NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2259688705|ref|WP_252403813|]
View 

sugar phosphate nucleotidyltransferase, partial [Escherichia coli]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RmlA1 super family cl43356
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-103 2.11e-58

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


The actual alignment was detected with superfamily member COG1209:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 181.06  E-value: 2.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTIEKRQGMKVACLEEIAYRNDWLSAEGV 80
Cdd:COG1209   187 LKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIEKRQGLKIACPEEIAYRMGWIDAEQL 266

                          90       100
                  ....*....|....*....|...
gi 2259688705  81 AAQAERLKKTEYGAYLKRLLNER 103
Cdd:COG1209   267 AKLANSLEKSGYGPYLLRLLDSN 289
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-103 2.11e-58

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 181.06  E-value: 2.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTIEKRQGMKVACLEEIAYRNDWLSAEGV 80
Cdd:COG1209   187 LKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIEKRQGLKIACPEEIAYRMGWIDAEQL 266

                          90       100
                  ....*....|....*....|...
gi 2259688705  81 AAQAERLKKTEYGAYLKRLLNER 103
Cdd:COG1209   267 AKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 1-100 1.17e-57

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: 178.74  E-value: 1.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTIEKRQGMKVACLEEIAYRNDWLSAEGV 80
Cdd:TIGR01207 186 LKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIEKRQGLKVACPEEIAWRNGWIDDEQL 265

                          90       100
                  ....*....|....*....|
gi 2259688705  81 AAQAERLKKTEYGAYLKRLL 100
Cdd:TIGR01207 266 EELARPLAKNGYGQYLLRLL 285
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 1-100 9.44e-39

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 130.56  E-value: 9.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTIEKRQGMKVACLEEIAYRNDWLSAEGV 80
Cdd:PRK15480  190 LKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEEIAFRKGFIDAEQV 269

                          90       100
                  ....*....|....*....|
gi 2259688705  81 AAQAERLKKTEYGAYLKRLL 100
Cdd:PRK15480  270 KVLAEPLKKNAYGQYLLKMI 289
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-54 1.83e-30

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: 108.05  E-value: 1.83e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTI 54
Cdd:cd02538   187 LKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-52 2.52e-15

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: 68.43  E-value: 2.52e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2259688705   3 PSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIH 52
Cdd:pfam00483 194 ELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANLFLL 243
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-103 2.11e-58

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 181.06  E-value: 2.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTIEKRQGMKVACLEEIAYRNDWLSAEGV 80
Cdd:COG1209   187 LKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTIEKRQGLKIACPEEIAYRMGWIDAEQL 266

                          90       100
                  ....*....|....*....|...
gi 2259688705  81 AAQAERLKKTEYGAYLKRLLNER 103
Cdd:COG1209   267 AKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 1-100 1.17e-57

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: 178.74  E-value: 1.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTIEKRQGMKVACLEEIAYRNDWLSAEGV 80
Cdd:TIGR01207 186 LKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIEKRQGLKVACPEEIAWRNGWIDDEQL 265

                          90       100
                  ....*....|....*....|
gi 2259688705  81 AAQAERLKKTEYGAYLKRLL 100
Cdd:TIGR01207 266 EELARPLAKNGYGQYLLRLL 285
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 1-100 9.44e-39

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 130.56  E-value: 9.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTIEKRQGMKVACLEEIAYRNDWLSAEGV 80
Cdd:PRK15480  190 LKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEEIAFRKGFIDAEQV 269

                          90       100
                  ....*....|....*....|
gi 2259688705  81 AAQAERLKKTEYGAYLKRLL 100
Cdd:PRK15480  270 KVLAEPLKKNAYGQYLLKMI 289
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-54 1.83e-30

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: 108.05  E-value: 1.83e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2259688705   1 VTPSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIHTI 54
Cdd:cd02538   187 LKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-52 2.52e-15

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: 68.43  E-value: 2.52e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2259688705   3 PSERGELEITTLNQMYLDRGDLQVELLGRGFAWLDTGTHDSLIEASQFIH 52
Cdd:pfam00483 194 ELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANLFLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 2-51 1.58e-07

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: 47.18  E-value: 1.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2259688705   2 TPSERGELEITTLNQMYLDRG-DLQVELLgRGFaWLDTGTHDSLIEASQFI 51
Cdd:cd04189   185 KPSWRGELEITDAIQWLIDRGrRVGYSIV-TGW-WKDTGTPEDLLEANRLL 233
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 3-63 4.73e-07

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: 46.24  E-value: 4.73e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2259688705   3 PSERGELEITTLNQMYLDRGDLQVELLGRGFaWLDTGTHDSLIEASQFI-HTIEKR-QGMKVA 63
Cdd:TIGR01208 187 PSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIlDEVEREvQGVDDE 248
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH