ACSF3_BOVIN
ID ACSF3_BOVIN Reviewed; 586 AA.
AC Q58DN7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT021560; AAX46407.1; -; mRNA.
DR EMBL; BC102586; AAI02587.1; -; mRNA.
DR RefSeq; NP_001030240.1; NM_001035068.2.
DR RefSeq; XP_005218566.1; XM_005218509.3.
DR AlphaFoldDB; Q58DN7; -.
DR SMR; Q58DN7; -.
DR STRING; 9913.ENSBTAP00000021234; -.
DR PaxDb; Q58DN7; -.
DR PRIDE; Q58DN7; -.
DR Ensembl; ENSBTAT00000021234; ENSBTAP00000021234; ENSBTAG00000015968.
DR Ensembl; ENSBTAT00000076555; ENSBTAP00000073922; ENSBTAG00000015968.
DR Ensembl; ENSBTAT00000085479; ENSBTAP00000068809; ENSBTAG00000015968.
DR GeneID; 509209; -.
DR KEGG; bta:509209; -.
DR CTD; 197322; -.
DR VEuPathDB; HostDB:ENSBTAG00000015968; -.
DR VGNC; VGNC:25563; ACSF3.
DR eggNOG; KOG1176; Eukaryota.
DR GeneTree; ENSGT00940000157000; -.
DR HOGENOM; CLU_000022_59_11_1; -.
DR InParanoid; Q58DN7; -.
DR OrthoDB; 533939at2759; -.
DR TreeFam; TF312995; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015968; Expressed in cortex of kidney and 105 other tissues.
DR ExpressionAtlas; Q58DN7; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0090409; F:malonyl-CoA synthetase activity; IEA:RHEA.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic 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..89
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 90..586
FT /note="Malonate--CoA ligase ACSF3, mitochondrial"
FT /id="PRO_0000315799"
FT BINDING 203..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 586 AA; 64990 MW; 5D45A8D1D4C07992 CRC64;
MPLPYVGMAL RRLAWAVASC RLAPWTRGAS GPLHSAPAAR SDCSAPVFIR APAFGDRLAL
IDQHGRHTYK DLYLRSLRLS REICQLRACA DGDLREERVS LLCSNDVSFV VAQWAAWMSG
GVAVPLYRKH PRAQLEYFIQ DSRSSVVLAG PEHVELLSPV AQKLGVPLLP LPPTVYHGVA
EDPEEGLVLE RNWRDRGAMI IYTSGTTGRP KGVLSTHDNI RAVVTGLVHK WAWTKDDVIL
HVLPLHHVHG VVNKLLCPLW VGATCVMLPE FSAQLVWEKF LSSEAPQINV FMAVPTIYSK
LMDYYDKHFT QPHVQDFVRA VCEEKIRLMV SGSAALPLPV LEKWKGITGH TLLERYGMTE
IGMALSNPLT AARLPGSVGT PLPGVEVRIV SENPQKDSSP YLIHAEGSEE NTKVTPGFEE
KEGELLVRGP SVFREYWDKP EETKAAFTSD GWFKTGDTVV FKDGCYWIRG RTSVDIIKSG
GYKVSALEVE RLLLAHPSIT DVAVIGVPDM TWGQRVTAVV TLQEGHSLSH RELKEWARGV
LAPYAVPSEL LLVEEIPRNQ MGKVNKRDLV RQLYPHEKGA PEAGSQ
