WECD_ECOL6
ID WECD_ECOL6 Reviewed; 224 AA.
AC Q8FBQ3;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=dTDP-fucosamine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_02027, ECO:0000305};
DE EC=2.3.1.210 {ECO:0000255|HAMAP-Rule:MF_02027, ECO:0000269|PubMed:16855251};
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, ECO:0000303|PubMed:16855251};
GN OrderedLocusNames=c4710;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 2-224 OF APOENZYME AND IN COMPLEX
RP WITH ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACTIVE SITE, AND
RP SUBUNIT.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=16855251; DOI=10.1128/jb.00306-06;
RA Hung M.N., Rangarajan E., Munger C., Nadeau G., Sulea T., Matte A.;
RT "Crystal structure of TDP-fucosamine acetyltransferase (WecD) from
RT Escherichia coli, an enzyme required for enterobacterial common antigen
RT synthesis.";
RL J. Bacteriol. 188:5606-5617(2006).
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, ECO:0000269|PubMed:16855251}.
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 ECO:0000269|PubMed:16855251};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02027,
CC ECO:0000305|PubMed:16855251}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02027,
CC ECO:0000269|PubMed:16855251}.
CC -!- SIMILARITY: Belongs to the WecD family. {ECO:0000255|HAMAP-
CC Rule:MF_02027, ECO:0000305}.
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DR EMBL; AE014075; AAN83143.1; -; Genomic_DNA.
DR RefSeq; WP_001145189.1; NC_004431.1.
DR PDB; 2FS5; X-ray; 1.95 A; A/B=2-224.
DR PDB; 2FT0; X-ray; 1.66 A; A/B=2-224.
DR PDBsum; 2FS5; -.
DR PDBsum; 2FT0; -.
DR AlphaFoldDB; Q8FBQ3; -.
DR SMR; Q8FBQ3; -.
DR STRING; 199310.c4710; -.
DR EnsemblBacteria; AAN83143; AAN83143; c4710.
DR KEGG; ecc:c4710; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_101319_1_0_6; -.
DR OMA; TAYWFYR; -.
DR BioCyc; ECOL199310:C4710-MON; -.
DR BRENDA; 2.3.1.210; 2026.
DR UniPathway; UPA00566; -.
DR EvolutionaryTrace; Q8FBQ3; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Transferase.
FT CHAIN 1..224
FT /note="dTDP-fucosamine acetyltransferase"
FT /id="PRO_0000421036"
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 ECO:0000305|PubMed:16855251"
FT BINDING 168..174
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027,
FT ECO:0000269|PubMed:16855251"
FT BINDING 201
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027,
FT ECO:0000269|PubMed:16855251"
FT BINDING 207
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02027,
FT ECO:0000269|PubMed:16855251"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 65..76
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:2FT0"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2FT0"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:2FT0"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:2FT0"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:2FT0"
SQ SEQUENCE 224 AA; 24218 MW; C836AD32CF146BA8 CRC64;
MPVRASIEPL TWENAFFGVN SAIVRITSEA PLLTPDALAP WSRVQAKIAA SNTGELDALQ
QLGFSLVEGE VDLALPVNNV SDSGAVVAQE TDIPALRQLA SAAFAQSRFR APWYAPDASG
RFYAQWIENA VRGTFDHQCL ILRAASGDIR GYVSLRELNA TDARIGLLAG RGAGAELMQT
ALNWAYARGK TTLRVATQMG NTAALKRYIQ SGANVESTAY WLYR
