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Conserved domains on  [gi|119767875|gb|ABM00446|]
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Glucose-1-phosphate thymidylyltransferase [Shewanella amazonensis SB2B]

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];
16-300 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 540.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:COG1209    2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:COG1209   82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTIE 255
Cdd:COG1209  162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 119767875 256 KRQGLKIACLEEIAYRNGWISTETLLQHAKALSQSGYGDYLRQLV 300
Cdd:COG1209  242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
16-300 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 540.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:COG1209    2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:COG1209   82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTIE 255
Cdd:COG1209  162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 119767875 256 KRQGLKIACLEEIAYRNGWISTETLLQHAKALSQSGYGDYLRQLV 300
Cdd:COG1209  242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 16-299 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: 526.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTIE 255
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 119767875  256 KRQGLKIACLEEIAYRNGWISTETLLQHAKALSQSGYGDYLRQL 299
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 16-254 1.13e-166

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: 462.04  E-value: 1.13e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:cd02538    2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:cd02538   82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119767875 176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTI 254
Cdd:cd02538  162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 16-300 2.82e-141

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 400.20  E-value: 2.82e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTIE 255
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 119767875 256 KRQGLKIACLEEIAYRNGWISTETLLQHAKALSQSGYGDYLRQLV 300
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 16-251 5.56e-96

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 283.38  E-value: 5.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   16 KGIILAGGTGSRLYPITRGVSKQLLPVYDK-PMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQ 94
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   95 SKPEGIAQAFLIGEDFIGNDKV-ALILGDNIFYGQSFSRQLQQAADCS--LGATVFAYHVTNPERFGVVEFDNTGRAVSI 171
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  172 EEKPREPK-SHYAVTGLYFYDNQVIEF-AKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGH 249
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 119767875  250 FV 251
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
16-300 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 540.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:COG1209    2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:COG1209   82 EPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEKP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTIE 255
Cdd:COG1209  162 KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 119767875 256 KRQGLKIACLEEIAYRNGWISTETLLQHAKALSQSGYGDYLRQLV 300
Cdd:COG1209  242 KRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLL 286
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 16-299 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: 526.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTIE 255
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 119767875  256 KRQGLKIACLEEIAYRNGWISTETLLQHAKALSQSGYGDYLRQL 299
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRL 284
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 16-254 1.13e-166

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: 462.04  E-value: 1.13e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:cd02538    2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:cd02538   82 KPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEKP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119767875 176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTI 254
Cdd:cd02538  162 KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 16-300 2.82e-141

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 400.20  E-value: 2.82e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGHFVQTIE 255
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 119767875 256 KRQGLKIACLEEIAYRNGWISTETLLQHAKALSQSGYGDYLRQLV 300
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 16-251 5.56e-96

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 283.38  E-value: 5.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   16 KGIILAGGTGSRLYPITRGVSKQLLPVYDK-PMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQ 94
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   95 SKPEGIAQAFLIGEDFIGNDKV-ALILGDNIFYGQSFSRQLQQAADCS--LGATVFAYHVTNPERFGVVEFDNTGRAVSI 171
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  172 EEKPREPK-SHYAVTGLYFYDNQVIEF-AKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFAWLDTGTHDALMEAGH 249
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 119767875  250 FV 251
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 16-247 2.02e-71

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 220.52  E-value: 2.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIsTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:cd04189    2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIV-VGPTGEEIKEALGDGSRFGVRITYILQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYG---QSFSRQLQQAADCSLGATvfayHVTNPERFGVVEFDNtGRAVSIE 172
Cdd:cd04189   81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEgisPLVRDFLEEDADASILLA----EVEDPRRFGVAVVDD-GRIVRLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119767875 173 EKPREPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGFaWLDTGTHDALMEA 247
Cdd:cd04189  156 EKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEA 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 17-239 1.93e-59

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 189.33  E-value: 1.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  17 GIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIsTASDLAGFQSLLGDGSGLGIRISYAVQSK 96
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILV-VGYLGEQIEEYFGDGSKFGVNIEYVVQEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  97 PEGIAQAFLIGEDFIGNDKVALILGDNIFYGqSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKPR 176
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119767875 177 EPKSHYAVTGLYFYDNQVIEFAKSLRPsaRGELEITDINNAYLAANQLQVsVLGRGFaWLDTG 239
Cdd:cd04181  159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 16-263 4.25e-57

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 187.61  E-value: 4.25e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLAGFQSLLGDGSGLGIRISYAVQS 95
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   96 KPEGIAQAFLIGEDFIGNDKVALILGDNIFYGqSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEKP 175
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  176 REPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITD-----INNAYLAANQLqvsVLGrgfAWLDTGTHDALMEAGHF 250
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDaiqwlIEKGYKVGGSK---VTG---WWKDTGKPEDLLDANRL 233

                         250
                  ....*....|....*
gi 119767875  251 V-QTIEKR-QGLKIA 263
Cdd:TIGR01208 234 IlDEVEREvQGVDDE 248
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 16-247 7.00e-45

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: 152.23  E-value: 7.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLisTASDLAG-FQSLLGDGSGLGIRISYAVQ 94
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVI--NVGYLAEqIEEYFGDGSRFGVRITYVDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  95 SKPEGIAQAFLIGEDFIGNDKVALILGDnIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRAVSIEEK 174
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119767875 175 PREPKSHYAVTGLYFYDNQVIEFAKslrpsARGELEITDINNAYLAANQLQVSVLgRGFaWLDTGTHDALMEA 247
Cdd:COG1208  158 PEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 15-239 1.11e-43

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: 153.52  E-value: 1.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   15 TKGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIstasdlAGF-----QSLLGDGSGLGIRI 89
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFV------VGYgkekvREYFGDGSRGGVPI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   90 SYAVQSKPEGIAQAFLIGEDFIgNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVfayhvTNPERFGVVEFDNtGRAV 169
Cdd:TIGR03992  75 EYVVQEEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLIRAEAPAIAVVEV-----DDPSDYGVVETDG-GRVT 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  170 SIEEKPREPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGRGfaWLDTG 239
Cdd:TIGR03992 148 GIVEKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 15-247 2.00e-28

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: 109.93  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  15 TKGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIS------------TASDL------AGFQ 76
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTgrgkraiedhfdRSYELeetlekKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  77 SLLGDGSGL--GIRISYAVQSKPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSF-SRQLQQAADcSLGATVFAYHVTN 153
Cdd:cd02541   81 DLLEEVRIIsdLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYE-KTGASVIAVEEVP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 154 PE---RFGVVEF----DNTGRAVSIEEKPR--EPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDinnaylAANQL 224
Cdd:cd02541  160 PEdvsKYGIVKGekidGDVFKVKGLVEKPKpeEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTD------AIAKL 233

                        250       260
                 ....*....|....*....|....*..
gi 119767875 225 --QVSVLGRGF--AWLDTGTHDALMEA 247
Cdd:cd02541  234 leEEPVYAYVFegKRYDCGNKLGYLKA 260
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 18-247 9.02e-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: 91.03  E-value: 9.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDIlLISTasdlaGF-----QSLLGDGSGLGIRISYA 92
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISV-----NYlaemiEDYFGDGSKFGVNISYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  93 VQSKPEGIAQAF-LIGEDFigNDKVALILGD---NIFYGQSFSRQLQQAADCSLGATVfaYHVTNPerFGVVEFDNtGRA 168
Cdd:cd06426   76 REDKPLGTAGALsLLPEKP--TDPFLVMNGDiltNLNYEHLLDFHKENNADATVCVRE--YEVQVP--YGVVETEG-GRI 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119767875 169 VSIEEKPREpkSHYAVTGLYFYDNQVIEfakSLRPSARgeLEITDINNAYLAANQLQVSVLGRGFaWLDTGTHDALMEA 247
Cdd:cd06426  149 TSIEEKPTH--SFLVNAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
15-247 6.15e-20

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 87.40  E-value: 6.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  15 TKGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYplSV--LMLAGIRDILLIS------------TASDL------AG 74
Cdd:COG1210    4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTgrgkraiedhfdRSYELeatleaKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  75 FQSLLG--DGSGLGIRISYAVQSKPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQ-SFSRQLQQAADcSLGATVFAYHV 151
Cdd:COG1210   82 KEELLEevRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkPCLKQMIEVYE-ETGGSVIAVQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 152 TNPE---RFGVVE----FDNTGRAVSIEEKPR--EPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITD-InnAYLAA 221
Cdd:COG1210  161 VPPEevsKYGIVDgeeiEGGVYRVTGLVEKPApeEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDaI--AALAK 238

                        250       260
                 ....*....|....*....|....*...
gi 119767875 222 NQlqvSVLGRGFA--WLDTGTHDALMEA 247
Cdd:COG1210  239 EE---PVYAYEFEgkRYDCGDKLGYLKA 263
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 16-240 7.94e-20

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 86.11  E-value: 7.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILL-IS-TASDLAGFQSLLGDgsGLGIRISYAV 93
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNyRPEDMVPFLKEYEK--KLGIKITFSI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  94 QSKPEGIAQAFLIGEDFI-GNDKVALILGDNIFYGQSFSRQLQ--QAADCSlgATVFAYHVTNPERFGVVEFD-NTGRAV 169
Cdd:cd06425   80 ETEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDfhKKHGAE--GTILVTKVEDPSKYGVVVHDeNTGRIE 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119767875 170 SIEEKPREPKSHYAVTGLYFYDNQVIEFAKsLRPSargELEiTDINNAYLAANQLQVSVLgRGFaWLDTGT 240
Cdd:cd06425  158 RFVEKPKVFVGNKINAGIYILNPSVLDRIP-LRPT---SIE-KEIFPKMASEGQLYAYEL-PGF-WMDIGQ 221
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 18-188 3.90e-19

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: 84.14  E-value: 3.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILListasdLAGF-----QSLLGDGSGLGIRISYA 92
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVL------SVGYlaeqiEEYFGDGYRGGIRIYYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  93 VQSKPEGIAQAFLIGEDFIGNDKVALILGDNIF---YGQSFSRQLQQAADcslgATVFAYHVTNPERFGVVEFDNTGRAV 169
Cdd:cd06915   76 IEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFdvdLLALLAALRASGAD----ATMALRRVPDASRYGNVTVDGDGRVI 151

                        170
                 ....*....|....*....
gi 119767875 170 SIEEKPREPKSHYAVTGLY 188
Cdd:cd06915  152 AFVEKGPGAAPGLINGGVY 170
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 17-191 1.13e-16

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 79.35  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  17 GIILAGGTGSRLYPITRGVSKqllpvydkPMVYY---------PLSVLMLAGIRDILListasdLAGFQSL-----LGDG 82
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGV------LTQYKSHslndhIGSG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  83 S--GL-----GIRISYAVQSKP-----EGIAQAFLIGEDFI--GNDKVALIL-GDNIF---YGQSFSRQLQQAADCslga 144
Cdd:COG0448   70 KpwDLdrkrgGVFILPPYQQREgedwyQGTADAVYQNLDFIerSDPDYVLILsGDHIYkmdYRQMLDFHIESGADI---- 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119767875 145 TVFAYHVTNPE--RFGVVEFDNTGRAVSIEEKPREPKSHYAVTGLYFYD 191
Cdd:COG0448  146 TVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
8-213 9.60e-15

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 73.02  E-value: 9.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   8 SAFNTQKTKGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASD---------------- 71
Cdd:PRK13389   2 AAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKnsienhfdtsfeleam 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  72 ---------LAGFQSLLGDgsglGIRISYAVQSKPEGIAQAFLIGEDFIGNDKVALILGDNIF--YGQSFSR----QLQQ 136
Cdd:PRK13389  82 lekrvkrqlLDEVQSICPP----HVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQdnlaEMIR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 137 AADCSLGATVFAYHVTNPERFGVVEFD----NTGRA---VSIEEKPR--EPKSHYAVTGLYFYDNQVIEFAKSLRPSARG 207
Cdd:PRK13389 158 RFDETGHSQIMVEPVADVTAYGVVDCKgvelAPGESvpmVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGD 237


                 ....*.
gi 119767875 208 ELEITD 213
Cdd:PRK13389 238 EIQLTD 243
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 16-247 2.48e-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: 70.68  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDIllISTASDLAG-FQSLLGD-GSGLGIRISYav 93
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI--VVNTHHLADqIEAHLGDsRFGLRITISD-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  94 qskpE---------GIAQAfligEDFIGNDKVALILGDnIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEF-- 162
Cdd:cd06422   77 ----EpdelletggGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFsl 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 163 DNTGRavsIEEKPREPKSHYAVTGLYFYDNQVIEFAKslrpsaRGELEITDINNAYLAANQLQVSVLgRGFaWLDTGTHD 242
Cdd:cd06422  148 DADGR---LRRGGGGAVAPFTFTGIQILSPELFAGIP------PGKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPE 216


                 ....*
gi 119767875 243 ALMEA 247
Cdd:cd06422  217 RLLAA 221
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 16-66 3.24e-14

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: 70.38  E-value: 3.24e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLI 66
Cdd:cd04198    2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVV 52
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
14-247 6.62e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 64.91  E-value: 6.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  14 KTKGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLISTASDLA---GF--------------- 75
Cdd:PRK10122   3 NLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAvenHFdtsyeleslleqrvk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  76 QSLLGDGSGL---GIRISYAVQSKPEGIAQAFLIGEDFIGNDKVALILGDNIFYGQSFS--RQLQQAADCSLGAT----V 146
Cdd:PRK10122  83 RQLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADplRYNLAAMIARFNETgrsqV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 147 FAYHVTNP-ERFGVVE----FDNTG---RAVSIEEKPREPK---SHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDIn 215
Cdd:PRK10122 163 LAKRMPGDlSEYSVIQtkepLDREGkvsRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDA- 241

                        250       260       270
                 ....*....|....*....|....*....|..
gi 119767875 216 NAYLAANQLQVSVLGRGFAWlDTGTHDALMEA 247
Cdd:PRK10122 242 IAELAKKQSVDAMLMTGDSY-DCGKKMGYMQA 272
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 18-247 2.31e-11

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 62.25  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIstasdlAGFQS-----LLGDgsglGIRISYA 92
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIV------TGYKKeqieeLLKK----YPNIKFV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  93 VQSKPE--GIAQAFLIGEDFIGNDkVALILGDNIFYgqsfSRQLQQAADCSLGATVFAYHVTNPERFGVVE-FDNTGRAV 169
Cdd:cd02523   72 YNPDYAetNNIYSLYLARDFLDED-FLLLEGDVVFD----PSILERLLSSPADNAILVDKKTKEWEDEYVKdLDDAGVLL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 170 SIEEKPREPKS-HYAVTGLYFYDNQ----VIEFAKSLRPSARGELEITDINNAYLAANQLQVSVLGrGFAWLDTGTHDAL 244
Cdd:cd02523  147 GIISKAKNLEEiQGEYVGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDL 225


                 ...
gi 119767875 245 MEA 247
Cdd:cd02523  226 ERA 228
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 16-66 2.93e-11

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: 61.89  E-value: 2.93e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLI 66
Cdd:cd02507    2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
16-247 1.93e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 59.87  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIStasdlaGFQSLLGDG--SGLGIRISYAV 93
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT------GYKAELIEEalARPGPDVTFVY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  94 QSKPE--GIAQAFLIGEDFIGNDkVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFgvVEFDNTGRAVSI 171
Cdd:COG1213   75 NPDYDetNNIYSLWLAREALDED-FLLLNGDVVFDPAILKRLLASDGDIVLLVDRKWEKPLDEEVK--VRVDEDGRIVEI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 172 EEKPREPKSHYAVTGLYFYDNQ----VIEFAKSLRPSARGELEITDINNAyLAANQLQVSVLG-RGFAWLDTGTHDALME 246
Cdd:COG1213  152 GKKLPPEEADGEYIGIFKFSAEgaaaLREALEALIDEGGPNLYYEDALQE-LIDEGGPVKAVDiGGLPWVEIDTPEDLER 230


                 .
gi 119767875 247 A 247
Cdd:COG1213  231 A 231
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 12-180 4.21e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 57.16  E-value: 4.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  12 TQKTKGIILAGGTGSRLYPITRGVSkqllpvydKPMVY---------YPLSVLMLAGIRDILLIStasdlagfQ----SL 78
Cdd:PRK00725  13 TRDTLALILAGGRGSRLKELTDKRA--------KPAVYfggkfriidFALSNCINSGIRRIGVLT--------QykahSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  79 ---LGDGSG-----LG--IRISYAVQSKPE-----GIAQAFLIGEDFIG--NDKVALIL-GDNIfYGQSFSRQLQQ---- 136
Cdd:PRK00725  77 irhIQRGWSffreeLGefVDLLPAQQRVDEenwyrGTADAVYQNLDIIRryDPKYVVILaGDHI-YKMDYSRMLADhves 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119767875 137 AADCslgaTVFAYHVTNPE--RFGVVEFDNTGRAVSIEEKPREPKS 180
Cdd:PRK00725 156 GADC----TVACLEVPREEasAFGVMAVDENDRITAFVEKPANPPA 197
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 18-214 2.44e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.84  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTG----SRLYpitrgvsKQLLPVYDKPMVYYPLSVLMLAGIRDILLIstasdlagfqslLGDGSG-----LGIR 88
Cdd:PRK14354   6 IILAAGKGtrmkSKLP-------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGAEevkevLGDR 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  89 ISYAVQSKPEGIAQAFLIGEDFIGNDK--VALILGDN-IFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNT 165
Cdd:PRK14354  67 SEFALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119767875 166 GRAVSI-EEK---PREPKSHYAVTGLYFYDNQVIEFA-KSLRP-SARGELEITDI 214
Cdd:PRK14354 147 GEVEKIvEQKdatEEEKQIKEINTGTYCFDNKALFEAlKKISNdNAQGEYYLTDV 201
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 18-214 4.40e-08

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 52.90  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTGSRL---YPitrgvsKQLLPVYDKPMVYYPLSVLMLAGIRDILLIstasdlAGFQSLLGDGSGLGIRISYAVQ 94
Cdd:cd02540    2 VILAAGKGTRMksdLP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------VGHGAEQVKKALANPNVEFVLQ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  95 SKPEGIAQAFLIGEDFIG--NDKVaLILgdnifYG-------QSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNT 165
Cdd:cd02540   70 EEQLGTGHAVKQALPALKdfEGDV-LVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGN 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119767875 166 GRAVSI-EEK---PREPKSHYAVTGLYFYDNQVIEFA-KSLRPS-ARGELEITDI 214
Cdd:cd02540  144 GKVLRIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI 198
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 17-247 2.62e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 51.41  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  17 GIILAGGTGSRLYPITRGVSKqllpvydkPMVYY---------PLSVLMLAGIRDILLISTASDLAgFQSLLGDGS---- 83
Cdd:PRK05293   6 AMILAGGQGTRLGKLTKNIAK--------PAVPFggkyriidfTLSNCANSGIDTVGVLTQYQPLE-LNNHIGIGSpwdl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  84 -----GLGIRISYAVQSKP---EGIAQAFLIGEDFIG--NDKVALIL-GDNIF---YGQSFSRQLQQAADcslgATVFAY 149
Cdd:PRK05293  77 dringGVTILPPYSESEGGkwyKGTAHAIYQNIDYIDqyDPEYVLILsGDHIYkmdYDKMLDYHKEKEAD----VTIAVI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 150 HVTNPE--RFGVVEFDNTGRAVSIEEKPREPKSHYAVTGLYFYDNQVIEfaKSLRPSARGELEITD----INNAYLAANQ 223
Cdd:PRK05293 153 EVPWEEasRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLK--EYLIEDEKNPNSSHDfgknVIPLYLEEGE 230

                        250       260
                 ....*....|....*....|....
gi 119767875 224 LQVSVLGRGFaWLDTGTHDALMEA 247
Cdd:PRK05293 231 KLYAYPFKGY-WKDVGTIESLWEA 253
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 18-81 3.66e-06

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 47.05  E-value: 3.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119767875  18 IILAGGTGSRLypiTRGVSKQLLPVYDKPMVYYPLSVLMLAG-IRDILLISTASDLAGFQSLLGD 81
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 17-180 6.27e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 47.13  E-value: 6.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  17 GIILAGGTGSRLYPITRGVSKQLLP---VYDkpMVYYPLSVLMLAGIRDILL------------ISTASDLAGfqsLLGd 81
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhISQTWRLSG---LLG- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  82 gsglgiriSYaVQSKP----------EGIAQAFLIGEDFIGNDK---VALILGDNIfYGQSFSRQLQQAADCSLGATVFA 148
Cdd:PRK00844  82 --------NY-ITPVPaqqrlgkrwyLGSADAIYQSLNLIEDEDpdyVVVFGADHV-YRMDPRQMVDFHIESGAGVTVAA 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 119767875 149 YHVTNPE--RFGVVEFDNTGRAVSIEEKPREPKS 180
Cdd:PRK00844 152 IRVPREEasAFGVIEVDPDGRIRGFLEKPADPPG 185
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 18-214 7.24e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 47.05  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTGSRLypiTRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIstasdlAGFQS------LLGDGSglgirISY 91
Cdd:PRK14355   7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLV------VGHQAekvrehFAGDGD-----VSF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  92 AVQSKPEGIAQAFLIGEDFI--GNDKVALILGDN-IFYGQSFSRQLQQAADCSLGATVFAYHVTNPERFGVVEFDNTGRA 168
Cdd:PRK14355  73 ALQEEQLGTGHAVACAAPALdgFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119767875 169 VSI-EEK---PREPKSHYAVTGLYFYDNQVIEFA-KSLR-PSARGELEITDI 214
Cdd:PRK14355 153 LRIvEEKdatPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDI 204
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 18-220 7.86e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 46.90  E-value: 7.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTGSRLypiTRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIsTASDLAGFQSLLgDGSGlgirISYAVQSKP 97
Cdd:PRK14358  11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVV-TGHGAEQVEAAL-QGSG----VAFARQEQQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  98 EGIAQAFLIGEDFI--GNDKVALILGDNIFYGQSFSRQLQQAADCSLGA-TVFAYHVTNPERFGVVEFDNTGRAVSIEEK 174
Cdd:PRK14358  82 LGTGDAFLSGASALteGDADILVLYGDTPLLRPDTLRALVADHRAQGSAmTILTGELPDATGYGRIVRGADGAVERIVEQ 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119767875 175 PREPKSHYAV----TGLYFYDNQVIEFAKSL-RPSARGELEITDINNAYLA 220
Cdd:PRK14358 162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRA 212
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 18-190 1.88e-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: 44.94  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  18 IILAGGTGSRLYPITRGVSKQLLPVYDKPMVYYplSVLMLAGIRD--ILLISTASDLAGF---QSLLGDGSGLGIrisYA 92
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrFIFICRDEHNTKFhldESLKLLAPNATV---VE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  93 VQSKPEGIAQAFLIGEDFIGNDKVALIL-GDNIF-YGQSFSRQLQQAADCSLGA-TVFAYHvtnpERFGVVEFDNTGRAV 169
Cdd:cd04183   77 LDGETLGAACTVLLAADLIDNDDPLLIFnCDQIVeSDLLAFLAAFRERDLDGGVlTFFSSH----PRWSYVKLDENGRVI 152

                        170       180
                 ....*....|....*....|.
gi 119767875 170 SIEEKprEPKSHYAVTGLYFY 190
Cdd:cd04183  153 ETAEK--EPISDLATAGLYYF 171
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 18-89 2.40e-05

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 44.44  E-value: 2.40e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119767875  18 IILAGGTGSRLypiTRGVSKQLLPVYDKPMVYYPLSVLM-LAGIRDILLISTASDLAGFQSLLGDGSGLGIRI 89
Cdd:cd02516    4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 17-146 2.91e-05

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 44.07  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  17 GIILAGGTGSRLYPITRGVSKQLLPVYDKpmvY----YPLSVLMLAGIRDILLISTASdlagFQSLL----------GDG 82
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR---YrlidFPLSNMVNSGIRNVGVLTQYK----SRSLNdhlgsgkewdLDR 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119767875  83 SGLGIRISYAVQSKP----EGIAQAFLIGEDFI---GNDKVALILGDNIF---YGQSFSRQLQQAADCSLGATV 146
Cdd:cd02508   74 KNGGLFILPPQQRKGgdwyRGTADAIYQNLDYIersDPEYVLILSGDHIYnmdYREMLDFHIESGADITVVYKA 147
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 17-216 3.84e-05

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 44.17  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  17 GIILAGG--TGSRLYPITRGVSKQLLPVYDKPMVYYPLSVL-MLAGIRDILLISTASDLAgFQSLLGDGSG-LGIRISYA 92
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQQeFNVPIRYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  93 VQSKPEGIAQAFLIGEDFI--GNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAyhvTNPER-----FG-VVEFDN 164
Cdd:cd06428   80 QEYKPLGTAGGLYHFRDQIlaGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILG---TEASReqasnYGcIVEDPS 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119767875 165 TGRAVSIEEKPREPKSHYAVTGLYFYDNQVIEFAKSLRPSARGELEITDINN 216
Cdd:cd06428  157 TGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNN 208
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
18-79 6.65e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 43.20  E-value: 6.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119767875  18 IILAGGTGSRLYPitrGVSKQLLPVYDKPMVYYPLSVLMLAG-IRDILLISTASDLAGFQSLL 79
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 13-214 1.61e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 43.09  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  13 QKTKGIILAGGTGSRLY---PitrgvsKQLLPVYDKPMVYYPLSVLMLAGIRDILLIstasdlAGFQ-----SLLGDgsg 84
Cdd:COG1207    1 SPLAVVILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------VGHGaeqvrAALAD--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  85 lgIRISYAVQSKPEGIAQAFLIGEDFIGNDK-VALILgdnifYG-------QSFSRQLQQAADCSLGATVFAYHVTNPER 156
Cdd:COG1207   66 --LDVEFVLQEEQLGTGHAVQQALPALPGDDgTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTG 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119767875 157 FGVVEFDNTGRAVSI-EEK---PREPKSHYAVTGLYFYDNQVIEFA-KSLRPS-ARGELEITDI 214
Cdd:COG1207  139 YGRIVRDEDGRVLRIvEEKdatEEQRAIREINTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV 202
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 14-177 1.97e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 42.56  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  14 KTKGIILAGGTGSRLYPITRGVSKQLLPVYDK-PMVYYPLSVLMLAGIRDILLIS---TASdL--------------AGF 75
Cdd:PRK02862   3 RVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLTqfnSAS-LnrhisqtynfdgfsGGF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  76 QSLLgdgsglgirisyAVQSKPE------GIAQA-----FLIGEDFIGNdkvALIL-GDNIF---YGQSFSRQLQQAADC 140
Cdd:PRK02862  82 VEVL------------AAQQTPEnpswfqGTADAvrkylWHFQEWDVDE---YLILsGDQLYrmdYRLFVQHHRETGADI 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119767875 141 SLGAT-VFAYhvtNPERFGVVEFDNTGRAVSIEEKPRE 177
Cdd:PRK02862 147 TLAVLpVDEK---DASGFGLMKTDDDGRITEFSEKPKG 181
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 17-150 2.14e-04

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 41.03  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875   17 GIILAGGTGSRLypitrGVSKQLLPVYDKPMVYYplSVLMLAGIRDILLISTasdlaGFQSLLGDGSGLGIRIsYAVQSK 96
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLER--VLERLRPAGDEVVVVA-----NDEEVLAALAGLGVPV-VPDPDP 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119767875   97 PEGIAQAFLIGEDFI-GNDKVALILGDNIFYGQSFSRQLQQAADCSLGATVFAYH 150
Cdd:pfam12804  68 GQGPLAGLLAALRAApGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVY 122
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
14-66 3.47e-04

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 40.91  E-value: 3.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119767875  14 KTKGIILAGGTGSRLypitrGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLI 66
Cdd:COG2068    3 KVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV 50
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 12-55 3.50e-04

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: 40.56  E-value: 3.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 119767875  12 TQKTKGIILAGGTGSRLypitrGVSKQLLPVYDKPMVYYPLSVL 55
Cdd:COG0746    2 TMPITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERL 40
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 17-67 1.36e-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: 39.08  E-value: 1.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119767875  17 GIILAGGTGSRLypitrGVSKQLLPVYDKPMVYYPLSVLMLAGIRDILLIS 67
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVL 48
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-214 1.62e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 39.71  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  11 NTQKTKGIILAGGTGSRLYPITRGVSKQLLpvyDKPMVYYPLSVLmlagirDILLISTASDLAGFQSLLGDGSGLGIRIS 90
Cdd:PRK14356   2 MASTTGALILAAGKGTRMHSDKPKVLQTLL---GEPMLRFVYRAL------RPLFGDNVWTVVGHRADMVRAAFPDEDAR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875  91 YAVQSKPEGIAQAFLIGEDFI---GNDKVALILGDN-IFYGQSFSRQLQQAADCSLG-ATVfayHVTNPERFG-VVEFDN 164
Cdd:PRK14356  73 FVLQEQQLGTGHALQCAWPSLtaaGLDRVLVVNGDTpLVTTDTIDDFLKEAAGADLAfMTL---TLPDPGAYGrVVRRNG 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119767875 165 TGRAVsIEEKPREPKSHYAVT-----GLYFYDNQVIEfakSLRP-----SARGELEITDI 214
Cdd:PRK14356 150 HVAAI-VEAKDYDEALHGPETgevnaGIYYLRLDAVE---SLLPrltnaNKSGEYYITDL 205
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 20-64 1.83e-03

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: 38.72  E-value: 1.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119767875  20 LAGGTGSRLypitRGVSKQLLPVYDKPMVYYPLSVLMLAGIRDIL 64
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIY 41
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 16-44 1.86e-03

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: 39.10  E-value: 1.86e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 119767875  16 KGIILAGGTGSRLYPITR-GVSKQLLPVYD 44
Cdd:cd02509    2 YPVILAGGSGTRLWPLSReSYPKQFLKLFG 31
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 17-47 1.92e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 39.45  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 119767875  17 GIILAGGTGSRLYPITRGVSKQLLPV---Y---DKPM 47
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYrliDIPM 42
 
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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