(data stored in SCRATCH zone)

SWISSPROT: D3VHX8_XENNA

ID   D3VHX8_XENNA            Unreviewed;       241 AA.
AC   D3VHX8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   RecName: Full=dTDP-fucosamine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_02027};
DE            EC=2.3.1.210 {ECO:0000256|HAMAP-Rule:MF_02027};
DE   AltName: Full=TDP-fucosamine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_02027};
DE   AltName: Full=dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase {ECO:0000256|HAMAP-Rule:MF_02027};
GN   Name=rffC {ECO:0000313|EMBL:CBJ88467.1};
GN   Synonyms=wecD {ECO:0000256|HAMAP-Rule:MF_02027};
GN   OrderedLocusNames=XNC1_0390 {ECO:0000313|EMBL:CBJ88467.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88467.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88467.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-
CC       amino-4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized
CC       in the biosynthesis of the enterobacterial common antigen (ECA).
CC       {ECO:0000256|HAMAP-Rule:MF_02027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose =
CC         CoA + 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:0000256|HAMAP-Rule:MF_02027};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial
CC       common antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02027}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02027}.
CC   -!- SIMILARITY: Belongs to the WecD family. {ECO:0000256|HAMAP-
CC       Rule:MF_02027}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02027}.
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DR   EMBL; FN667742; CBJ88467.1; -; Genomic_DNA.
DR   RefSeq; WP_013183249.1; NC_014228.1.
DR   STRING; 406817.XNC1_0390; -.
DR   EnsemblBacteria; CBJ88467; CBJ88467; XNC1_0390.
DR   KEGG; xne:XNC1_0390; -.
DR   eggNOG; ENOG4108WJ1; Bacteria.
DR   eggNOG; COG0454; LUCA.
DR   HOGENOM; HOG000126448; -.
DR   KO; K16704; -.
DR   OMA; TAYWFYR; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000008075; 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; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR02382; wecD_rffC; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHX8.
DR   SWISS-2DPAGE; D3VHX8.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_02027,
KW   ECO:0000313|EMBL:CBJ88467.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02027,
KW   ECO:0000313|EMBL:CBJ88467.1}.
FT   DOMAIN       93    241       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
FT   ACT_SITE    224    224       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02027}.
FT   BINDING     217    217       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_02027}.
SQ   SEQUENCE   241 AA;  26496 MW;  707F95A07340DC8A CRC64;
     MSIHANLEPL AWDSQFFGLS TARLNLSPGA AVITAAHLDE YALVQAKIPA QQTAVLDALS
     ALSFSLAEGE ADLLLSLDAG DQTEIQTGQN AVPKFVIAKP QDIPALKAVA EQVFKVSRFR
     APWYQPDDSG RFYAVWVENA VLGTFDHECL MINDEHGQMM GFVTLRDIGS HEARIGLLAT
     VPGSHHQGIG KKLMSAAQQW CQQHQIQRLR IATQISNIAA LRLYTRRGAI IESTAYWLYR
     G
//

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