ID   SAST_ANAPL              Reviewed;         251 AA.
AC   P00633;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=S-acyl fatty acid synthase thioesterase, medium chain;
DE            EC=3.1.2.14;
DE   AltName: Full=Thioesterase II;
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uropygial gland;
RX   PubMed=2415525; DOI=10.1016/s0021-9258(17)36351-2;
RA   Poulose A.J., Rogers L., Cheesbrough T.M., Kolattukudy P.E.;
RT   "Cloning and sequencing of the cDNA for S-acyl fatty acid synthase
RT   thioesterase from the uropygial gland of mallard duck.";
RL   J. Biol. Chem. 260:15953-15958(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Uropygial gland;
RX   PubMed=2850144; DOI=10.1089/dna.1.1988.7.449;
RA   Sasaki G.C., Cheesbrough V., Kolattukudy P.E.;
RT   "Nucleotide sequence of the S-acyl fatty acid synthase thioesterase gene
RT   and its tissue-specific expression.";
RL   DNA 7:449-457(1988).
CC   -!- FUNCTION: In fatty acid biosynthesis chain termination and release of
CC       the free fatty acid product is achieved by hydrolysis of the thio ester
CC       by a thioesterase I, a component of the fatty acid synthetase complex.
CC       The chain length of the released fatty acid is usually C16. However, in
CC       the mammary glands of non-ruminant mammals, and in the uropygial gland
CC       of certain waterfowl there exists a second thioesterase which releases
CC       medium-chain length fatty acids (C8 to C2).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-
CC         [ACP] + H(+); Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC   -!- SIMILARITY: Belongs to the thioesterase family. {ECO:0000305}.
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DR   EMBL; M12101; AAA49222.1; -; mRNA.
DR   EMBL; M21635; AAA49219.1; -; Genomic_DNA.
DR   PIR; A00775; ESDKTM.
DR   PIR; I50520; I50520.
DR   RefSeq; XP_005017942.1; XM_005017885.6.
DR   AlphaFoldDB; P00633; -.
DR   SMR; P00633; -.
DR   ESTHER; anapl-sast; Thioesterase.
DR   GeneID; 101793583; -.
DR   KEGG; apla:101793583; -.
DR   CTD; 55301; -.
DR   OrthoDB; 541883at2759; -.
DR   GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IEA:UniProtKB-ARBA.
DR   FunFam; 3.40.50.1820:FF:000153; Surfactin synthase thioesterase subunit; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR012223; TEII.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR11487:SF0; S-ACYL FATTY ACID SYNTHASE THIOESTERASE, MEDIUM CHAIN; 1.
DR   PANTHER; PTHR11487; THIOESTERASE; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW   Lipid biosynthesis; Lipid metabolism.
FT   CHAIN           1..251
FT                   /note="S-acyl fatty acid synthase thioesterase, medium
FT                   chain"
FT                   /id="PRO_0000180357"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000250"
FT   CONFLICT        43
FT                   /note="V -> E (in Ref. 2; AAA49219)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   251 AA;  28807 MW;  3DFA25170D9EDC50 CRC64;
     MDKVIARPYK RPNALCRLIC FPWAGGNCSF FIRWCEAFSS IIVVSVIRLA GRECRDTEPF
     PEDMAEVVNE ITNALLKDLQ EKPFALFGHS FGSFVSYALA VHLKEKHGLE PVHMFFSGSY
     GPHSEYFHLM YKLPEVEDSR LLELIHTLGG TPPEFLQNEQ ITKHLLRVLK EDQKVLVTYP
     WHDVRKKYFS CDLTCFNGSD EKNHGSEAWI AITSGDTSIY SLPGNHFYLM EPSNETFLIK
     YITKCIENSD I
//