ID A0A3B4VM16_SERDU Unreviewed; 396 AA.
AC A0A3B4VM16;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acetyl-CoA acyltransferase 2 {ECO:0000313|Ensembl:ENSSDUP00000032006.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000032006.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000032006.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR AlphaFoldDB; A0A3B4VM16; -.
DR STRING; 41447.ENSSDUP00000032006; -.
DR Ensembl; ENSSDUT00000032556.1; ENSSDUP00000032006.1; ENSSDUG00000022985.1.
DR GeneTree; ENSGT01030000234626; -.
DR OMA; RWCASSM; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProt.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 7..266
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..394
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 396 AA; 41470 MW; A0DC3095CA05D9C6 CRC64;
MALLRGVFIV AAKRTPFGTY GGVLKDHSAT DLAEHAAKAA LAAGGVAPEL VNSVIMGNVM
QSSADAPYIA RHVGLRCGVP IPVPALTVNR LCGSGFQAVI SGAHEICLKE SEVVLCGGSE
SMSQAPYAVR NIRFGTKFGV DLKLEDTLWA GLTDLHIKIP MGITAENLAE KYQITREDCD
NYAFQTQQRW KAAHEGGHYT AEIAPIDVKA RKGKVSMAQD EHPRPQTTLE QMAKLPPVFK
KGGTVTAANA SGVSDGAAAL VIASEDALKE HKLTPLARIV AYHVSGCDPS IMGIGPVPAI
TEALKKAGLT LNDMDVVEVN EAFASQYLAV AKALGLDPEK SNVNGGAIAI GHPLGASGAR
ITAHLVHELR RRGGKYAVGS ACIGGGQGIA IVLENY
//
