NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1718626009|ref|WP_145022123|]
View 

MULTISPECIES: glucose-1-phosphate thymidylyltransferase RfbA [unclassified Paenibacillus]

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];
1-289 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 541.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 161 PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1718626009 241 EKRQSLKVACLEEISYSKGYINREQLTLLAERMSKNAYGAYLMQLAAGN 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 541.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 161 PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1718626009 241 EKRQSLKVACLEEISYSKGYINREQLTLLAERMSKNAYGAYLMQLAAGN 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-286 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: 520.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQE 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  82 QPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 162 AEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1718626009 242 KRQSLKVACLEEISYSKGYINREQLTLLAERMSKNAYGAYLMQLA 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-240 8.91e-171

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: 472.06  E-value: 8.91e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 161 PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-288 5.42e-149

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 419.08  E-value: 5.42e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  82 QPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 162 AEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1718626009 242 KRQSLKVACLEEISYSKGYINREQLTLLAERMSKNAYGAYLMQLAAG 288
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKG 291
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 8.70e-98

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: 287.61  E-value: 8.70e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDK-PMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSV-ALILGDNLFHGHGLTEMLQTAVQREQ--GATIFGYHVQDPGRFGVVEFDADGRAVSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 158 QEKPAEPR-SNYAVTGLYFYDRNVVDY-AKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 1718626009 236 YIE 238
Cdd:pfam00483 241 FLL 243
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 541.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 161 PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1718626009 241 EKRQSLKVACLEEISYSKGYINREQLTLLAERMSKNAYGAYLMQLAAGN 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-286 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: 520.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQE 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  82 QPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 162 AEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1718626009 242 KRQSLKVACLEEISYSKGYINREQLTLLAERMSKNAYGAYLMQLA 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-240 8.91e-171

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: 472.06  E-value: 8.91e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 161 PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-288 5.42e-149

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 419.08  E-value: 5.42e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  82 QPNGLAESFIIGEEFIGGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 162 AEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQYIETIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1718626009 242 KRQSLKVACLEEISYSKGYINREQLTLLAERMSKNAYGAYLMQLAAG 288
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKG 291
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-238 8.70e-98

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: 287.61  E-value: 8.70e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDK-PMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSV-ALILGDNLFHGHGLTEMLQTAVQREQ--GATIFGYHVQDPGRFGVVEFDADGRAVSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 158 QEKPAEPR-SNYAVTGLYFYDRNVVDY-AKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFSWFDSGTHESLLEASQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ...
gi 1718626009 236 YIE 238
Cdd:pfam00483 241 FLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-237 1.14e-72

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 223.21  E-value: 1.14e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDtPRFEELFGTGEQLGIRLSYAVQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGGDSVALILGDNLFHGhGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDaDGRAVSIQEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVEK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 161 PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITD-INRMyLERGQlrvEILGRGFS--WFDSGTHESLLEASQYI 237
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDaIQWL-IDRGR---RVGYSIVTgwWKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-225 4.96e-65

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: 203.20  E-value: 4.96e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDtPRFEELFGTGEQLGIRLSYAVQEQ 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  83 PNGLAESFIIGEEFIGGDSVALILGDNLFHGhGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKPA 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718626009 163 EPRSNYAVTGLYFYDRNVVDYAKQIVPsdRGELEITDINRMYLERGQLRVeILGRGFsWFDSG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-243 7.60e-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: 7.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAVQE 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  82 QPNGLAESFIIGEEFIGGDSVALILGDNLFHGhGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 162 AEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGFsWFDSGTHESLLEASQYI-ETI 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIlDEV 238

                  ...
gi 1718626009 241 EKR 243
Cdd:TIGR01208 239 ERE 241
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-238 2.24e-51

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: 168.79  E-value: 2.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDIlIISTPQDTPRFEELFGTGEQLGIRLSYAVQE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  82 QPNGLAESFIIGEEFIGGDSVALILGDNLFhGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKP 161
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEPFLVLNGDILT-DLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEKP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718626009 162 AEPRSNYAVTGLYFYDRNVVDYakqiVPSDRgELEITDINRMYLERGQLRVEILgRGFsWFDSGTHESLLEASQYIE 238
Cdd:COG1208   159 EEPPSNLINAGIYVLEPEIFDY----IPEGE-PFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANALLL 228
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-237 5.25e-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: 167.39  E-value: 5.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTpRFEELFGTGEQLGIRLSYAVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKE-KVREYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFIIGEEFIGgDSVALILGDNLFHGHGLTEMLqtavqREQGATIFGYHVQDPGRFGVVEFDaDGRAVSIQEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD-DEFLVLNGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETD-GGRVTGIVEK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718626009 161 PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGRGfsWFDSGTHESLLEASQYI 237
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANEAL 227
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-234 1.60e-30

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


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 115.32  E-value: 1.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQ--------DTPRF--EELFGTGEQ 70
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfDRSYEleETLEKKGKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  71 ----------LGIRLSYAVQEQPNGLAESFIIGEEFIGGDSVALILGDNLFHGH--GLTEMLQtaVQREQGATIFGyhVQ 138
Cdd:cd02541    81 dlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepCLKQLIE--AYEKTGASVIA--VE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 139 -----DPGRFGVVE-FDADGRAVSIQ---EKPA--EPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITD-INRMYLE 206
Cdd:cd02541   157 evppeDVSKYGIVKgEKIDGDVFKVKglvEKPKpeEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDaIAKLLEE 236
                         250       260
                  ....*....|....*....|....*...
gi 1718626009 207 RGQLRVEILGRgfsWFDSGTHESLLEAS 234
Cdd:cd02541   237 EPVYAYVFEGK---RYDCGNKLGYLKAT 261
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-233 1.80e-25

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: 100.71  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDIlIISTPQDTPRFEELFGTGEQLGIRLSYAVQEQP 83
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  84 NGLAESFIIGEEFIGGDSVALILGDNLFHGhGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQEKPAE 163
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718626009 164 PRSNYAVTGLYFYDRNVVDYAKQIVPSDRgeleiTDINRMYLERGQLRVEIlgrGFSWF-DSGTHESLLEA 233
Cdd:cd06915   160 AAPGLINGGVYLLRKEILAEIPADAFSLE-----ADVLPALVKRGRLYGFE---VDGYFiDIGIPEDYARA 222
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-236 2.41e-23

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: 95.36  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRD-ILIIS-TPQDTPRFEELFgtGEQLGIRLSYA 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEY--EKKLGIKITFS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  79 VQEQPNGLAESFIIGEEFIGGDSVA-LILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDAD-GRAVS 156
Cdd:cd06425    79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 157 IQEKPAEPRSNYAVTGLYFYDRNVVdyakqivpsDRGELEITDINR----MYLERGQLRVEILgRGFsWFDSGTHESLLE 232
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVL---------DRIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WMDIGQPKDFLK 227

                  ....
gi 1718626009 233 ASQY 236
Cdd:cd06425   228 GMSL 231
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 6.54e-23

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 95.48  E-value: 6.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYplSV--LMLAGIRDILIISTPQ--------DT-PRFEELF---GT 67
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRGkraiedhfDRsYELEATLeakGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  68 GEQL--------GIRLSYAVQEQPNGLAESFIIGEEFIGGDSVALILGDNLFHGH--GLTEMLQtaVQREQGATIFGyhV 137
Cdd:COG1210    83 EELLeevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkpCLKQMIE--VYEETGGSVIA--V 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 138 Q-----DPGRFGVVEFDADG----RAVSIQEKPA--EPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITD-INRMYL 205
Cdd:COG1210   159 QevppeEVSKYGIVDGEEIEggvyRVTGLVEKPApeEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDaIAALAK 238
                         250       260
                  ....*....|....*....|....*...
gi 1718626009 206 ERGQLRVEILGRgfsWFDSGTHESLLEA 233
Cdd:COG1210   239 EEPVYAYEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-233 1.00e-22

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: 93.35  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDIlIISTPQDTPRFEELFGTGEQLGIRLSYAVQEQP 83
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  84 NGLAESFIIGEEFIgGDSVALILGDnLFHGHGLTEMLQTAVQREQGATIFG--YHVQDPgrFGVVEFDaDGRAVSIQEKP 161
Cdd:cd06426    81 LGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETE-GGRITSIEEKP 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718626009 162 AEprsNYAV-TGLYFYDRNVVDYakqiVPSDRgELEITDINRMYLERGQlRV---EILGrgfSWFDSGTHESLLEA 233
Cdd:cd06426   156 TH---SFLVnAGIYVLEPEVLDL----IPKNE-FFDMPDLIEKLIKEGK-KVgvfPIHE---YWLDIGRPEDYEKA 219
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-57 1.05e-16

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 76.93  E-value: 1.05e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQD 57
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-207 3.56e-15

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 74.17  E-value: 3.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIIsTPQDTPRFEELFGTGEQLGIRLSYAVQE 81
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKNSIENHFDTSFELEAMLEKRVKR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  82 Q----------------------PNGLAESFIIGEEFIGGDSVALILGDNLFHGH-------GLTEMLQTAvqREQGAT- 131
Cdd:PRK13389   89 QlldevqsicpphvtimqvrqglAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYesdlsqdNLAEMIRRF--DETGHSq 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 132 IFGYHVQDPGRFGVVefDADGRA---------VSIQEKPA--EPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDI 200
Cdd:PRK13389  167 IMVEPVADVTAYGVV--DCKGVElapgesvpmVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244

                  ....*..
gi 1718626009 201 NRMYLER 207
Cdd:PRK13389  245 IDMLIEK 251
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-233 1.79e-14

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: 71.06  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDIlIIST---PQdtpRFEELFG-TGEQLGIRLSY 77
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlAD---QIEAHLGdSRFGLRITISD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  78 avqEQPN------GLAEsfiiGEEFIGGDSVALILGDNLFHGhGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEF--D 149
Cdd:cd06422    77 ---EPDElletggGIKK----ALPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 150 ADGRavsIQEKPAEPRSNYAVTGLYFYDRNVVDYAKQivpsdrGELEITDINRMYLERGQLRVEILgRGFsWFDSGTHES 229
Cdd:cd06422   149 ADGR---LRRGGGGAVAPFTFTGIQILSPELFAGIPP------GKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPER 217

                  ....
gi 1718626009 230 LLEA 233
Cdd:cd06422   218 LLAA 221
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-237 1.04e-13

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 69.11  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   2 KGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTpRFEELFgtgEQLGIRLSYAVQ- 80
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAE-LIEEAL---ARPGPDVTFVYNp 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 --EQPNGLAeSFIIGEEFIGGDsVALILGDNLFHghglTEMLQTAVQREQGATIF-GYHVQDPGRFGV-VEFDADGRAVS 156
Cdd:COG1213    77 dyDETNNIY-SLWLAREALDED-FLLLNGDVVFD----PAILKRLLASDGDIVLLvDRKWEKPLDEEVkVRVDEDGRIVE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 157 IQEKPAEPRSNYAVTGLYFYDRN----VVDYAKQIVPSDRGELEITD-INRMYLERGQLRVEILGRGFsWFDSGTHESLL 231
Cdd:COG1213   151 IGKKLPPEEADGEYIGIFKFSAEgaaaLREALEALIDEGGPNLYYEDaLQELIDEGGPVKAVDIGGLP-WVEIDTPEDLE 229

                  ....*.
gi 1718626009 232 EASQYI 237
Cdd:COG1213   230 RAEELF 235
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-197 1.14e-13

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 70.49  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGGSGTRLYPLTRIISKqllpiydkPMIYY---------PLSVLMLAGIRDILIIStpQDTPRfeELF---GTGE- 69
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT--QYKSH--SLNdhiGSGKp 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  70 -QLGIRLSY-----AVQEQPN-----GLAESF-----II---GEEFIggdsvaLIL-GDNL----FHghgltEMLQTAVQ 125
Cdd:COG0448    72 wDLDRKRGGvfilpPYQQREGedwyqGTADAVyqnldFIersDPDYV------LILsGDHIykmdYR-----QMLDFHIE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 126 REQGATIFGYHV--QDPGRFGVVEFDADGRAVSIQEKPAEPRSNYAVTGLYFYDRNV-------------VDYAKQIVPS 190
Cdd:COG0448   141 SGADITVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVlielleedapnssHDFGKDIIPR 220

                  ....*..
gi 1718626009 191 DRGELEI 197
Cdd:COG0448   221 LLDRGKV 227
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-52 3.67e-13

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 67.28  E-value: 3.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILII 52
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
4-208 7.49e-12

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 65.39  E-value: 7.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLyplTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDtprfEELFGTGEQLGIRlsYAVQEQP 83
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGA----EQVEAALQGSGVA--FARQEQQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  84 NGLAESFIIGEEFIG-GDSVALIL-GDN-LFHGHGLTEMLqtAVQREQGA--TIFGYHVQDPGRFGVVEFDADGRAVSIQ 158
Cdd:PRK14358   82 LGTGDAFLSGASALTeGDADILVLyGDTpLLRPDTLRALV--ADHRAQGSamTILTGELPDATGYGRIVRGADGAVERIV 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1718626009 159 EKPAEPRSNYAV----TGLYFYDRNVVDYAKQIVPSDR-GELEITDINRMYLERG 208
Cdd:PRK14358  160 EQKDATDAEKAIgefnSGVYVFDARAPELARRIGNDNKaGEYYLTDLLGLYRAGG 214
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-213 7.72e-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: 64.20  E-value: 7.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGG--SGTRLYPLTRIISKQLLPIYDKPMIYYPLSVL-MLAGIRDILIISTPQDTPRFEELFGTGEQLGIRLSYAV 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  80 QEQPNGLAesfiigeefiGG-----DsvaLILGDN---LFHGHG-------LTEMLQTAVQREQGATIFGYHV--QDPGR 142
Cdd:cd06428    81 EYKPLGTA----------GGlyhfrD---QILAGNpsaFFVLNAdvccdfpLQELLEFHKKHGASGTILGTEAsrEQASN 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718626009 143 FG-VVEFDADGRAVSIQEKPAEPRSNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITDINRMYLERGQLRVE 213
Cdd:cd06428   148 YGcIVEDPSTGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-233 1.09e-11

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 63.02  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTpRFEELFgtGEQLGIRLSYAVQEQP 83
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKE-QIEELL--KKYPNIKFVYNPDYAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  84 NGLAESFIIGEEFIGGDSVaLILGDNLFHghglTEMLQTAVQREQGATIFgyhVQDPGRFGVVEFDAD----GRAVSIQE 159
Cdd:cd02523    79 TNNIYSLYLARDFLDEDFL-LLEGDVVFD----PSILERLLSSPADNAIL---VDKKTKEWEDEYVKDlddaGVLLGIIS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718626009 160 KPAEPRSNYAVT-GLYFYDRN----VVDYAKQIVPSDRGELEITDINRMYLERGQLRVEILGrGFSWFDSGTHESLLEA 233
Cdd:cd02523   151 KAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-199 4.36e-11

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 62.21  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIIsTPQDTPRFEELFGTGEQL--------- 71
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLV-THASKNAVENHFDTSYELeslleqrvk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  72 -------------GIRLSYAVQEQPNGLAESFIIGEEFIGGDSVALILGDNLFHGHG---LTEMLQTAVQR--EQG-ATI 132
Cdd:PRK10122   83 rqllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASadpLRYNLAAMIARfnETGrSQV 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718626009 133 FGYHVQ-DPGRFGVVE----FDADG---RAVSIQEKPAEPR---SNYAVTGLYFYDRNVVDYAKQIVPSDRGELEITD 199
Cdd:PRK10122  163 LAKRMPgDLSEYSVIQtkepLDREGkvsRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-208 8.30e-10

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 58.99  E-value: 8.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLyplTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELFGTGEqlgirLSYAVQEQP 83
Cdd:PRK14355    7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEEQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  84 NGLAESFIIG-EEFIGGDSVALIL-GDN-LFHGHGLTEMLqtAVQREQGA--TIFGYHVQDPGRFGVVEFDADGRAVSIQ 158
Cdd:PRK14355   79 LGTGHAVACAaPALDGFSGTVLILcGDVpLLRAETLQGML--AAHRATGAavTVLTARLENPFGYGRIVRDADGRVLRIV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1718626009 159 EK----PAEPRSNYAVTGLYFYDRNVVDYAKQIVPSD--RGELEITDINRMYLERG 208
Cdd:PRK14355  157 EEkdatPEERSIREVNSGIYCVEAAFLFDAIGRLGNDnaQGEYYLTDIVAMAAAEG 212
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-234 1.83e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 57.96  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIISKQLLPIYDK-PMIYYPLSVLMLAGIRDILIIStpQDTPRfeEL---FGTGEQLGI-RL 75
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT--QYQPL--ELnnhIGIGSPWDLdRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  76 S--------YAVQEQPN---GLAESFIIGEEFIggDSV----ALIL-GDNLFHgHGLTEMLQTAVQREQGATIFGYHV-- 137
Cdd:PRK05293   80 NggvtilppYSESEGGKwykGTAHAIYQNIDYI--DQYdpeyVLILsGDHIYK-MDYDKMLDYHKEKEADVTIAVIEVpw 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 138 QDPGRFGVVEFDADGRAVSIQEKPAEPRSNYAVTGLYFYDRNVV------DYAKQIVPSDRGEleitDINRMYLERGQLR 211
Cdd:PRK05293  157 EEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLkeylieDEKNPNSSHDFGK----NVIPLYLEEGEKL 232
                         250       260
                  ....*....|....*....|...
gi 1718626009 212 VEILGRGFsWFDSGTHESLLEAS 234
Cdd:PRK05293  233 YAYPFKGY-WKDVGTIESLWEAN 254
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-209 3.29e-09

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 55.98  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLY-PLtriiSKQLLPIYDKPMIYYPLSVLMLAGIRDILIIsTPQDTPRFEELFGtgeqlGIRLSYAVQEQ 82
Cdd:cd02540     2 VILAAGKGTRMKsDL----PKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALA-----NPNVEFVLQEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  83 PNGLAESFIIGEEFIGGDS-VALIL-GDN-LFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADGRAVSIQE 159
Cdd:cd02540    72 QLGTGHAVKQALPALKDFEgDVLVLyGDVpLITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1718626009 160 ----KPAEPRSNYAVTGLY-FYDRNVVDYAKQIVPSD-RGELEITDINRMYLERGQ 209
Cdd:cd02540   152 ekdaTEEEKAIREVNAGIYaFDAEFLFEALPKLTNNNaQGEYYLTDIIALAVADGL 207
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-209 9.72e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 52.91  E-value: 9.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRL---YPltriisKQLLPIYDKPMIYYPLSVLMLAGIRDILIIstpqdtprfeelFGTG-----EQLGIRL 75
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGaeevkEVLGDRS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  76 SYAVQEQPNGLAESFIIGEEFIGGDS--VALILGDN-LFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADG 152
Cdd:PRK14354   68 EFALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718626009 153 RAVSIQE----KPAEPRSNYAVTGLYFYDRNVVDYA-KQIVPSD-RGELEITDINRMYLERGQ 209
Cdd:PRK14354  148 EVEKIVEqkdaTEEEKQIKEINTGTYCFDNKALFEAlKKISNDNaQGEYYLTDVIEILKNEGE 210
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-64 1.11e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 51.67  E-value: 1.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718626009   4 IILAGGSGTRL---YPltriisKQLLPIYDKPMIYYPLSVLMLAG-IRDILIISTPQDTPRFEEL 64
Cdd:PRK00155    7 IIPAAGKGSRMgadRP------KQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAEL 65
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-94 2.14e-07

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: 51.04  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIIS-KQLLPIY-DKPMIYYPLS-VLMLAGIRDILIIstpqdtprfeelfgTGEQLGIRlsy 77
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSRESYpKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVV--------------TNEEYRFL--- 63
                          90
                  ....*....|....*...
gi 1718626009  78 aVQEQ-PNGLAESFIIGE 94
Cdd:cd02509    64 -VREQlPEGLPEENIILE 80
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-64 2.16e-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: 2.16e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718626009   4 IILAGGSGTRLyplTRIISKQLLPIYDKPMIYYPLSVLMLAG-IRDILIISTPQDTPRFEEL 64
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEEL 59
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
3-189 2.48e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 51.42  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGGSGTRLYPLTRIISKQLLPIYDK-PMIYYPLSVLMLAGIRDILIIStpQ-----------DTPRFEElFGTG-- 68
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT--QfnsaslnrhisQTYNFDG-FSGGfv 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  69 EQLgirlsyAVQEQPN------GLAES-----FIIGEEFIggDSVaLIL-GDNLFHgHGLTEMLQTavQREQGA--TIFG 134
Cdd:PRK02862   83 EVL------AAQQTPEnpswfqGTADAvrkylWHFQEWDV--DEY-LILsGDQLYR-MDYRLFVQH--HRETGAdiTLAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 135 YHV--QDPGRFGVVEFDADGRAVSIQEKP---------------------AEPRSNYAVTGLYFYDRNVV---------- 181
Cdd:PRK02862  151 LPVdeKDASGFGLMKTDDDGRITEFSEKPkgdelkamavdtsrlglspeeAKGKPYLASMGIYVFSRDVLfdllnknpey 230

                  ....*....
gi 1718626009 182 -DYAKQIVP 189
Cdd:PRK02862  231 tDFGKEIIP 239
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-53 4.40e-07

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 49.46  E-value: 4.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1718626009   3 GIILAGGSGTRLYPLTRIISKQLLPI---YDkpMIYYPLSVLMLAGIRDILIIS 53
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT 52
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
4-159 4.91e-07

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: 50.41  E-value: 4.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLY---PltriisKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQdtprfeelfgtGEQL-----GIRL 75
Cdd:COG1207     6 VILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHG-----------AEQVraalaDLDV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  76 SYAVQEQPNGLAESFIIGEEFIGGDS-VALIL-GDN-LFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFGVVEFDADG 152
Cdd:COG1207    69 EFVLQEEQLGTGHAVQQALPALPGDDgTVLVLyGDVpLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDG 148

                  ....*..
gi 1718626009 153 RAVSIQE 159
Cdd:COG1207   149 RVLRIVE 155
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-64 1.81e-06

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 47.90  E-value: 1.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718626009   4 IILAGGSGTRlypLTRIISKQLLPIYDKPMIYYPLSVLM-LAGIRDILIISTPQDTPRFEEL 64
Cdd:cd02516     4 IILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKEL 62
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-94 2.92e-06

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 48.14  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRLYPLTRIIS-KQLLPIY-DKPMIYypLSVLMLAGI---RDILIIstpqdtprfeelfgTGEqlgiRL 75
Cdd:COG0836     3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ--QTVERLAGLvppENILVV--------------TNE----EH 62
                          90
                  ....*....|....*....
gi 1718626009  76 SYAVQEQPNGLAESFIIGE 94
Cdd:COG0836    63 RFLVAEQLPELGPANILLE 81
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-64 9.33e-06

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: 45.26  E-value: 9.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1718626009   6 LAGGSGTRLypltRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPqDTPRFEEL 64
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREY 54
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-214 1.02e-05

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 45.71  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYplSVLMLAGIRD---ILIIstpqdtpRFEELfgTGEQLGIRLS---- 76
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFIC-------RDEHN--TKFHLDESLKllap 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  77 -YAVQEQPN---GLAESFIIGEEFIGGDSVALIL-GDNLFHGhGLTEMLQTAVQREQGATIFGYHVQDPgRFGVVEFDAD 151
Cdd:cd04183    71 nATVVELDGetlGAACTVLLAADLIDNDDPLLIFnCDQIVES-DLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDEN 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718626009 152 GRAVSIQEKpaEPRSNYAVTGLYFYDRN--VVDYAKQIVPSDR---GELEITDINRmYLERGQLRVEI 214
Cdd:cd04183   149 GRVIETAEK--EPISDLATAGLYYFKSGslFVEAAKKMIRKDDsvnGEFYISPLYN-ELILDGKKVGI 213
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-200 3.30e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 45.14  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   1 MKGIILAGGSGTRL---YPltriisKQLLPIYDKPMIYYPLSV---------LMLAGIRDILIISTPQDTPRFeelfgtg 68
Cdd:PRK14357    1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINWVIDTakkvaqkvgVVLGHEAELVKKLLPEWVKIF------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  69 eqlgirlsyaVQEQPNGLAESFIIGEEFIGGDSVALIL-GDNLFHGHG-LTEMLQTAVQREQGATIFGYHVQDPGRFGVV 146
Cdd:PRK14357   68 ----------LQEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENtLKRLIEEHNRKGADVTILVADLEDPTGYGRI 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1718626009 147 EFDaDGRAVSIQEKPAEPRSNYAV---TGLYFYD-RNVVDYAKQIVPSD-RGELEITDI 200
Cdd:PRK14357  138 IRD-GGKYRIVEDKDAPEEEKKIKeinTGIYVFSgDFLLEVLPKIKNENaKGEYYLTDA 195
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-233 5.57e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.05  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGGSGTRLYPLTRIISKQLLP---IYDkpMIYYPLSVLMLAGIRDILI------------ISTpqdtprfeelfgt 67
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhISQ------------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  68 geqlGIRLSyavqeqpnGLAESFI--------IGEEFIGG-----------------DSVALILGDNLFHgHGLTEMLQT 122
Cdd:PRK00844   73 ----TWRLS--------GLLGNYItpvpaqqrLGKRWYLGsadaiyqslnliededpDYVVVFGADHVYR-MDPRQMVDF 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009 123 AVQREQGATIFGYHV--QDPGRFGVVEFDADGRAVSIQEKPAEPRS-------NYAVTGLYFYDRNVV------------ 181
Cdd:PRK00844  140 HIESGAGVTVAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDALvdalrrdaaded 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1718626009 182 ---DYAKQIVPS--DRGELEITDI--NRMyleRGQLRVEilgRGFsWFDSGTHESLLEA 233
Cdd:PRK00844  220 sshDMGGDIIPRlvERGRAYVYDFstNEV---PGATERD---RGY-WRDVGTIDAYYDA 271
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
3-52 7.89e-05

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 43.69  E-value: 7.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1718626009   3 GIILAGGSGTRLYPLTRIISKQLLPI---YDkpMIYYPLSVLMLAGIRDILII 52
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-108 2.64e-04

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 41.30  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGGSGTRL-YPltriisKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDTPRFEELfgtgEQLGIRLSYaVQE 81
Cdd:COG2068     6 AIILAAGASSRMgRP------KLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAL----AGLGVRVVV-NPD 74
                          90       100
                  ....*....|....*....|....*....
gi 1718626009  82 QPNGLAESFIIGEEFIGG--DSVALILGD 108
Cdd:COG2068    75 WEEGMSSSLRAGLAALPAdaDAVLVLLGD 103
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
4-52 3.56e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 41.75  E-value: 3.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLYPLTRIISKQLLPIYDK-PMIYYPLSVLMLAGIRDILII 52
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVL 68
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
4-196 4.25e-04

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 41.02  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRD-ILIISTPQDTPR--FEELFGTGEQLGIRLSYAVQ 80
Cdd:cd02524     2 VILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDfILCLGYKGHVIKeyFLNYFLHNSDVTIDLGTNRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  81 EQPNGLAESFII-----GEE-FIGGDSVAL---ILGDNLF---HGHGLT----EMLqTAVQREQGATIFGYHVQDPGRFG 144
Cdd:cd02524    82 ELHNSDIEDWKVtlvdtGLNtMTGGRLKRVrryLGDDETFmltYGDGVSdvniNAL-IEFHRSHGKLATVTAVHPPGRFG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1718626009 145 VVEFDADGRAVSIQEKPAEPRSnyAVTGLYF-YDRNVVDYakqiVPSDRGELE 196
Cdd:cd02524   161 ELDLDDDGQVTSFTEKPQGDGG--WINGGFFvLEPEVFDY----IDGDDTVFE 207
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-159 5.02e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.39  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   4 IILAGGSGTRL-YPLtriiSKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQdtprFEELFGTGEQLGIRLSYAVQEQ 82
Cdd:PRK14353    9 IILAAGEGTRMkSSL----PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPG----AEAVAAAAAKIAPDAEIFVQKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009  83 PNGLAESFIIGEEFI--GGDSVALILGDNLFHGHGLTEMLQTAVQREQGATIFGYHVQDPGRFG--VVEfdaDGRAVSIQ 158
Cdd:PRK14353   81 RLGTAHAVLAAREALagGYGDVLVLYGDTPLITAETLARLRERLADGADVVVLGFRAADPTGYGrlIVK---GGRLVAIV 157

                  .
gi 1718626009 159 E 159
Cdd:PRK14353  158 E 158
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-64 1.58e-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: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718626009   1 MKGIILAGGSGTRLYpltriISKQLLPIYDKPMIYYPLSVlmLAGIRDILIISTPQDtPRFEEL 64
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP-ERYAAL 60
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
3-54 3.84e-03

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 37.70  E-value: 3.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1718626009   3 GIILA-GGSgtrlyplTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILIIST 54
Cdd:pfam02348   2 AIIPArLGS-------KRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT 47
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-75 3.96e-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: 37.17  E-value: 3.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718626009   3 GIILAGGSGTRL-YPltriisKQLLPIYDKPMIYYplSVLMLAGIRDILIISTPqdtprFEELFGTGEQLGIRL 75
Cdd:pfam12804   1 AVILAGGRSSRMgGD------KALLPLGGKPLLER--VLERLRPAGDEVVVVAN-----DEEVLAALAGLGVPV 61
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-108 4.27e-03

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: 37.54  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGGSGTRLYPltriiSKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPQDtprfEELfgTGEQLGIRLSYAVQEQ 82
Cdd:cd04182     3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEA----DAV--RAALAGLPVVVVINPD 71
                          90       100
                  ....*....|....*....|....*....
gi 1718626009  83 P-NGLAESFIIGEEFIGGDS--VALILGD 108
Cdd:cd04182    72 WeEGMSSSLAAGLEALPADAdaVLILLAD 100
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-52 5.68e-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: 37.20  E-value: 5.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1718626009   3 GIILAGGSGTRLYPLTRIISKQLLPIYDKPMIYYPLSVLMLAGIRDILII 52
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
 
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