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Conserved domains on  [gi|2027676947|ref|WP_210867545|]
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MULTISPECIES: glucose-1-phosphate thymidylyltransferase RfbA [Enterobacter]

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];
1-287 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 553.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2027676947 241 EKRQGFKIACLEEIAYNQGWLDKEMVKSIGNTLSKTGYGNYLLNLVK 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 553.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2027676947 241 EKRQGFKIACLEEIAYNQGWLDKEMVKSIGNTLSKTGYGNYLLNLVK 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-287 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: 545.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  82 TPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 162 KAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2027676947 242 KRQGFKIACLEEIAYNQGWLDKEMVKSIGNTLSKTGYGNYLLNLVK 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 1.67e-170

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: 471.29  E-value: 1.67e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-287 6.36e-143

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 403.67  E-value: 6.36e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  82 TPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 162 KAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2027676947 242 KRQGFKIACLEEIAYNQGWLDKEMVKSIGNTLSKTGYGNYLLNLVK 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 9.83e-99

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: 289.54  E-value: 9.83e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSV-CLVLGDNIFFGQSFGKQLKHAVE--NLNGATVFGYKVMDPERFGVVEFDKDFNAISI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 158 EEKPKAPK-SNWAVTGLYFYDNRVVD-IAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2027676947 236 FV 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-287 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 553.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2027676947 241 EKRQGFKIACLEEIAYNQGWLDKEMVKSIGNTLSKTGYGNYLLNLVK 287
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-287 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: 545.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  82 TPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 162 KAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2027676947 242 KRQGFKIACLEEIAYNQGWLDKEMVKSIGNTLSKTGYGNYLLNLVK 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 1.67e-170

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: 471.29  E-value: 1.67e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTV 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-287 6.36e-143

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 403.67  E-value: 6.36e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  82 TPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 162 KAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQFVQTVE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2027676947 242 KRQGFKIACLEEIAYNQGWLDKEMVKSIGNTLSKTGYGNYLLNLVK 287
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIK 290
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 9.83e-99

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: 289.54  E-value: 9.83e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSV-CLVLGDNIFFGQSFGKQLKHAVE--NLNGATVFGYKVMDPERFGVVEFDKDFNAISI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEkaADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 158 EEKPKAPK-SNWAVTGLYFYDNRVVD-IAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFAWLDTGTHDSLLEASQ 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 2027676947 236 FV 237
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-237 3.82e-68

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: 211.27  E-value: 3.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEdQASFKRILGNGNQFGINLQYQVQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSVCLVLGDNiFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDkDFNAISIEEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDN-LIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFaWLDTGTHDSLLEASQFV 237
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 3.55e-62

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: 195.49  E-value: 3.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQAsFKRILGNGNQFGINLQYQVQPT 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQ-IEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  83 PDGLAQAFILGEDFIGDDSVCLVLGDNIFFGqSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEKPK 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2027676947 163 APKSNWAVTGLYFYDNRVVDIAKKVQPseRGELEITSVNQKYLEMGELKVEQLgrGFAWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-249 4.82e-61

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: 197.24  E-value: 4.82e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQVQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  82 TPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGqSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 162 KAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGFaWLDTGTHDSLLEASQFV--QT 239
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIldEV 238

                         250
                  ....*....|
gi 2027676947 240 VEKRQGFKIA 249
Cdd:TIGR01208 239 EREVQGVDDE 248
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-235 1.17e-46

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: 160.84  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQAsFKRILGNGNQFGINLQYQVQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEK-VREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIgDDSVCLVLGDNIFFGQSfgkqLKHAVEnLNGATVFGYKVMDPERFGVVEFDKDfNAISIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDL----LERLIR-AEAPAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGRGfaWLDTGTHDSLLEASQ 235
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDANE 225
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-237 4.58e-43

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: 147.22  E-value: 4.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITT-PEDQasFKRILGNGNQFGINLQYQVQ 80
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGyLAEQ--IEEYFGDGSRFGVRITYVDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  81 PTPDGLAQAFILGEDFIGDDSVCLVLGDnIFFGQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDFNAISIEEK 160
Cdd:COG1208    79 GEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027676947 161 PKAPKSNWAVTGLYFYDNRVVDIAKKVQPsergeLEITSVNQKYLEMGELKVEQLgRGFaWLDTGTHDSLLEASQFV 237
Cdd:COG1208   158 PEEPPSNLINAGIYVLEPEIFDYIPEGEP-----FDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEANALL 227
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-234 3.52e-31

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: 116.86  E-value: 3.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTP------------------------E 56
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdrsyeleetlekkgkT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  57 DQASFKRILGNgnqfGINLQYQVQPTPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFG-KQLKHAVENLnGATVFGY 135
Cdd:cd02541    81 DLLEEVRIISD----LANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPClKQLIEAYEKT-GASVIAV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 136 KVMDPE---RFGVVEFDKD----FNAISIEEKPK---APkSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYL 205
Cdd:cd02541   156 EEVPPEdvsKYGIVKGEKIdgdvFKVKGLVEKPKpeeAP-SNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLL 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2027676947 206 EMGELkveqLGRGF--AWLDTGTHDSLLEAS 234
Cdd:cd02541   235 EEEPV----YAYVFegKRYDCGNKLGYLKAT 261
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-226 4.34e-25

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: 99.98  E-value: 4.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITT--PEDQASFKRILgnGNQFGINLQYQ 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEY--EKKLGIKITFS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  79 VQPTPDGLAQAFILGEDFIGDDSVC-LVLGDNIF----FGQ--SFGKqlKHAVEnlngATVFGYKVMDPERFGVVEFDKD 151
Cdd:cd06425    79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVIcdfpLAEllDFHK--KHGAE----GTILVTKVEDPSKYGVVVHDEN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 152 FNAI-SIEEKPKAPKSNWAVTGLYFYDNRVVDiakkvqpseRGELEITSVNQ----KYLEMGELKVEQLgRGFaWLDTGT 226
Cdd:cd06425   153 TGRIeRFVEKPKVFVGNKINAGIYILNPSVLD---------RIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WMDIGQ 221
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 4.26e-20

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


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 86.45  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITtpedqaSFKR-----ILGNGNQFGINLQYQ 78
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSV------GYLAeqieeYFGDGYRGGIRIYYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  79 VQPTPDGLAQAFILGEDFIGDDSVCLVLGDNiFFGQSFgKQLKHAVENLNG-ATVFGYKVMDPERFGVVEFDKDFNAISI 157
Cdd:cd06915    76 IEPEPLGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDL-LALLAALRASGAdATMALRRVPDASRYGNVTVDGDGRVIAF 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027676947 158 EEKPKAPKSNWAVTGLYFYDNRVVDIAKKVQPSergeLEiTSVNQKYLEMGELKV-EQLGRgFawLDTGTHDSLLEA 233
Cdd:cd06915   154 VEKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRLYGfEVDGY-F--IDIGIPEDYARA 222
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-233 3.16e-19

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: 83.72  E-value: 3.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITT--PEdqaSFKRILGNGNQFGINLQYQVQP 81
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNylAE---MIEDYFGDGSKFGVNISYVRED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  82 TPDGLAQAFILGEDFIgDDSVCLVLGDnIFFGQSFGKQLKHAVENLNGATV----FGYKVmdPerFGVVEFDkDFNAISI 157
Cdd:cd06426    79 KPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVcvreYEVQV--P--YGVVETE-GGRITSI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 158 EEKpkaPKSNWAV-TGLYFYDNRVVDiakKVQPSERgeLEITSVNQKYLEMGElKV------EQlgrgfaWLDTGTHDSL 230
Cdd:cd06426   152 EEK---PTHSFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGK-KVgvfpihEY------WLDIGRPEDY 216


                  ...
gi 2027676947 231 LEA 233
Cdd:cd06426   217 EKA 219
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-198 7.02e-19

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 84.31  E-value: 7.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYplSV--LMLAGIRDILLITTP-----EDQ--ASF----------- 61
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiEDHfdRSYeleatleakgk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  62 -------KRILGngnqfGINLQYQVQPTPDGLAQAFILGEDFIGDDSVCLVLGDNIFFGQSFG-KQLKHAVENLnGATVF 133
Cdd:COG1210    83 eelleevRSISP-----LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPClKQMIEVYEET-GGSVI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027676947 134 GYKVMDPE---RFGVV---EFDKDFNAIS-IEEKPK---APkSNWAVTGLYFYDNRVVDIAKKVQPSERGELEIT 198
Cdd:COG1210   157 AVQEVPPEevsKYGIVdgeEIEGGVYRVTgLVEKPApeeAP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLT 230
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-59 3.01e-16

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 75.39  E-value: 3.01e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQA 59
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQA 59
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-177 1.25e-13

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 70.10  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGGSGSRLHPITLGTSKqllpiydkPMIYY---------PLSVLMLAGIRDILLITtpedQ---ASFKRILGNGNQ 70
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT----QyksHSLNDHIGSGKP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  71 FGIN--------LQYQVQPTPD----GLAQAFILGEDFIGD---DSVCLVLGDNIF---FGQSfgkqLKHAVENLNGATV 132
Cdd:COG0448    72 WDLDrkrggvfiLPPYQQREGEdwyqGTADAVYQNLDFIERsdpDYVLILSGDHIYkmdYRQM----LDFHIESGADITV 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2027676947 133 FGYKV--MDPERFGVVEFDKDFNAISIEEKPKAPKSNWAVTGLYFYD 177
Cdd:COG0448   148 ACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-59 3.85e-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: 66.89  E-value: 3.85e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQA 59
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQA 59
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-233 4.45e-11

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: 61.05  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDIlLITT---PEDQASFkriLGNgNQFGINLQYQ 78
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlADQIEAH---LGD-SRFGLRITIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  79 VQP-----TPDGLAQAfilgEDFIGDDSVCLVLGDNIFFGqSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEF--DKD 151
Cdd:cd06422    76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDAD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 152 FNAISIEEKPKAPksnWAVTGLYFYDNRVVDIAKkvqpseRGELEITSVNQKYLEMGELKVEqLGRGFaWLDTGTHDSLL 231
Cdd:cd06422   151 GRLRRGGGGAVAP---FTFTGIQILSPELFAGIP------PGKFSLNPLWDRAIAAGRLFGL-VYDGL-WFDVGTPERLL 219


                  ..
gi 2027676947 232 EA 233
Cdd:cd06422   220 AA 221
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-223 1.08e-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: 60.32  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITtpedqasfkrilG-NGNQF------GINLQ 76
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT------------GyKKEQIeellkkYPNIK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  77 YQVQPTPD--GLAQAFILGEDFIGDDsvCLVL-GDnIFFGQSFGKQLKHAVENlngatvFGYKVMDPERFGVVEFDKDFN 153
Cdd:cd02523    70 FVYNPDYAetNNIYSLYLARDFLDED--FLLLeGD-VVFDPSILERLLSSPAD------NAILVDKKTKEWEDEYVKDLD 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027676947 154 A----ISIEEKPKAPKSN-WAVTGLYFYD----NRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQLGrGFAWLD 223
Cdd:cd02523   141 DagvlLGIISKAKNLEEIqGEYVGISKFSpedaDRLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYE 218
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-198 4.14e-10

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 59.53  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQA-------SF----------KRI 64
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSienhfdtSFeleamlekrvKRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  65 LGNGNQF----GINLQYQVQPTPDGLAQAFILGEDFIGDDSVCLVLGDNIFfgQSFGKQLKHavENLNG----------A 130
Cdd:PRK13389   90 LLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIL--DEYESDLSQ--DNLAEmirrfdetghS 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027676947 131 TVFGYKVMDPERFGVVEFD-KDFNA------ISIEEKPKAPK--SNWAVTGLYFYDNRVVDIAKKVQPSERGELEIT 198
Cdd:PRK13389  166 QIMVEPVADVTAYGVVDCKgVELAPgesvpmVGVVEKPKADVapSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 4.28e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.71  E-value: 4.28e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2027676947   2 KGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLIT 53
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-65 2.06e-09

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: 56.29  E-value: 2.06e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2027676947   4 IILAGGSGSRLHpitLGTSKQLLPIYDKPMIYYPLSVLMLAG-IRDILLITTPEDQASFKRIL 65
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELL 60
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-110 5.37e-09

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 56.05  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQA-----------------SFKR 63
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAvenhfdtsyeleslleqRVKR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2027676947  64 ILGNGNQF----GINLQYQVQPTPDGLAQAFILGEDFIGDDSVCLVLGDNI 110
Cdd:PRK10122   84 QLLAEVQSicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVV 134
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-214 6.98e-09

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: 55.34  E-value: 6.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGG--SGSRLHPITLGTSKQLLPIYDKPMIYYPLSVL-MLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQV 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  80 QPTPDGLAQAFILGEDFI--GDDSVCLVLGDNI-----------FFGQSFGKQLKHAVE-NLNGATVFGYKVMDPERFGV 145
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQIlaGNPSAFFVLNADVccdfplqelleFHKKHGASGTILGTEaSREQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027676947 146 VEFdkdfnaisiEEKPKAPKSNWAVTGLYFYDNRVVDIAKKVQPSERGELEITSVNQKYLEMGELKVEQ 214
Cdd:cd06428   161 LHY---------VEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQ 220
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-166 1.69e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 54.83  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGGSGSRLHPITLGTSKQLLP---IYDkpMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYqV 79
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLLGNY-I 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  80 QPTP----------DGLAQAFILGEDFIGD---DSVCLVLGDNIF---FGQsfgkQLKHAVENLNGATVFGYKV--MDPE 141
Cdd:PRK00844   85 TPVPaqqrlgkrwyLGSADAIYQSLNLIEDedpDYVVVFGADHVYrmdPRQ----MVDFHIESGAGVTVAAIRVprEEAS 160

                         170       180
                  ....*....|....*....|....*
gi 2027676947 142 RFGVVEFDKDFNAISIEEKPKAPKS 166
Cdd:PRK00844  161 AFGVIEVDPDGRIRGFLEKPADPPG 185
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-108 5.31e-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: 5.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGGSGSRLhpitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGINLQYQvqpt 82
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWE---- 73

                          90       100
                  ....*....|....*....|....*...
gi 2027676947  83 pDGLAQAFILGEDFIGDD-SVCLV-LGD 108
Cdd:cd04182    74 -EGMSSSLAAGLEALPADaDAVLIlLAD 100
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-69 8.63e-08

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: 51.76  E-value: 8.63e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027676947   4 IILAGGSGSRLHpitLGTSKQLLPIYDKPMIYYPLSVLM-LAGIRDILLITTPEDQASFKRILGNGN 69
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGL 67
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-212 1.18e-07

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: 51.49  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRLHPITLGTSKQLLPIYDKPMIYYplSVLMLAGIRD--ILLITTPEDQASF---KRILGNGNQFGInlqYQ 78
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrFIFICRDEHNTKFhldESLKLLAPNATV---VE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  79 VQPTPDGLAQAFILGEDFI-GDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGATVFGYKVMDpeRFGVVEFDKDFNAISI 157
Cdd:cd04183    77 LDGETLGAACTVLLAADLIdNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP--RWSYVKLDENGRVIET 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 158 EEKpkAPKSNWAVTGLYFYDN--RVVDIAKKVQP---SERGELEITSVNQKYLEMGeLKV 212
Cdd:cd04183   155 AEK--EPISDLATAGLYYFKSgsLFVEAAKKMIRkddSVNGEFYISPLYNELILDG-KKV 211
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-63 2.32e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 50.52  E-value: 2.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027676947   4 IILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYPLSVLMLAG-IRDILLITTPEDQASFKR 63
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAE 64
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-111 1.23e-06

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 47.92  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGGSGSRLHPITLGTSKQLLPI---YDkpMIYYPLSVLMLAGIRDIlLITTPEDQASFKRILGNGNQFGIN----- 74
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNV-GVLTQYKSRSLNDHLGSGKEWDLDrkngg 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2027676947  75 ---LQYQVQPTPD---GLAQAFILGEDFIGD---DSVCLVLGDNIF 111
Cdd:cd02508    78 lfiLPPQQRKGGDwyrGTADAIYQNLDYIERsdpEYVLILSGDHIY 123
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-166 2.00e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 48.68  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILLITtpEDQA-SFKRILGNG--------NQFgI 73
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLT--QYKAhSLIRHIQRGwsffreelGEF-V 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  74 NL---QYQV------QPTPDGLAQAFilgeDFIG--DDSVCLVL-GDNIfFGQSFGKQLKHAVEnlNGA--TVFGYKV-- 137
Cdd:PRK00725   96 DLlpaQQRVdeenwyRGTADAVYQNL----DIIRryDPKYVVILaGDHI-YKMDYSRMLADHVE--SGAdcTVACLEVpr 168

                         170       180
                  ....*....|....*....|....*....
gi 2027676947 138 MDPERFGVVEFDKDFNAISIEEKPKAPKS 166
Cdd:PRK00725  169 EEASAFGVMAVDENDRITAFVEKPANPPA 197
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-59 2.66e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 47.08  E-value: 2.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2027676947   3 GIILAGGSGSRLhpitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQA 59
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEE 57
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-132 3.47e-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: 46.03  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGGSGSRlhpitLGTSKQLLPIYDKPMIYYPLSVLMLAGiRDILLITTPEDQASFKRILGngnqfginLQYQVQPT 82
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2027676947  83 PD-GLAQAFILGEDFIGDDSVCLVL-GDNIFFGQSFGKQLKHAVENLNGATV 132
Cdd:pfam12804  67 PGqGPLAGLLAALRAAPGADAVLVLaCDMPFLTPELLRRLLAAAEESGADIV 118
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-234 3.47e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 47.94  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILLITTPEDQASFKRIlGNGNQFGIN----- 74
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHI-GIGSPWDLDringg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  75 ---LQ-YQVQPTPD---GLAQAFILGEDFIG--DDSVCLVL-GDNIFfGQSFGKQLKHAVENLNGATVfgyKVMD----- 139
Cdd:PRK05293   83 vtiLPpYSESEGGKwykGTAHAIYQNIDYIDqyDPEYVLILsGDHIY-KMDYDKMLDYHKEKEADVTI---AVIEvpwee 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947 140 PERFGVVEFDKDFNAISIEEKPKAPKSNWAVTGLYFY---------------DNRVVDIAKKVQPsergeleitsvnqKY 204
Cdd:PRK05293  159 ASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkrlkeyliedeknPNSSHDFGKNVIP-------------LY 225

                         250       260       270
                  ....*....|....*....|....*....|
gi 2027676947 205 LEMGELKVEQLGRGFaWLDTGTHDSLLEAS 234
Cdd:PRK05293  226 LEEGEKLYAYPFKGY-WKDVGTIESLWEAN 254
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-208 1.42e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 46.13  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQASFKRILGNGNQFGinlqyqVQPTP 83
Cdd:PRK14358   11 VILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAFA------RQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  84 DGLAQAFILGEDFI--GDDSVCLVLGDNIFFGQSFGKQLKHAVENLNGA-TVFGYKVMDPERFGVVEFDKDFNAISIEEK 160
Cdd:PRK14358   82 LGTGDAFLSGASALteGDADILVLYGDTPLLRPDTLRALVADHRAQGSAmTILTGELPDATGYGRIVRGADGAVERIVEQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2027676947 161 PKAPKSNWAV----TGLYFYDNRVVDIAKKV-QPSERGELEITSVNQKYLEMG 208
Cdd:PRK14358  162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-59 3.90e-05

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: 43.26  E-value: 3.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027676947   1 MKGIILAGGSGSRlhpitLGTSKQLLPIYDKPMIYYPLSVlmLAGIRDILLITTPEDQA 59
Cdd:COG0746     5 ITGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRPER 56
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-165 6.09e-05

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 43.72  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPI-TLGTSKQLLPIY-DKPMIYYPLS-VLMLAGIRDILLITTpEDQASfkRILGNGNQFGINLQY 77
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVTN-EEYRF--LVREQLPEGLPEENI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  78 QVQPTPDGLAQAFILGEDFI---GDDSVCLVL------GDNiffgQSFGKQLKHAVENLNG-------------ATVFGY 135
Cdd:cd02509    78 ILEPEGRNTAPAIALAALYLakrDPDAVLLVLpsdhliEDV----EAFLKAVKKAVEAAEEgylvtfgikptrpETGYGY 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2027676947 136 ----KVMDPERFGVVEFdkdfnaisiEEKPKAPK 165
Cdd:cd02509   154 ieagEKLGGGVYRVKRF---------VEKPDLET 178
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-55 6.84e-05

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 42.57  E-value: 6.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027676947   6 LAGGSGSRLHpitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTP 55
Cdd:COG2266     1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-63 2.91e-04

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 40.64  E-value: 2.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2027676947   1 MKGIILAGGSGSRlhpitLGTSKQLLPIYDKPMIYYPLSvlMLAGIRDILLITTPEDQASFKR 63
Cdd:cd02503     1 ITGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYAL 56
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-160 3.11e-04

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: 41.35  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYPLSVLMLAGIRDILLITTPEDQAsFKRILGNgnqfgINLQYQVQPTP 83
Cdd:cd02540     2 VILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQ-VKKALAN-----PNVEFVLQEEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  84 DGLAQAFILGEDFI-GDDSVCLVL-GDNIFF-GQSFGKQLKHAVENLNGATVFGYKVMDPERFG--VVEFDKDFNAIsIE 158
Cdd:cd02540    73 LGTGHAVKQALPALkDFEGDVLVLyGDVPLItPETLQRLLEAHREAGADVTVLTAELEDPTGYGriIRDGNGKVLRI-VE 151


                  ..
gi 2027676947 159 EK 160
Cdd:cd02540   152 EK 153
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 9.20e-04

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.05  E-value: 9.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2027676947   1 MKGIILAGGSGSRL-------HPitlgtsKQLLPIY-DKPMIYypLSVLMLAGI---RDILLIT 53
Cdd:COG0836     3 IYPVILAGGSGTRLwplsresYP------KQFLPLLgEKSLLQ--QTVERLAGLvppENILVVT 58
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-67 9.40e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 40.22  E-value: 9.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027676947   4 IILAGGSGSRLhpiTLGTSKQLLPIYDKPMIYYPLSVLMLAG-IRDILLITTPEDQASFKRILGN 67
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-63 1.81e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 38.63  E-value: 1.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2027676947   1 MKGIILAGGSGSRLHpitlGTSKQLLPIYDKPMIYYplsVLM-LAGIRDILLITTPEDQASFKR 63
Cdd:PRK00317    4 ITGVILAGGRSRRMG----GVDKGLQELNGKPLIQH---VIErLAPQVDEIVINANRNLARYAA 60
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-213 1.92e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.43  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   4 IILAGGSGSRL---HPitlgtsKQLLPIYDKPMIYYPLSVLMLAGIRDIllITtpedqasfkrILGNG-----NQFGINL 75
Cdd:PRK14354    6 IILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKI--VT----------VVGHGaeevkEVLGDRS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  76 QYQVQPTPDGLAQAFILGEDFIGD-DSVCLVL-GDNIFF-GQSFGKQLKHAVENLNGATVFGYKVMDPERFGVVEFDKDF 152
Cdd:PRK14354   68 EFALQEEQLGTGHAVMQAEEFLADkEGTTLVIcGDTPLItAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027676947 153 NAISIEEKPKAPKSNWAV----TGLYFYDNRVVDIA-KKVQP-SERGELEITSVNQKYLEMGElKVE 213
Cdd:PRK14354  148 EVEKIVEQKDATEEEKQIkeinTGTYCFDNKALFEAlKKISNdNAQGEYYLTDVIEILKNEGE-KVG 213
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-163 2.04e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 39.48  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   3 GIILAGGSGSRLHPITLGTSKQLLPIYDK-PMIYYPLSVLMLAGIRDILLITtpedQ---ASFKRILGNGNQFGINLQYQ 78
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT----QfnsASLNRHISQTYNFDGFSGGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  79 V-----QPTPD------GLAQA-----FILGEDFIgdDSVCLVLGDNIfFGQSFGKQLKHAVENLNGATVFGYKVmDPER 142
Cdd:PRK02862   82 VevlaaQQTPEnpswfqGTADAvrkylWHFQEWDV--DEYLILSGDQL-YRMDYRLFVQHHRETGADITLAVLPV-DEKD 157

                         170       180
                  ....*....|....*....|....
gi 2027676947 143 ---FGVVEFDKDFNAISIEEKPKA 163
Cdd:PRK02862  158 asgFGLMKTDDDGRITEFSEKPKG 181
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-53 2.84e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 38.68  E-value: 2.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2027676947   3 GIILAGGSGSRLHPITLGTSKQLLPI---YDkpMIYYPLSVLMLAGIRDILLIT 53
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLT 57
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-200 3.11e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.59  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947   1 MKGIILAGGSGSRLHPitlGTSKQLLPIYDKPMIYYplsVLMLAG-IRDILLITTPEDQASFKRILGNgnqfgiNLQYQV 79
Cdd:PRK14357    1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINW---VIDTAKkVAQKVGVVLGHEAELVKKLLPE------WVKIFL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027676947  80 QPTPDGLAQAFILGEDFIGDDSVCLVL-GDNIFFGQSFGKQL-KHAVENLNGATVFGYKVMDPERFGVVEfdKDFNAISI 157
Cdd:PRK14357   69 QEEQLGTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLiEEHNRKGADVTILVADLEDPTGYGRII--RDGGKYRI 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2027676947 158 EEKPKAPKSNWAV----TGLYFYDNR-VVDIAKKVQP-SERGELEITSV 200
Cdd:PRK14357  147 VEDKDAPEEEKKIkeinTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
 
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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