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Conserved domains on  [gi|516449019|ref|WP_017837931|]
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glucose-1-phosphate thymidylyltransferase RfbA [Dietzia sp. UCD-THP]

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];
1-291 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 518.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  81 AAPEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEK 159
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGAtIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 160 PQNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTI 239
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516449019 240 EDRQGLKIGCPEEVAWRMGYLDDDELTARAHDLAKSGYGAYLLDVLRREKGR 291
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRAR 292
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-291 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 518.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  81 AAPEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEK 159
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGAtIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 160 PQNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTI 239
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516449019 240 EDRQGLKIGCPEEVAWRMGYLDDDELTARAHDLAKSGYGAYLLDVLRREKGR 291
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRAR 292
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-286 1.17e-176

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


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 488.83  E-value: 1.17e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019    2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQA 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   82 APEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEKP 160
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGAtVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  161 QNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTIE 240
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 516449019  241 DRQGLKIGCPEEVAWRMGYLDDDELTARAHDLAKSGYGAYLLDVLR 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-239 3.12e-150

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: 420.06  E-value: 3.12e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  81 AAPEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEK 159
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGAtVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 160 PQNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTI 239
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-286 2.06e-125

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 359.37  E-value: 2.06e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQA 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  82 APEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEKP 160
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGAtVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 161 QNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTIE 240
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 516449019 241 DRQGLKIGCPEEVAWRMGYLDDDELTARAHDLAKSGYGAYLLDVLR 286
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-236 2.27e-89

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: 266.04  E-value: 2.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019    2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDK-PMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   81 AAPEGLAQAFVLGADHIGDEAV-ALILGDNIFYGPGMGNQLRRFADLDGGA---VFAYRVSNPGDYGVIDFDSDGRAISL 156
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADAtvtFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  157 EEKPQNP-SSDFVVPGLYFYSADVVE-VARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGN 234
Cdd:pfam00483 161 VEKPKLPkASNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 516449019  235 YV 236
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-291 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 518.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  81 AAPEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEK 159
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGAtIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 160 PQNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTI 239
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516449019 240 EDRQGLKIGCPEEVAWRMGYLDDDELTARAHDLAKSGYGAYLLDVLRREKGR 291
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRAR 292
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-286 1.17e-176

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


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 488.83  E-value: 1.17e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019    2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQA 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   82 APEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEKP 160
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGAtVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  161 QNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTIE 240
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 516449019  241 DRQGLKIGCPEEVAWRMGYLDDDELTARAHDLAKSGYGAYLLDVLR 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-239 3.12e-150

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: 420.06  E-value: 3.12e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  81 AAPEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEK 159
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGAtVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 160 PQNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTI 239
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-286 2.06e-125

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 359.37  E-value: 2.06e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQA 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  82 APEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA-VFAYRVSNPGDYGVIDFDSDGRAISLEEKP 160
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGAtVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 161 QNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGNYVRTIE 240
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 516449019 241 DRQGLKIGCPEEVAWRMGYLDDDELTARAHDLAKSGYGAYLLDVLR 286
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-236 2.27e-89

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: 266.04  E-value: 2.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019    2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDK-PMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   81 AAPEGLAQAFVLGADHIGDEAV-ALILGDNIFYGPGMGNQLRRFADLDGGA---VFAYRVSNPGDYGVIDFDSDGRAISL 156
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADAtvtFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  157 EEKPQNP-SSDFVVPGLYFYSADVVE-VARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTAWLDTGTHDSLLDAGN 234
Cdd:pfam00483 161 VEKPKLPkASNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 516449019  235 YV 236
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-232 5.71e-66

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: 206.27  E-value: 5.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEdAPQFRRLLGDGSQFGITLSYVEQ 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  81 AAPEGLAQAFVLGADHIGDEAVALILGDNIFyGPGMGNQLRRFADLDGGAVFAY-RVSNPGDYGVIDFDsDGRAISLEEK 159
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLI-QEGISPLVRDFLEEDADASILLaEVEDPRRFGVAVVD-DGRIVRLVEK 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516449019 160 PQNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRlqvEVLPRGTA--WLDTGTHDSLLDA 232
Cdd:cd04189  158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGR---RVGYSIVTgwWKDTGTPEDLLEA 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-224 7.83e-60

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 189.71  E-value: 7.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   3 GIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEdAPQFRRLLGDGSQFGITLSYVEQAA 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYL-GEQIEEYFGDGSKFGVNIEYVVQEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  83 PEGLAQAFVLGADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGAVFAYRVSNPGDYGVIDFDSDGRAISLEEKPQN 162
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPTL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516449019 163 PSSDFVVPGLYFYSADVVEVARslEKSPRGEYEITDVNRHYLEEGRLQVEVLPrgTAWLDTG 224
Cdd:cd04181  160 PESNLANAGIYIFEPEILDYIP--EILPRGEDELTDAIPLLIEEGKVYGYPVD--GYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-232 6.40e-59

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: 191.85  E-value: 6.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019    2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLLGDGSQFGITLSYVEQA 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   82 APEGLAQAFVLGADHIGDEAVALILGDNIFYGpGMGNQLRRFADLDGGAVFAY-RVSNPGDYGVIDFDSDGRAISLEEKP 160
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLtKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516449019  161 QNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGTaWLDTGTHDSLLDA 232
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-242 5.32e-55

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: 182.79  E-value: 5.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019    1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDApQFRRLLGDGSQFGITLSYVEQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKE-KVREYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   81 AAPEGLAQAFVLGADHIGDEaVALILGDNIFYGPGmgnqLRRFADLDGGAVFAYRVSNPGDYGVIDFDsDGRAISLEEKP 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDDE-FLVLNGDVLLDSDL----LERLIRAEAPAIAVVEVDDPSDYGVVETD-GGRVTGIVEKP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  161 QNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLPRGtaWLDTGTHDSLLDAGNYV-RTI 239
Cdd:TIGR03992 154 ENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEALlDNL 231

                  ...
gi 516449019  240 EDR 242
Cdd:TIGR03992 232 EPR 234
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-232 2.03e-44

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: 150.69  E-value: 2.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDIlLITTPEDAPQFRRLLGDGSQFGITLSYVEQA 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  82 APEGLAQAFVLGADHIGDEAVALILGDnIFYGPGMGNQLRRFADLDGGAVFA-YRVSNPGDYGVIDFDSDGRAISLEEKP 160
Cdd:COG1208   80 EPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLAlVPVPDPSRYGVVELDGDGRVTRFVEKP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516449019 161 QNPSSDFVVPGLYFYSADVvevarsLEKSPRGE-YEITDVNRHYLEEGRLQVEVLPrgTAWLDTGTHDSLLDA 232
Cdd:COG1208  159 EEPPSNLINAGIYVLEPEI------FDYIPEGEpFDLEDLLPRLIAEGRVYGYVHD--GYWLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-232 2.22e-25

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: 101.84  E-value: 2.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTP-----EDapQFRR-------LLGDG 68
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiED--HFDRsyeleetLEKKG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  69 SQ----------FGITLSYVEQAAPEGLAQAFVLGADHIGDEAVALILGDNIFYG--PGMGNQLRRFADLdGGAVFAYRV 136
Cdd:cd02541   79 KTdlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSkePCLKQLIEAYEKT-GASVIAVEE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 137 SNPGD---YGVID-FDSDGRAISLE---EKP--QNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEG 207
Cdd:cd02541  158 VPPEDvskYGIVKgEKIDGDVFKVKglvEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEE 237
                        250       260
                 ....*....|....*....|....*
gi 516449019 208 RLQVEVLpRGTaWLDTGTHDSLLDA 232
Cdd:cd02541  238 PVYAYVF-EGK-RYDCGNKLGYLKA 260
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-232 4.76e-23

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: 94.12  E-value: 4.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDIlLITTPEDAPQFRRLLGDGSQFGITLSYVEQAAP 83
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAFVLGADHIgDEAVALILGD---NIFYgpgmgNQLRRFADLDGG----AVFAYRVSNPgdYGVIDFDsDGRAISL 156
Cdd:cd06426   81 LGTAGALSLLPEKP-TDPFLVMNGDiltNLNY-----EHLLDFHKENNAdatvCVREYEVQVP--YGVVETE-GGRITSI 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516449019 157 EEKPQNPSsdFVVPGLYFYSADVvevarsLEKSPRGEY-EITDVNRHYLEEGRlQVEVLPRGTAWLDTGTHDSLLDA 232
Cdd:cd06426  152 EEKPTHSF--LVNAGIYVLEPEV------LDLIPKNEFfDMPDLIEKLIKEGK-KVGVFPIHEYWLDIGRPEDYEKA 219
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-181 2.37e-22

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 92.62  E-value: 2.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEdAPQFRRLLGDGSQFGITLSYVEQAAP 83
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYL-AEQIEEYFGDGYRGGIRIYYVIEPEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAFVLGADHIGDEAVALILGDNIF---YgpgmgNQLRRFADLDG--GAVFAYRVSNPGDYGVIDFDSDGRAISLEE 158
Cdd:cd06915   81 LGTGGAIKNALPKLPEDQFLVLNGDTYFdvdL-----LALLAALRASGadATMALRRVPDASRYGNVTVDGDGRVIAFVE 155
                        170       180
                 ....*....|....*....|...
gi 516449019 159 KPQNPSSDFVVPGLYFYSADVVE 181
Cdd:cd06915  156 KGPGAAPGLINGGVYLLRKEILA 178
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-232 6.83e-21

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: 88.40  E-value: 6.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDIlLITTPEDAPQFRRLLGD-GSQFGITLSYVEQ 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTHHLADQIEAHLGDsRFGLRITISDEPD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  81 AAPE---GLAQAfvlgADHIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGAVFAYRVSNPGDYGVIDF--DSDGRais 155
Cdd:cd06422   80 ELLEtggGIKKA----LPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDADGR--- 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516449019 156 LEEKPQNPSSDFVVPGLYFYSADVvevarsLEKSPRGEYEITDVNRHYLEEGRLQVEVLpRGTaWLDTGTHDSLLDA 232
Cdd:cd06422  153 LRRGGGGAVAPFTFTGIQILSPEL------FAGIPPGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-225 1.16e-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: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITT--PEDAPQFRRLLGDgsQFGITLSYV 78
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEYEK--KLGIKITFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  79 EQAAPEGLAQAFVLGADHIGDEAVALIL--GDNIFYGPgmgnqlrrFADLDG--------GAVFAYRVSNPGDYGVIDFD 148
Cdd:cd06425   79 IETEPLGTAGPLALARDLLGDDDEPFFVlnSDVICDFP--------LAELLDfhkkhgaeGTILVTKVEDPSKYGVVVHD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516449019 149 SD-GRAISLEEKPQNPSSDFVVPGLYFYSADVvevarsLEKSPRGEYEI-TDVNRHYLEEGRLQVEVLPrgTAWLDTGT 225
Cdd:cd06425  151 ENtGRIERFVEKPKVFVGNKINAGIYILNPSV------LDRIPLRPTSIeKEIFPKMASEGQLYAYELP--GFWMDIGQ 221
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 1.97e-18

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 83.40  E-value: 1.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPE------------------DAPQFR 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASknavenhfdtsyelesllEQRVKR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  63 RLLGDGSQF---GITLSYVEQAAPEGLAQAFVLGADHIGDEAVALILGDnIFYGPGMGNQLR--------RFADLDGGAV 131
Cdd:PRK10122  84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPD-VVIDDASADPLRynlaamiaRFNETGRSQV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 132 FAYRVsnPGD---YGVID----FDSDG---RAISLEEKPQNP---SSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITD 198
Cdd:PRK10122 163 LAKRM--PGDlseYSVIQtkepLDREGkvsRIVEFIEKPDQPqtlDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-232 4.58e-18

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 82.00  E-value: 4.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTP-----ED----APQFRRLL---GD-- 67
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiEDhfdrSYELEATLeakGKee 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  68 ------GSQFGITLSYVEQAAPEGLAQAFVLGADHIGDEAVALILGDNIFYG--PGMGNQLRRFADLDGGAVFAYRVsnP 139
Cdd:COG1210   85 lleevrSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSekPCLKQMIEVYEETGGSVIAVQEV--P 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 140 GD----YGVIDF-DSDGRAISLE---EKP---QNPsSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGR 208
Cdd:COG1210  163 PEevskYGIVDGeEIEGGVYRVTglvEKPapeEAP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEP 241
                        250       260
                 ....*....|....*....|....
gi 516449019 209 LQVeVLPRGTaWLDTGTHDSLLDA 232
Cdd:COG1210  242 VYA-YEFEGK-RYDCGDKLGYLKA 263
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-198 3.93e-15

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 74.17  E-value: 3.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPED-----------------APQFRRL 64
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKnsienhfdtsfeleamlEKRVKRQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  65 LGDGSQF----GITLSYVEQAAPEGLAQAFVLGADHIGDEAVALILGDNI-------FYGPGMGNQLRRFADLDGGAVFA 133
Cdd:PRK13389  90 LLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeyesdLSQDNLAEMIRRFDETGHSQIMV 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516449019 134 YRVSNPGDYGVIDFD-------SDGRAISLEEKPQ--NPSSDFVVPGLYFYSADVVEVarsLEKSPRG---EYEITD 198
Cdd:PRK13389 170 EPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPL---LAKTPPGagdEIQLTD 243
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-65 9.35e-15

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 71.54  E-value: 9.35e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDAPQFRRLL 65
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-216 1.46e-12

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: 66.12  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   3 GIVLAGG--SGTRLRPLTVATSKQLMPVYDKPMIYYPLSTL-MLAGIHDILLITTPEDApQFRRLLGDGSQ-FGITLSYV 78
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPES-VFSDFISDAQQeFNVPIRYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  79 EQAAPEGLAQAFVLGADHI---GDEAVALILGDNI--FYGPGMGNQLRRFAdlDGGAVFAYRVS--NPGDYGVIDFD-SD 150
Cdd:cd06428   80 QEYKPLGTAGGLYHFRDQIlagNPSAFFVLNADVCcdFPLQELLEFHKKHG--ASGTILGTEASreQASNYGCIVEDpST 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516449019 151 GRAISLEEKPQNPSSDFVVPGLYFYSADVVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVE--VLPR 216
Cdd:cd06428  158 GEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEqdVLTP 225
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-58 5.48e-12

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: 63.81  E-value: 5.48e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDA 58
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQ 58
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-232 7.37e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 62.01  E-value: 7.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   3 GIVLAGGSGTRLRPLTvatskQLMPvydKPMIYY---------PLSTLMLAGIHDILLITtpedapQFR-----RLLGDG 68
Cdd:COG0448    4 AIILAGGRGSRLGPLT-----KDRA---KPAVPFggkyriidfPLSNCVNSGIRRVGVLT------QYKshslnDHIGSG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  69 S--QFGITLSYVEQAAPE----------GLAQAFVLGADHIGDEAV--ALIL-GDNIF---YgpgmgNQLRRF-----AD 125
Cdd:COG0448   70 KpwDLDRKRGGVFILPPYqqregedwyqGTADAVYQNLDFIERSDPdyVLILsGDHIYkmdY-----RQMLDFhiesgAD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 126 LdggAVFAYRVSNP--GDYGVIDFDSDGRAISLEEKPQNPSSDFVVPGLYFYSADV-VEVarsLEKS-PRGEYE-ITDVN 200
Cdd:COG0448  145 I---TVACIEVPREeaSRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVlIEL---LEEDaPNSSHDfGKDII 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 516449019 201 RHYLEEGRLQvevlprgtA------WLDTGTHDSLLDA 232
Cdd:COG0448  219 PRLLDRGKVY--------AyefdgyWRDVGTIDSYYEA 248
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-208 6.41e-10

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 59.37  E-value: 6.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPLTVatsKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTpEDAPQFRRLLGDgsQFGITLSYVEQAAP 83
Cdd:PRK14355   7 IILAAGKGTRMKSDLV---KVMHPLAGRPMVSWPVAAAREAGAGRIVLVVG-HQAEKVREHFAG--DGDVSFALQEEQLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAFVLGADHIGDEAVALILGDNIFYGPGmgnQLRRFADLDG--GA---VFAYRVSNPGDYGVIDFDSDGRAISL-E 157
Cdd:PRK14355  81 TGHAVACAAPALDGFSGTVLILCGDVPLLRAE---TLQGMLAAHRatGAavtVLTARLENPFGYGRIVRDADGRVLRIvE 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516449019 158 EK---PQNPSSDFVVPGLYFYSADVVEVARSLEKS--PRGEYEITDVNRHYLEEGR 208
Cdd:PRK14355 158 EKdatPEERSIREVNSGIYCVEAAFLFDAIGRLGNdnAQGEYYLTDIVAMAAAEGL 213
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-215 8.25e-10

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: 57.63  E-value: 8.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEDApQFRRLLGDgsQFGITLSYVEQAAP 83
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKE-QIEELLKK--YPNIKFVYNPDYAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAFVLGADHIGDEAVaLILGDNIFYgPGMGNQLRRFAdlDGGAVFAYRVSNP-GDYGVIDFDSDGRAISLEEKPQN 162
Cdd:cd02523   79 TNNIYSLYLARDFLDEDFL-LLEGDVVFD-PSILERLLSSP--ADNAILVDKKTKEwEDEYVKDLDDAGVLLGIISKAKN 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 163 PSSD---FVvpGLYFYSAD----VVEVARSLEKSPRGEYEITDVNRHYLEEGRLQVEVLP 215
Cdd:cd02523  155 LEEIqgeYV--GISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS 212
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-222 1.21e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 57.17  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   2 KGIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEdAPQFRRLLGdgsQFGITLSYVEQA 81
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYK-AELIEEALA---RPGPDVTFVYNP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  82 APE--GLAQAFVLGADHIGDEAVaLILGDnIFYGPGMgnqLRRFADLDGGAVFA--YRVSNPGDYGV-IDFDSDGRAISL 156
Cdd:COG1213   77 DYDetNNIYSLWLAREALDEDFL-LLNGD-VVFDPAI---LKRLLASDGDIVLLvdRKWEKPLDEEVkVRVDEDGRIVEI 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516449019 157 EEKPQNPSSDFVVPGLYFYSAD----VVEVARSLEKSPRGEYEITDVNRHYLEEGrLQVEVLP-RGTAWLD 222
Cdd:COG1213  152 GKKLPPEEADGEYIGIFKFSAEgaaaLREALEALIDEGGPNLYYEDALQELIDEG-GPVKAVDiGGLPWVE 221
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
4-207 2.91e-09

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 57.30  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPltvATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTpEDAPQFRRLLgdgSQFGITlsYVEQAAP 83
Cdd:PRK14358  11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTG-HGAEQVEAAL---QGSGVA--FARQEQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAFVLGAD--HIGDEAVALILGDNIFYGPGMGNQLRRFADLDGGA--VFAYRVSNPGDYGVIDFDSDGRAISL-EE 158
Cdd:PRK14358  82 LGTGDAFLSGASalTEGDADILVLYGDTPLLRPDTLRALVADHRAQGSAmtILTGELPDATGYGRIVRGADGAVERIvEQ 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516449019 159 KPQNPSSDFV---VPGLYFYSADVVEVARSL-EKSPRGEYEITDVNRHYLEEG 207
Cdd:PRK14358 162 KDATDAEKAIgefNSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-232 2.93e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 57.14  E-value: 2.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   3 GIVLAGGSGTRLRPLTVATSKQLMP---VYDkpMIYYPLSTLMLAGIHDILLIT-------------------------T 54
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLTqykshsldrhisqtwrlsgllgnyiT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  55 PEDApQFRrlLG----DGSQFGI--TLSYVEQAAPEglaQAFVLGADHIGDEAVALILGDNIfygpgmgnqlrrfadlDG 128
Cdd:PRK00844  86 PVPA-QQR--LGkrwyLGSADAIyqSLNLIEDEDPD---YVVVFGADHVYRMDPRQMVDFHI----------------ES 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 129 GA---VFAYRV--SNPGDYGVIDFDSDGRAISLEEKPQNP-----SSD--FVVPGLYFYSADV-VEVARSLEKSPRGEye 195
Cdd:PRK00844 144 GAgvtVAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPpglpdDPDeaLASMGNYVFTTDAlVDALRRDAADEDSS-- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516449019 196 iTDVNRH----YLEEGRLQV-----EVLPRGTA-----WLDTGTHDSLLDA 232
Cdd:PRK00844 222 -HDMGGDiiprLVERGRAYVydfstNEVPGATErdrgyWRDVGTIDAYYDA 271
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-208 1.64e-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: 54.06  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPltvATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLItTPEDAPQFRRLLGDGSqfgitLSYVEQAAP 83
Cdd:cd02540    2 VILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALANPN-----VEFVLQEEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAfVLGA-DHI-GDEAVALIL-GDNIFYGPgmgNQLRRFADL-----DGGAVFAYRVSNPGDYGVIDFDSDGR--A 153
Cdd:cd02540   73 LGTGHA-VKQAlPALkDFEGDVLVLyGDVPLITP---ETLQRLLEAhreagADVTVLTAELEDPTGYGRIIRDGNGKvlR 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 154 IsLEEK---PQNPSSDFVVPGLY-FYSADVVEVARSLEKSP-RGEYEITDVNRHYLEEGR 208
Cdd:cd02540  149 I-VEEKdatEEEKAIREVNAGIYaFDAEFLFEALPKLTNNNaQGEYYLTDIIALAVADGL 207
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-139 5.32e-08

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: 51.79  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   3 GIVLAGGSGTRLRpltvaTSKQLMPVYDKPMIYYPLSTLMLAGIHDILLItTPEDAPQFRRLLgdgSQFGITLSYVEQAA 82
Cdd:cd04182    3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVV-LGAEADAVRAAL---AGLPVVVVINPDWE 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516449019  83 pEGLAQAFVLGADHIGD--EAVALILGDNIFYGPGMGNQLRRFADLDGG----AVFAYRVSNP 139
Cdd:cd04182   74 -EGMSSSLAAGLEALPAdaDAVLILLADQPLVTAETLRALIDAFREDGAgivaPVYQGRRGHP 135
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-67 2.22e-07

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: 50.51  E-value: 2.22e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516449019   4 IVLAGGSGTRLRpltVATSKQLMPVYDKPMIYYPLSTLMLAG-IHDILLITTPEDAPQFRRLLGD 67
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-108 4.20e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.39  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   3 GIVLAGGSGTRL-RPltvatsKQLMPVYDKPMIYYPLSTLMLAGIHDILLItTPEDAPQFRRLLgdgSQFGITLSYVEQA 81
Cdd:COG2068    6 AIILAAGASSRMgRP------KLLLPLGGKPLLERAVEAALAAGLDPVVVV-LGADAEEVAAAL---AGLGVRVVVNPDW 75
                         90       100
                 ....*....|....*....|....*....
gi 516449019  82 ApEGLAQAFVLGADHIGD--EAVALILGD 108
Cdd:COG2068   76 E-EGMSSSLRAGLAALPAdaDAVLVLLGD 103
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 1.36e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 48.21  E-value: 1.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516449019   4 IVLAGGSGTRLRpltVATSKQLMPVYDKPMIYYPLSTLMLAG-IHDILLITTPEDAPQFRRLL 65
Cdd:PRK00155   7 IIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-232 1.46e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 49.10  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPLTVATSKQLMPVYDK-PMIYYPLSTLMLAGIHDILLITtpedapQFRRLL-----GDGSQF--- 71
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT------QYQPLElnnhiGIGSPWdld 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  72 ----GITL--SYVEQAAP---EGLAQA------FVlgaDHIGDEAVaLIL-GDNIF---YGPGMGNQLRRFADLDGgAVF 132
Cdd:PRK05293  78 ringGVTIlpPYSESEGGkwyKGTAHAiyqnidYI---DQYDPEYV-LILsGDHIYkmdYDKMLDYHKEKEADVTI-AVI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019 133 AYRVSNPGDYGVIDFDSDGRAISLEEKPQNPSSDFVVPGLYFYSADVV-EVARSLEKSPRGEYEI-TDVNRHYLEEGRlQ 210
Cdd:PRK05293 153 EVPWEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLkEYLIEDEKNPNSSHDFgKNVIPLYLEEGE-K 231
                        250       260
                 ....*....|....*....|..
gi 516449019 211 VEVLPRGTAWLDTGTHDSLLDA 232
Cdd:PRK05293 232 LYAYPFKGYWKDVGTIESLWEA 253
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-143 1.94e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 48.70  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPltvATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPeDAPQFRRLLgdgSQFGITLSYVEQAAP 83
Cdd:PRK14353   9 IILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAA---AKIAPDAEIFVQKER 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516449019  84 EGLAQAFVLGADHI--GDEAVALILGDNIFYGPG----MGNQLRRFADLdggAVFAYRVSNPGDYG 143
Cdd:PRK14353  82 LGTAHAVLAAREALagGYGDVLVLYGDTPLITAEtlarLRERLADGADV---VVLGFRAADPTGYG 144
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-138 4.87e-06

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: 45.65  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019    3 GIVLAGGSGTRLRpltvaTSKQLMPVYDKPMIYYPLSTLMLAGiHDILLITTPEDAPQFRRLLGdgsqfgitLSYVEQAA 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 516449019   83 P-EGLAQAFVLGADHIGD-EAVALILGDNIFYGPGMGNQLRRFADLDGGAVFAYRVSN 138
Cdd:pfam12804  67 PgQGPLAGLLAALRAAPGaDAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDG 124
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-199 1.24e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 46.29  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPltvATSKQLMPVYDKPMIYYPLST---------LMLAGIHDILLITTPEDAPQFrrllgdgsqf 71
Cdd:PRK14357   1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTakkvaqkvgVVLGHEAELVKKLLPEWVKIF---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  72 gitlsyvEQAAPEGLAQAFVLGADHIGDEAVALIL-GDNIFYGPGMGNQLRRFADLDGG--AVFAYRVSNPGDYGVIDFD 148
Cdd:PRK14357  68 -------LQEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLIEEHNRKGAdvTILVADLEDPTGYGRIIRD 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516449019 149 SDGRAIsLEEKPQNPSSDFVV---PGLYFYSAD-VVEVARSLE-KSPRGEYEITDV 199
Cdd:PRK14357 141 GGKYRI-VEDKDAPEEEKKIKeinTGIYVFSGDfLLEVLPKIKnENAKGEYYLTDA 195
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-68 1.31e-05

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: 45.21  E-value: 1.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516449019   4 IVLAGGSGTRLRpltVATSKQLMPVYDKPMIYYPLSTLM-LAGIHDILLITTPEDAPQFRRLLGDG 68
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-159 1.31e-05

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 46.17  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPltvATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEdAPQFRRLLGDgsqfgITLSYVEQAAP 83
Cdd:COG1207    6 VILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHG-AEQVRAALAD-----LDVEFVLQEEQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAFVLGADHI-GDEAVALILgdnifYG--PGMGNQ-LRRFADL-----DGGAVFAYRVSNPGDYGVIDFDSDGR-- 152
Cdd:COG1207   77 LGTGHAVQQALPALpGDDGTVLVL-----YGdvPLIRAEtLKALLAAhraagAAATVLTAELDDPTGYGRIVRDEDGRvl 151

                 ....*..
gi 516449019 153 AIsLEEK 159
Cdd:COG1207  152 RI-VEEK 157
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-53 4.11e-05

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: 43.69  E-value: 4.11e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516449019   3 GIVLAGGSGTRLRPLTVATSKQLMPV---YDkpMIYYPLSTLMLAGIHDILLIT 53
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT 52
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-101 1.66e-04

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: 42.18  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   1 MKGIVLAGGSGTRLRPL-TVATSKQLMPVY-DKPMIYYPLSTLM-LAGIHDILLITTPEDAPQFRRLLGDGSQ------- 70
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVVTNEEYRFLVREQLPEGLPeeniile 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 516449019  71 ---------FGITLSYVEQAAPEGLaqAFVLGADH-IGDEA 101
Cdd:cd02509   81 pegrntapaIALAALYLAKRDPDAV--LLVLPSDHlIEDVE 119
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-65 1.82e-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: 41.41  E-value: 1.82e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   6 LAGGSGTRLRPltvaTSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPeDAPQFRRLL 65
Cdd:COG2266    1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREYL 55
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
3-161 3.15e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 41.79  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   3 GIVLAGGSGTRLRPLTVATSKQLMPVYDK-PMIYYPLSTLMLAGIHDILLITtpedapQF-----RRLLGDGSQF-GITL 75
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT------QFnsaslNRHISQTYNFdGFSG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  76 SYVE----QAAPE------GLAQA----FVLGADHIGDEavALILGdnifygpgmGNQLRR--FADL-----DGGA---- 130
Cdd:PRK02862  80 GFVEvlaaQQTPEnpswfqGTADAvrkyLWHFQEWDVDE--YLILS---------GDQLYRmdYRLFvqhhrETGAditl 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 516449019 131 ----VFAYRVSnpgDYGVIDFDSDGRAISLEEKPQ 161
Cdd:PRK02862 149 avlpVDEKDAS---GFGLMKTDDDGRITEFSEKPK 180
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-207 5.70e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019   4 IVLAGGSGTRLRPltvATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITTPEdAPQFRRLLGDGSQfgitlsYVEQAAP 83
Cdd:PRK14354   6 IILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHG-AEEVKEVLGDRSE------FALQEEQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516449019  84 EGLAQAFVLGADHIGDEA--VALILGDNIFYgpgMGNQLRRFAD--LDGGA---VFAYRVSNPGDYGVIDFDSDGRAISL 156
Cdd:PRK14354  76 LGTGHAVMQAEEFLADKEgtTLVICGDTPLI---TAETLKNLIDfhEEHKAaatILTAIAENPTGYGRIIRNENGEVEKI 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516449019 157 -EEKPQNPSSDFVV---PGLYFYsaDVVEVARSLEK----SPRGEYEITDVNRHYLEEG 207
Cdd:PRK14354 153 vEQKDATEEEKQIKeinTGTYCF--DNKALFEALKKisndNAQGEYYLTDVIEILKNEG 209
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-54 3.79e-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: 37.97  E-value: 3.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516449019   3 GIVLAGGSGTRLRPLTVATSKQLMPVYDKPMIYYPLSTLMLAGIHDILLITT 54
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCC 54
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 4.18e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 38.12  E-value: 4.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516449019   1 MKGIVLAGGSGTRLRPL-TVATSKQLMPVY-DKPMIYyplSTLM----LAGIHDILLIT 53
Cdd:COG0836    3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLLQ---QTVErlagLVPPENILVVT 58
 
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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