FABY_ECOLI
ID FABY_ECOLI Reviewed; 329 AA.
AC P0ADQ2; P32148; Q2M8I5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable acyltransferase FabY {ECO:0000305};
DE EC=2.3.1.- {ECO:0000255|PROSITE-ProRule:PRU00532};
GN Name=fabY {ECO:0000303|PubMed:31331975}; Synonyms=yiiD;
GN OrderedLocusNames=b3888, JW3859;
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=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 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 [4]
RP FUNCTION, OVEREXPRESSION, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31331975; DOI=10.1128/jb.00354-19;
RA Sanyal R., Singh V., Harinarayanan R.;
RT "A novel gene contributing to the initiation of fatty acid biosynthesis in
RT Escherichia coli.";
RL J. Bacteriol. 201:e00354-e00354(2019).
CC -!- FUNCTION: Supports initiation of fatty acid biosynthesis in the absence
CC of FabH. {ECO:0000269|PubMed:31331975}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:31331975}.
CC -!- INDUCTION: In the absence of FabH, expression is positively regulated
CC by the stringent response factors (p)ppGpp and DksA.
CC {ECO:0000269|PubMed:31331975}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant does not exhibit any growth
CC defect. Combined inactivation of FabH and FabY results in growth
CC arrest, possibly due to the loss of fatty acid biosynthesis.
CC {ECO:0000269|PubMed:31331975}.
CC -!- MISCELLANEOUS: Overexpression rescues altered fatty acid profile,
CC growth defect and reduced cell size of the fabH deletion mutant.
CC {ECO:0000269|PubMed:31331975}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. FabY subfamily.
CC {ECO:0000305}.
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DR EMBL; L19201; AAB03021.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13450.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77421.1; -; Genomic_DNA.
DR PIR; S40832; S40832.
DR RefSeq; NP_418324.1; NC_000913.3.
DR AlphaFoldDB; P0ADQ2; -.
DR SMR; P0ADQ2; -.
DR BioGRID; 4261099; 128.
DR DIP; DIP-48207N; -.
DR IntAct; P0ADQ2; 10.
DR STRING; 511145.b3888; -.
DR jPOST; P0ADQ2; -.
DR PaxDb; P0ADQ2; -.
DR PRIDE; P0ADQ2; -.
DR EnsemblBacteria; AAD13450; AAD13450; b3888.
DR EnsemblBacteria; BAE77421; BAE77421; BAE77421.
DR GeneID; 948387; -.
DR KEGG; ecj:JW3859; -.
DR KEGG; eco:b3888; -.
DR PATRIC; fig|511145.12.peg.4000; -.
DR EchoBASE; EB1799; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_063776_0_0_6; -.
DR OMA; SEKDGYD; -.
DR PhylomeDB; P0ADQ2; -.
DR BioCyc; EcoCyc:EG11853-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:P0ADQ2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039143; GNPNAT1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR012660; YiiD_C.
DR PANTHER; PTHR13355; PTHR13355; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF09500; YiiD_C; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR02447; yiiD_Cterm; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..329
FT /note="Probable acyltransferase FabY"
FT /id="PRO_0000169679"
FT DOMAIN 18..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 329 AA; 37094 MW; 42411FE2B0D21175 CRC64;
MSQLPGLSRE TRESIAMYHL RVPQTEEELE RYYQFRWEML RKPLHQPKGS ERDAWDAMAH
HQMVVDEQGN LVAVGRLYIN ADNEASIRFM AVHPDVQDKG LGTLMAMTLE SVARQEGVKR
VTCSAREDAV EFFAKLGFVN QGEITTPTTT PIRHFLMIKP VATLDDILHR GDWCAQLQQA
WYEHIPLSEK MGVRIQQYTG QKFITTMPET GNQNPHHTLF AGSLFSLATL TGWGLIWLML
RERHLGGTII LADAHIRYSK PISGKPHAVA DLGALSGDLD RLARGRKARV QMQVEIFGDE
TPGAVFEGTY IVLPAKPFGP YEEGGNEEE
