ID   ACSF2_DANRE             Reviewed;         606 AA.
AC   Q0P4F7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000250|UniProtKB:Q96CM8};
DE            EC=6.2.1.2 {ECO:0000250|UniProtKB:Q96CM8};
DE   Flags: Precursor;
GN   Name=acsf2 {ECO:0000250|UniProtKB:Q96CM8}; ORFNames=zgc:152887;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty
CC       acid metabolism, by forming a thioester with CoA. Has some preference
CC       toward medium-chain substrates. Plays a role in adipocyte
CC       differentiation. {ECO:0000250|UniProtKB:Q96CM8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q96CM8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC         Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q96CM8};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; BC122098; AAI22099.1; -; mRNA.
DR   AlphaFoldDB; Q0P4F7; -.
DR   SMR; Q0P4F7; -.
DR   STRING; 7955.ENSDARP00000081474; -.
DR   PaxDb; Q0P4F7; -.
DR   ZFIN; ZDB-GENE-060825-7; acsf2.
DR   eggNOG; KOG1177; Eukaryota.
DR   InParanoid; Q0P4F7; -.
DR   PhylomeDB; Q0P4F7; -.
DR   Reactome; R-DRE-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   PRO; PR:Q0P4F7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..13
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..606
FT                   /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT                   /id="PRO_0000315798"
FT   BINDING         256..264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         499
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         590
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   606 AA;  67514 MW;  D2FD627E986DF056 CRC64;
     MSSKILLTNL RTSASFCKTL KFPQRPRTPF IASQQSCAIH VDNPPSIPTL TTSYVHGLSS
     HPLQSSTVDQ CLQATVERYP DREAMVFVQD GIRKTFAEFY QDVEKAAAGL LAAGLKRGDR
     LGMWGPNIYE WVLMQFATAK AGIILVAVNP AYQLQEVEFA LRKVQCNAVV CPTKFKSQHY
     CDMLKQLCPE METASPGGIK SSRLPDLHTV IVTDSQQPGS FLLKDLMQAG SSQHYQQLQD
     LQKKLVCDDP INIQFTSGTT GKPKGATLSH HNIVNNAYFT GMRIGYNWRK NVRICLPVPL
     YHCFGSVGGG VIMALYGTTV IFPSTGYDGR ANLRAIEKEK CTFVYGTPTM YIDMLGQPDL
     AKFDLSSVRG GIAAGSPCPP EVMRKILNVM GIKEMVIGYG TTENSPVTFC GFPVDSAERK
     IVTVGCISPH TEAKVVDPTT GEIVPLGAQG ELMIRGYCVM LEYWQDEEKT RECITKDRWY
     KTGDIASLDQ FAYCKIEGRI KDLIIRGGEN IYPAEIEQFL HTHPKILEAQ VVGVKDERMG
     EEVCACIRLK EGQECTVEEI KAYCKGKIAH YKVPRYILFV QDYPLTITGK IQKHKLRERT
     EKQLGL