ID   GCAT_AERHY              Reviewed;         335 AA.
AC   P10480;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 3.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Phosphatidylcholine-sterol acyltransferase;
DE            EC=2.3.1.43;
DE   AltName: Full=Glycerophospholipid-cholesterol acyltransferase;
DE            Short=GCAT;
DE   Flags: Precursor;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=2271578; DOI=10.1021/bi00490a026;
RA   Hilton S., McCubbin W.D., Kay C.M., Buckley J.T.;
RT   "Purification and spectral study of a microbial fatty acyltransferase:
RT   activation by limited proteolysis.";
RL   Biochemistry 29:9072-9078(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=3280033; DOI=10.1016/0005-2760(88)90026-4;
RA   Thornton J., Howard S.P., Buckley J.T.;
RT   "Molecular cloning of a phospholipid-cholesterol acyltransferase from
RT   Aeromonas hydrophila. Sequence homologies with lecithin-cholesterol
RT   acyltransferase and other lipases.";
RL   Biochim. Biophys. Acta 959:153-159(1988).
RN   [3]
RP   MUTAGENESIS, AND ACTIVE SITE.
RX   PubMed=1985976; DOI=10.1016/s0021-9258(17)35273-0;
RA   Hilton S., Buckley J.T.;
RT   "Studies on the reaction mechanism of a microbial lipase/acyltransferase
RT   using chemical modification and site-directed mutagenesis.";
RL   J. Biol. Chem. 266:997-1000(1991).
RN   [4]
RP   MUTAGENESIS.
RX   PubMed=8294469; DOI=10.1016/s0021-9258(17)42147-8;
RA   Robertson D.L., Hilton S., Wong K.R., Koepke A., Buckley J.T.;
RT   "Influence of active site and tyrosine modification on the secretion and
RT   activity of the Aeromonas hydrophila lipase/acyltransferase.";
RL   J. Biol. Chem. 269:2146-2150(1994).
CC   -!- FUNCTION: Fatty acid transfer between phosphatidylcholine and
CC       cholesterol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a sterol = a 1-
CC         acyl-sn-glycero-3-phosphocholine + a sterol ester;
CC         Xref=Rhea:RHEA:21204, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=2.3.1.43;
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA30260.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X07279; CAA30260.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A36035; XXFOGA.
DR   AlphaFoldDB; P10480; -.
DR   SMR; P10480; -.
DR   STRING; 1448139.AI20_00250; -.
DR   eggNOG; COG3240; Bacteria.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR008265; Lipase_GDSL_AS.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cholesterol metabolism; Lipid metabolism; Signal;
KW   Steroid metabolism; Sterol metabolism; Transferase.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..335
FT                   /note="Phosphatidylcholine-sterol acyltransferase"
FT                   /id="PRO_0000017844"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         34
FT                   /note="S->N: Loss of activity."
FT   MUTAGEN         36
FT                   /note="S->G: Loss of activity."
SQ   SEQUENCE   335 AA;  37067 MW;  58A72BA2B4C8B870 CRC64;
     MKKWFVCLLG LVALTVQAAD SRPAFSRIVM FGDSLSDTGK MYSKMRGYLP SSPPYYEGRF
     SNGPVWLEQL TNEFPGLTIA NEAEGGPTAV AYNKISWNPK YQVINNLDYE VTQFLQKDSF
     KPDDLVILWV GANDYLAYGW NTEQDAKRVR DAISDAANRM VLNGAKEILL FNLPDLGQNP
     SARSQKVVEA ASHVSAYHNQ LLLNLARQLA PTGMVKLFEI DKQFAEMLRD PQNFGLSDTE
     NACYGGSYVW KPFASRSAST DSQLSAFNPQ ERLAIAGNPL LAQAVASPMA ARSASTLNCE
     GKMFWDQVHP TTVVHAALSE PAATFIESQY EFLAH