ID   ACSF3_XENLA             Reviewed;         578 AA.
AC   Q6GLK6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Malonate--CoA ligase ACSF3, mitochondrial {ECO:0000250|UniProtKB:Q4G176};
DE            EC=6.2.1.n3 {ECO:0000250|UniProtKB:Q4G176};
DE   AltName: Full=Acyl-CoA synthetase family member 3;
DE   Flags: Precursor;
GN   Name=acsf3 {ECO:0000250|UniProtKB:Q4G176};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the initial reaction in intramitochondrial fatty
CC       acid synthesis, by activating malonate and methylmalonate, but not
CC       acetate, into their respective CoA thioester. May have some preference
CC       toward very-long-chain substrates. {ECO:0000250|UniProtKB:Q4G176}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC         tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q4G176};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC         Evidence={ECO:0000250|UniProtKB:Q4G176};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + malonate = AMP + diphosphate + malonyl-CoA;
CC         Xref=Rhea:RHEA:32139, ChEBI:CHEBI:15792, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456215; EC=6.2.1.n3;
CC         Evidence={ECO:0000250|UniProtKB:Q4G176};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32140;
CC         Evidence={ECO:0000250|UniProtKB:Q4G176};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q4G176}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; BC074473; AAH74473.1; -; mRNA.
DR   RefSeq; NP_001086314.2; NM_001092845.1.
DR   AlphaFoldDB; Q6GLK6; -.
DR   SMR; Q6GLK6; -.
DR   PRIDE; Q6GLK6; -.
DR   DNASU; 444743; -.
DR   GeneID; 444743; -.
DR   KEGG; xla:444743; -.
DR   CTD; 444743; -.
DR   Xenbase; XB-GENE-964816; acsf3.S.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 444743; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0090409; F:malonyl-CoA synthetase activity; IEA:RHEA.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..578
FT                   /note="Malonate--CoA ligase ACSF3, mitochondrial"
FT                   /id="PRO_0000315802"
FT   REGION          394..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         205..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         565
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   578 AA;  64557 MW;  3B5C8BC27619D36D CRC64;
     MRVGAFLGRS LFSCSHVRGA LVRRRTPQHS CSFHISKPRS LSHVVPVFSR APLFSERTAM
     VDQHGKHTYK DLYIRSQALS KMIIQLLGNP SHNNTPERVS FLCPNNSSYV VCQWAVWMSG
     AIAVPLCKSH PPSELKYVLQ DSQSALVVAE ESYTNVLSPL AEQLGIPVLT MSGSQNLHPS
     ELLQEIKISQ LDLDWKDRGA MIIYTSGTTG RPKGVLSTHY NLYSMVTALV NEWGWTKEDS
     ILHVLPLHHV HGVVNKLMCP LWVGATCVIL PEFCPKTVWQ HFLGRDVPSI NIFMAVPTIY
     SKLIAYYEQH FTHSNVREFV RAACQERIRL MVSGSSALPV PVLERWQEIT GHTLLERYGM
     TEIGMALTNP LHGPRVPGAV GAPLPGVEVR TVTQNPRKEG TSYTTHAQGD STGTMVSVGL
     ENREGELQVR GPAVFKEYWN KRLDTQEAFT SDGWFKTGDT AMYKDGTYWI LGRTSVDIIK
     SGGYKVSALE VERHLLGHPS ITDVAVIGAP DVTWGQRVAA IVKLRDGHAL SLQELKEWAR
     AVMAPYCIPA ELIRVEEIPR NQMGKINKKQ LLVHFYPQ