLGEKYAKSGYGEYLKRL 284
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-239 5.93e-162

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: 449.33  E-value: 5.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDV-NGAAVFAYEVNDPERYGVVEFNEQKQAISIEEK 159
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQkEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 160 PKQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVI 239
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-284 2.58e-134

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 381.71  E-value: 2.58e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQH 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  82 EPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQS-FNDVNGAAVFAYEVNDPERYGVVEFNEQKQAISIEEKP 160
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAaVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 161 KQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACEFVRVIE 240
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2647439292 241 KRQSQKVGCIEEVAYRMGFIDRAQLMLLGEKYAKSGYGEYLKRL 284
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-236 4.96e-93

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 274.90  E-value: 4.96e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDK-PMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKV-CLILGDNIFYGAGFSKLVQSFNDVN---GAAVFAYEVNDPERYGVVEFNEQKQAISI 156
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAadaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 157 EEKPKQPK-SNYAVPGLYFYDNSVVE-IAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTAWLDTGTFDSFADACE 234
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2647439292 235 FV 236
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-236 6.28e-71

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: 218.59  E-value: 6.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQdQDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGaGFSKLVQSFNDVNGAAVFAY-EVNDPERYGVVEFnEQKQAISIEEK 159
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLaEVEDPRRFGVAVV-DDGRIVRLVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2647439292 160 PKQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGtLQVGIMNRGTAWLDTGTFDSFADACEFV 236
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRG-RRVGYSIVTGWWKDTGTPEDLLEANRLL 233
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-232 3.53e-64

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: 205.33  E-value: 3.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCSFSYEVQH 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  82 EPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGaGFSKLVQSFNDVNGAAVFAY-EVNDPERYGVVEFNEQKQAISIEEKP 160
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLtKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2647439292 161 KQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGTaWLDTGTFDSFADA 232
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-224 4.18e-58

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 185.09  E-value: 4.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   3 GIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDqDQFKRLLGDGSEIGCSFSYEVQHE 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  83 PNGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDVNGAAVFAYEVNDPERYGVVEFNEQKQAISIEEKPKQ 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2647439292 163 PKSNYAVPGLYFYDNSVVEIAKNIapSPRGEYEITDVNRVYLEKGTLQVGIMNrgTAWLDTG 224
Cdd:cd04181   160 PESNLANAGIYIFEPEILDYIPEI--LPRGEDELTDAIPLLIEEGKVYGYPVD--GYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-224 5.09e-49

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: 167.00  E-value: 5.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDqDQFKRLLGDGSEIGCSFSYEVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIgNDKVCLILGDNIFYGAGFSKLVqsfnDVNGAAVFAYEVNDPERYGVVEFNEQKqAISIEEKP 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLI----RAEAPAIAVVEVDDPSDYGVVETDGGR-VTGIVEKP 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2647439292 161 KQPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQVGIMNRGtaWLDTG 224
Cdd:TIGR03992 154 ENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-237 3.74e-40

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


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 139.52  E-value: 3.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEIlFITTPQDQDQFKRLLGDGSEIGCSFSYEVQH 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  82 EP----NGLAQAfvigEKFIGNDKVCLILGDnIFYGAGFSKLVQSFNDVNGAAVFA-YEVNDPERYGVVEFNEQKQAISI 156
Cdd:COG1208    80 EPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLAlVPVPDPSRYGVVELDGDGRVTRF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 157 EEKPKQPKSNYAVPGLYFYDNSVVEIAkniapsPRGE-YEITDVNRVYLEKGTLQVGIMNrgTAWLDTGTFDSFADACEF 235
Cdd:COG1208   155 VEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYGYVHD--GYWLDIGTPEDLLEANAL 226


                  ..
gi 2647439292 236 VR 237
Cdd:COG1208   227 LL 228
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-229 3.68e-35

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: 127.26  E-value: 3.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQD---QDQF-------KRLLGDGSE 70
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKraiEDHFdrsyeleETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  71 ----------IGCSFSYEVQHEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGA--GFSKLVQSFNDVnGAAVFAYEVND 138
Cdd:cd02541    81 dlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepCLKQLIEAYEKT-GASVIAVEEVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 139 PE---RYGVVEFNEQKQAI----SIEEKPKQ--PKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYLEKGTL 209
Cdd:cd02541   160 PEdvsKYGIVKGEKIDGDVfkvkGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239

                         250       260
                  ....*....|....*....|
gi 2647439292 210 QVGIMnRGTaWLDTGTFDSF 229
Cdd:cd02541   240 YAYVF-EGK-RYDCGNKLGY 257
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-198 4.19e-26

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 103.96  E-value: 4.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYplSV--LMLAGIKEILFITTPQD---QDQF--------------- 61
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRGKraiEDHFdrsyeleatleakgk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  62 KRLLGDGSEI--GCSFSYEVQHEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGA--GFSKLVQSFNDVNGAAVFAYEVn 137
Cdd:COG1210    83 EELLEEVRSIspLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkpCLKQMIEVYEETGGSVIAVQEV- 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 138 DPE---RYGVVEFNEQKQAI----SIEEKPKQPK--SNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITD 198
Cdd:COG1210   162 PPEevsKYGIVDGEEIEGGVyrvtGLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTD 231
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-232 2.08e-21

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: 89.88  E-value: 2.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEIlFITTPQDQDQFKRLLGDGSEIGCSFSYEVQHEP 83
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  84 NGLAQAFVIGEKFIgNDKVCLILGDnIFYGAGFSKLVQSFNDVNGAAVFA---YEVNDPerYGVVEFNEQKqAISIEEKP 160
Cdd:cd06426    81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCvreYEVQVP--YGVVETEGGR-ITSIEEKP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2647439292 161 KQpksNYAV-PGLYFYDNSVVE-IAKNIapsprgEYEITDVNRVYLEKGtLQVGIMNRGTAWLDTGTFDSFADA 232
Cdd:cd06426   156 TH---SFLVnAGIYVLEPEVLDlIPKNE------FFDMPDLIEKLIKEG-KKVGVFPIHEYWLDIGRPEDYEKA 219
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 4.67e-20

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: 86.07  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFiTTPQDQDQFKRLLGDGSEIGCSFSYEVQHEP 83
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVL-SVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  84 NGLAQAFVIGEKFIGNDKVCLILGDNiFYGAGFSKLVQSFNDVNGAAVFA-YEVNDPERYGVVEFNEQKQAISIEEKPKQ 162
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMAlRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2647439292 163 PKSNYAVPGLYFYDNSVVEIAKNIAPSprGEyeiTDVNRVYLEKGTLqVGIMNRGtAWLDTGTFDSFADAC 233
Cdd:cd06915   160 AAPGLINGGVYLLRKEILAEIPADAFS--LE---ADVLPALVKRGRL-YGFEVDG-YFIDIGIPEDYARAQ 223
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-180 1.75e-18

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: 82.26  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITT--PQDQDQFKRLLGDGSEIGCSFSYE 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  79 vqHEPNGLAQAFVIGEKFI-GNDKVCLILGDNIFYGAGFSKLVQsFNDVNG--AAVFAYEVNDPERYGVVEFNEQKQAI- 154
Cdd:cd06425    81 --TEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLD-FHKKHGaeGTILVTKVEDPSKYGVVVHDENTGRIe 157

                         170       180
                  ....*....|....*....|....*.
gi 2647439292 155 SIEEKPKQPKSNYAVPGLYFYDNSVV 180
Cdd:cd06425   158 RFVEKPKVFVGNKINAGIYILNPSVL 183
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-159 7.68e-18

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: 80.01  E-value: 7.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQ--------FKRLLGDGSEIg 72
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEistylrsfPLNLKQKLDEV- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  73 csfsYEVQHEPNGLAQAFVIGEKFIGNDkvCLILGDNIFYGAGFSKLVQSFN-DVNGAAVFAYEVNDPE----RYGVVEF 147
Cdd:cd04198    80 ----TIVLDEDMGTADSLRHIRKKIKKD--FLVLSCDLITDLPLIELVDLHRsHDASLTVLLYPPPVSSeqkgGKGKSKK 153

                         170
                  ....*....|..
gi 2647439292 148 NEQKQAISIEEK 159
Cdd:cd04198   154 ADERDVIGLDEK 165
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-210 3.79e-17

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 79.56  E-value: 3.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQD-----------------QDQFKRL 64
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKnsienhfdtsfeleamlEKRVKRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  65 LGDGSEIGCSFSYEVQHEPNGLAQ----AFVIGEKFIGNDKVCLILGDNIF--YGAGFSK-----LVQSFNDVNGAAVFA 133
Cdd:PRK13389   90 LLDEVQSICPPHVTIMQVRQGLAKglghAVLCAHPVVGDEPVAVILPDVILdeYESDLSQdnlaeMIRRFDETGHSQIMV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 134 YEVNDPERYGVVEFN-------EQKQAISIEEKPK--QPKSNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITDVNRVYL 204
Cdd:PRK13389  170 EPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLI 249


                  ....*.
gi 2647439292 205 EKGTLQ 210
Cdd:PRK13389  250 EKETVE 255
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 2.86e-15

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 74.15  E-value: 2.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQD---QDQF---------------K 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKnavENHFdtsyeleslleqrvkR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  63 RLLGDGSEI---GCSFSYEVQHEPNGLAQAFVIGEKFIGNDKVCLILGDNIFYGA-------GFSKLVQSFNDVNGAAVF 132
Cdd:PRK10122   84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplryNLAAMIARFNETGRSQVL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2647439292 133 AYEV-NDPERYGVVEFNEQ-------KQAISIEEKPKQPK---SNYAVPGLYFYDNSVVEIAKNIAPSPRGEYEITD 198
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; ...
 1-60 1.22e-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: 68.43  E-value: 1.22e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQ 60
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAI 60
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-211 6.34e-13

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: 66.49  E-value: 6.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQdQDQFKRLLGDGSEIgcSFSYEVQHEP 83
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYK-KEQIEELLKKYPNI--KFVYNPDYAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  84 NGLAQAFVIGEKFIGNDkvCLIL-GDNIFYGAGFSKLVQSfndvNGAAVFAYEVNDPERYG--VVEFNEQKQAISIEEKP 160
Cdd:cd02523    79 TNNIYSLYLARDFLDED--FLLLeGDVVFDPSILERLLSS----PADNAILVDKKTKEWEDeyVKDLDDAGVLLGIISKA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2647439292 161 KQPKSNYAVP-GLYFYDNS----VVEIAKNIAPSPRGEYEITDVNRVYLEKGTLQV 211
Cdd:cd02523   153 KNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKV 208
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-232 1.64e-12

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 65.28  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILfITTPQDQDQFKRLLGD---GSEIgcsfsyE 78
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIV-VNTHHLADQIEAHLGDsrfGLRI------T 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  79 VQHEPN-------GLAQAfvigEKFIGNDKVCLILGDnIFYGAGFSKLVQSFNDVNGAA-VFAYEVNDPERYGVVEFN-E 149
Cdd:cd06422    74 ISDEPDelletggGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALlLLLPLVRNPGHNGVGDFSlD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 150 QKQAISIEEKPKQPKSNYAvpGLYFYDNSVVEiakNIapsPRGEYEITDVNRVYLEKGTLQvGIMNRGTaWLDTGTFDSF 229
Cdd:cd06422   149 ADGRLRRGGGGAVAPFTFT--GIQILSPELFA---GI---PPGKFSLNPLWDRAIAAGRLF-GLVYDGL-WFDVGTPERL 218


                  ...
gi 2647439292 230 ADA 232
Cdd:cd06422   219 LAA 221
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-176 8.27e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 61.63  E-value: 8.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   3 GIILAGGSGTRLYPITKGISkqlmpvydKPMIYY---------PLSVLMLAGIKEILFITtpqdqdQFK-----RLLGDG 68
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRA--------KPAVPFggkyriidfPLSNCVNSGIRRVGVLT------QYKshslnDHIGSG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  69 SEigcsfsYEVQHEPNGL----AQAFVIGEK--------------FI--GNDKVCLIL-GDNIfYGAGFSKLVQSFNDvN 127
Cdd:COG0448    70 KP------WDLDRKRGGVfilpPYQQREGEDwyqgtadavyqnldFIerSDPDYVLILsGDHI-YKMDYRQMLDFHIE-S 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2647439292 128 GAA--VFAYEVNDPE--RYGVVEFNEQKQAISIEEKPKQPKSNYAVPGLYFYD 176
Cdd:COG0448   142 GADitVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 8.84e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 57.56  E-value: 8.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2647439292   2 KGIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFIT 53
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-223 2.58e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 54.38  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLypiTKGISKQLMPVYDKPMIYYPLSVLMLAGIKeiLFITTPQDQDQFKRLLGDGSEIgcsfsyEVQ 80
Cdd:PRK14357    1 MRALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQK--VGVVLGHEAELVKKLLPEWVKI------FLQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDKVCLIL-GDNIFYGAG-FSKLVQSFN-DVNGAAVFAYEVNDPERYGVVEFNEQKQAIsIE 157
Cdd:PRK14357   70 EEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENtLKRLIEEHNrKGADVTILVADLEDPTGYGRIIRDGGKYRI-VE 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2647439292 158 EK---PKQPKSNYAVPGLYFYD-NSVVEIAKNIAP-SPRGEYEITD-------VNRVYLEKGTLQVGIMNRGT-AWLDT 223
Cdd:PRK14357  149 DKdapEEEKKIKEINTGIYVFSgDFLLEVLPKIKNeNAKGEYYLTDavnfaekVRVVKTEDLLEITGVNTRIQlAWLEK 227
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 3.22e-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: 52.82  E-value: 3.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2647439292   4 IILAGGSGTRLypiTKGISKQLMPVYDKPMIYYPLSVLMLAG-IKEILFITTPQDQDQFKRLLGD 67
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-207 4.17e-08

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 53.83  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLypiTKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITtpqdqdqfkrllGDGSE------IGCSFSY 77
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVT------------GHGAEqveaalQGSGVAF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  78 EVQHEPNGLAQAFVIGEKFI--GNDKVCLILGDN-IFYGAGFSKLVQSFNDVNGA-AVFAYEVNDPERYG---------V 144
Cdd:PRK14358   76 ARQEQQLGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAmTILTGELPDATGYGrivrgadgaV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2647439292 145 VEFNEQKQAISIEEKPKQPKSnyavpGLYFYDNSVVEIAKNIA-PSPRGEYEITDVNRVYLEKG 207
Cdd:PRK14358  156 ERIVEQKDATDAEKAIGEFNS-----GVYVFDARAPELARRIGnDNKAGEYYLTDLLGLYRAGG 214
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-213 6.07e-08

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: 52.26  E-value: 6.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLYPITKGISKQLMPVYDKPMIYYplSVLMLAGI--KEILFITTPQDQDQFK-----RLLGDGSEIgcsfs 76
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIfdSRFIFICRDEHNTKFHldeslKLLAPNATV----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  77 YEVQHEPNGLAQAFVIGEKFIGNDKVCLIL-GDNIFYGAGFSKLVQSFNDVNGAAVFAYEVNDPeRYGVVEFNEQKQAIS 155
Cdd:cd04183    75 VELDGETLGAACTVLLAADLIDNDDPLLIFnCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVIE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2647439292 156 IEEKpkQPKSNYAVPGLYFYDNS--VVEIAKN-IAPSPR--GEYEITDVNRVYLEKGtLQVGI 213
Cdd:cd04183   154 TAEK--EPISDLATAGLYYFKSGslFVEAAKKmIRKDDSvnGEFYISPLYNELILDG-KKVGI 213
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-199 6.08e-08

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 52.13  E-value: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLYpitKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQdQDQFKRLLGDgseIGCSFSYevQHEP 83
Cdd:cd02540     2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHG-AEQVKKALAN---PNVEFVL--QEEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  84 NGLAQAFVIGEKFIG--NDKVcLILgdnifYG-------AGFSKLVQSFNDV-NGAAVFAYEVNDPERYG-VVEFNEQK- 151
Cdd:cd02540    73 LGTGHAVKQALPALKdfEGDV-LVL-----YGdvplitpETLQRLLEAHREAgADVTVLTAELEDPTGYGrIIRDGNGKv 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2647439292 152 QAIsIEEK---PKQPKSNYAVPGLYFYDNSVVEIA-KNIAPSP-RGEYEITDV 199
Cdd:cd02540   147 LRI-VEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNNaQGEYYLTDI 198
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-207 2.48e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 51.37  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRL---YPitkgisKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTpQDQDQFKRLLGDGSEigcsfsYEVQ 80
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVG-HGAEEVKEVLGDRSE------FALQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDK--VCLILGDN-IFYGAGFSKLVQSFNDVNGAA-VFAYEVNDPERYGVVEFNEQKQAISI 156
Cdd:PRK14354   73 EEQLGTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAAtILTAIAENPTGYGRIIRNENGEVEKI 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2647439292 157 -EEK---PKQPKSNYAVPGLYFYDN-SVVEIAKNIAP-SPRGEYEITDVNRVYLEKG 207
Cdd:PRK14354  153 vEQKdatEEEKQIKEINTGTYCFDNkALFEALKKISNdNAQGEYYLTDVIEILKNEG 209
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 6.34e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 49.36  E-value: 6.34e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2647439292   4 IILAGGSGTRLypiTKGISKQLMPVYDKPMIYYPLSVLMLAG-IKEILFITTPQDQDQFKRLL 65
Cdd:PRK00155    7 IIPAAGKGSRM---GADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-232 6.93e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 49.87  E-value: 6.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   1 MKGIILAGGSGTRLYPITKGISKQLMPVYDK-PMIYYPLSVLMLAGIKEILFITtpqdqdQFKRLL-----GDGS----- 69
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT------QYQPLElnnhiGIGSpwdld 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  70 EIGCSFS----YEVQHEPN---GLAQAFVIGEKFIG--NDKVCLIL-GDNIfYGAGFSKLVQsFNDVNGA----AVFAYE 135
Cdd:PRK05293   78 RINGGVTilppYSESEGGKwykGTAHAIYQNIDYIDqyDPEYVLILsGDHI-YKMDYDKMLD-YHKEKEAdvtiAVIEVP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 136 VNDPERYGVVEFNEQKQAISIEEKPKQPKSNYAVPGLYFY---------------DNSVVEIAKNIAPSprgeyeitdvn 200
Cdd:PRK05293  156 WEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIPL----------- 224

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2647439292 201 rvYLEKGTLQVGIMNRGTaWLDTGTFDSFADA 232
Cdd:PRK05293  225 --YLEEGEKLYAYPFKGY-WKDVGTIESLWEA 253
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-70 1.22e-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: 1.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2647439292   4 IILAGGSGTRLypiTKGISKQLMPVYDKPMIYYPLSVLM-LAGIKEILFITTPQDQDQFKRLLGDGSE 70
Cdd:cd02516     4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-207 2.51e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.20  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLypiTKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQdQDQFKRLLGDGSEIGCSfsyeVQHEP 83
Cdd:PRK14355    7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQ-AEKVREHFAGDGDVSFA----LQEEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  84 --NGLAQAFVIGEKFIGNDKVCLILGDNIFYGAGFSKLVQSFNDVNGAA--VFAYEVNDPERYGVVEFNEQKQAISI-EE 158
Cdd:PRK14355   79 lgTGHAVACAAPALDGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAAvtVLTARLENPFGYGRIVRDADGRVLRIvEE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2647439292 159 K---PKQPKSNYAVPGLYFYDNSVVEIA-KNIA-PSPRGEYEITDVNRVYLEKG 207
Cdd:PRK14355  159 KdatPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEG 212
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-56 3.24e-06

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 46.77  E-value: 3.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2647439292   3 GIILAGGSGTRLYPITKGISKQLMPV---YDkpMIYYPLSVLMLAGIKEIlFITTPQ 56
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNV-GVLTQY 54
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-70 4.05e-05

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: 44.17  E-value: 4.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2647439292   3 GIILAGG--SGTRLYPITKGISKQLMPVYDKPMIYYPLSVL-MLAGIKEILFITTPQDqDQFKRLLGDGSE 70
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPE-SVFSDFISDAQQ 70
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-159 8.17e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 43.70  E-value: 8.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLypiTKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPqDQDQFKRLLGDGSEIGCSFsyeVQHEP 83
Cdd:PRK14353    9 IILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAAAKIAPDAEIF---VQKER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  84 NGLAQAFVIGEKFI--GNDKVCLILGDNIFYGAG-FSKLVQSFNDVNGAAVFAYEVNDPERYG-VVEFNEQKQAIsIEEK 159
Cdd:PRK14353   82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAEtLARLRERLADGADVVVLGFRAADPTGYGrLIVKGGRLVAI-VEEK 160
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-34 8.76e-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: 42.95  E-value: 8.76e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2647439292   1 MKGIILAGGSGTRLYPI-TKGISKQLMPVY-DKPMI 34
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLL 36
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-232 1.10e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 43.28  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   3 GIILAGGSGTRLYPITKGISKQLMP---VYDkpMIYYPLSVLMLAGIKEILFITtpqdqdQFKrllgdgseigcSFSYeV 79
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLT------QYK-----------SHSL-D 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  80 QH-----EPNGLAQAFV--------IGEK-FIGN----------------DKVCLILGDNIfYGAGFSKLVQsFNDVNGA 129
Cdd:PRK00844   68 RHisqtwRLSGLLGNYItpvpaqqrLGKRwYLGSadaiyqslnliededpDYVVVFGADHV-YRMDPRQMVD-FHIESGA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292 130 A--VFAYEV--NDPERYGVVEFNEQKQAISIEEKPKQPKS-------NYAVPGLYFYD---------------NSVVEIA 183
Cdd:PRK00844  146 GvtVAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTtdalvdalrrdaadeDSSHDMG 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2647439292 184 KNIAPS--PRGE---YEITDvNRVylekgtlqVGIMNRGTA-WLDTGTFDSFADA 232
Cdd:PRK00844  226 GDIIPRlvERGRayvYDFST-NEV--------PGATERDRGyWRDVGTIDAYYDA 271
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-159 2.10e-04

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 42.32  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   4 IILAGGSGTRLY---PitkgisKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQdQDQFKRLLGDgseIGCSFSyeVQ 80
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHG-AEQVRAALAD---LDVEFV--LQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  81 HEPNGLAQAFVIGEKFIGNDK-VCLILgdnifYG-------AGFSKLVQSF-NDVNGAAVFAYEVNDPERYGVVEFNEQK 151
Cdd:COG1207    74 EEQLGTGHAVQQALPALPGDDgTVLVL-----YGdvpliraETLKALLAAHrAAGAAATVLTAELDDPTGYGRIVRDEDG 148


                  ....*....
gi 2647439292 152 QAISI-EEK 159
Cdd:COG1207   149 RVLRIvEEK 157
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-53 2.35e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 42.18  E-value: 2.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2647439292   3 GIILAGGSGTRLYPITKGISKQLMPVYDK-PMIYYPLSVLMLAGIKEILFIT 53
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-55 2.54e-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: 41.03  E-value: 2.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2647439292   6 LAGGSGTRLypitKGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTP 55
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-134 6.00e-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: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   3 GIILAGGSGTRLypitkGISKQLMPVYDKPMIYYPLSVLMLAGIKEILFITTPQDQDQFKRLLGDGSEIGCsfsyeVQHE 82
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVI-----NPDW 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2647439292  83 PNGLAQAFVIGEKFIGND-KVCLI-LGDNIFYGAG-FSKLVQSFNDVNGAAVFAY 134
Cdd:cd04182    73 EEGMSSSLAAGLEALPADaDAVLIlLADQPLVTAEtLRALIDAFREDGAGIVAPV 127
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-49 7.54e-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: 39.90  E-value: 7.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2647439292   3 GIILAGGSGTRLYPITKGISKQLMPVYDKPMIYYPLSVLMLAGIKEI 49
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEV 49
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-161 9.32e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.22  E-value: 9.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292   3 GIILAGGSGTRLYPITKGISKQLMPV---YDkpMIYYPLSVLMLAGIKEIlFITTpqdqdQFK-----RLL------GDG 68
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKI-YVLT-----QFNsaslnRHLsraynfGNG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2647439292  69 SEIGCSF-----SYEVQHEPN---GLAQA-----FVIGEKFIGNDKVCLIL-GDNIfYGAGFSKLVQSFNDVNG----AA 130
Cdd:PLN02241   78 GNFGDGFvevlaATQTPGEKGwfqGTADAvrqflWLFEDAKNKNVEEVLILsGDHL-YRMDYMDFVQKHRESGAditiAC 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2647439292 131 VFAYEVNDPeRYGVVEFNEQKQAISIEEKPK 161
Cdd:PLN02241  157 LPVDESRAS-DFGLMKIDDTGRIIEFSEKPK 186
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-34 1.19e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.05  E-value: 1.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2647439292   1 MKGIILAGGSGTRLYPI-TKGISKQLMPVY-DKPMI 34
Cdd:COG0836     3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLL 38
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-41 1.74e-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: 38.63  E-value: 1.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2647439292   1 MKGIILAGGSGTRLypitkGISKQLMPVYDKPMIYYPLSVL 41
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERL 40
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-67 1.80e-03

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 38.60  E-value: 1.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2647439292   3 GIILAGGSGTRLypitkGISKQLMPVYDKPMIYYPLSVLMLAGIKEILfITTPQDQDQFKRLLGD 67
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVV-VVLGADAEEVAAALAG 64
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-58 2.12e-03

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: 37.94  E-value: 2.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2647439292   3 GIILAGGSGTRLypitkGISKQLMPVYDKPMIYYplSVLMLAGIKEILFITTPQDQ 58
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLER--VLERLRPAGDEVVVVANDEE 49
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-64 7.82e-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: 36.40  E-value: 7.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2647439292   1 MKGIILAGGSGTRLypitkGISKQLMPVYDKPMIYYPLSvlMLAGIKEILFITTPQDQDQFKRL 64
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH