WECD_ECOLI
ID WECD_ECOLI Reviewed; 224 AA.
AC P27832; Q2M898; Q6BF00;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=dTDP-fucosamine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_02027};
DE EC=2.3.1.210 {ECO:0000255|HAMAP-Rule:MF_02027};
DE AltName: Full=TDP-fucosamine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_02027};
DE AltName: Full=dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase {ECO:0000255|HAMAP-Rule:MF_02027};
GN Name=wecD {ECO:0000255|HAMAP-Rule:MF_02027};
GN Synonyms=rffC {ECO:0000303|PubMed:8366065}, yifH;
GN OrderedLocusNames=b3790, JW5597;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP SEQUENCE REVISION TO 187.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION.
RX PubMed=8366065; DOI=10.1128/jb.175.17.5738-5739.1993;
RA Barr K., Rick P.D.;
RT "Physical map location of the rffC and rffA genes of Escherichia coli.";
RL J. Bacteriol. 175:5738-5739(1993).
CC -!- FUNCTION: Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino-
CC 4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the
CC biosynthesis of the enterobacterial common antigen (ECA).
CC {ECO:0000255|HAMAP-Rule:MF_02027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose = CoA
CC + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose + H(+);
CC Xref=Rhea:RHEA:34443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:68492, ChEBI:CHEBI:68493;
CC EC=2.3.1.210; Evidence={ECO:0000255|HAMAP-Rule:MF_02027};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02027}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02027}.
CC -!- SIMILARITY: Belongs to the WecD family. {ECO:0000255|HAMAP-
CC Rule:MF_02027}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67590.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77508.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M87049; AAA67590.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAT48214.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77508.1; ALT_INIT; Genomic_DNA.
DR PIR; A65183; A65183.
DR RefSeq; WP_001145183.1; NZ_SSZK01000025.1.
DR RefSeq; YP_026256.2; NC_000913.3.
DR AlphaFoldDB; P27832; -.
DR SMR; P27832; -.
DR BioGRID; 4261646; 249.
DR STRING; 511145.b3790; -.
DR PaxDb; P27832; -.
DR PRIDE; P27832; -.
DR EnsemblBacteria; AAT48214; AAT48214; b3790.
DR EnsemblBacteria; BAE77508; BAE77508; BAE77508.
DR GeneID; 948298; -.
DR KEGG; ecj:JW5597; -.
DR KEGG; eco:b3790; -.
DR PATRIC; fig|511145.12.peg.3906; -.
DR EchoBASE; EB1424; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_101319_1_0_6; -.
DR OMA; TAYWFYR; -.
DR PhylomeDB; P27832; -.
DR BioCyc; EcoCyc:TDPFUCACTRANS-MON; -.
DR BioCyc; MetaCyc:TDPFUCACTRANS-MON; -.
DR UniPathway; UPA00566; -.
DR PRO; PR:P27832; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IDA:EcoCyc.
DR HAMAP; MF_02027; WecD_RffC; 1.
DR InterPro; IPR012752; AcTrfase_WecD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR000182; GNAT_dom.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR02382; wecD_rffC; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..224
FT /note="dTDP-fucosamine acetyltransferase"
FT /id="PRO_0000067230"
FT DOMAIN 94..224
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027"
FT BINDING 168..174
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027"
FT BINDING 201
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027"
FT BINDING 207
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027"
FT CONFLICT 187
FT /note="A -> R (in Ref. 1; AAA67590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24220 MW; A1B196D4DA00321B CRC64;
MPVRASIEPL TWENAFFGVN SAIVRITSEA PLLTPDALAP WSRVQAKIAA SNTGELDALQ
QLGFSLVEGE VDLALPVNNA SDSGAVVAQE TDIPALRQLA SAAFAQSRFR APWYAPDASS
RFYAQWIENA VRGTFDHQCL ILRAASGDIR GYVSLRELNA TDARIGLLAG RGAGAELMQT
ALNWAYARGK TTLRVATQMG NTAALKRYIQ SGANVESTAY WLYR
