ACSF2_MACFA
ID ACSF2_MACFA Reviewed; 618 AA.
AC Q4R4Z9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=QnpA-14939;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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; AB169745; BAE01826.1; -; mRNA.
DR RefSeq; NP_001270429.1; NM_001283500.1.
DR AlphaFoldDB; Q4R4Z9; -.
DR SMR; Q4R4Z9; -.
DR STRING; 9541.XP_005583736.1; -.
DR GeneID; 101864763; -.
DR CTD; 80221; -.
DR eggNOG; KOG1177; Eukaryota.
DR OrthoDB; 386992at2759; -.
DR Proteomes; UP000233100; 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; 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 Acetylation; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..618
FT /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT /id="PRO_0000315794"
FT BINDING 266..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 182
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 185
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 185
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 343
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 481
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 513
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 547
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 547
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 573
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 573
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 602
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
SQ SEQUENCE 618 AA; 68309 MW; A3AA57119041B988 CRC64;
MRATAAYVGM LRLGRMCAGS PGVLGARAAL SRSWQEARLQ AVRFLSSREV DRMVPLPVGG
LSYVQGCTKN HLLSKTVGRC LEATAQRVPE REALVDLHEN IRLTFAQLKE EVDKAASGLL
SIGLCKGDRL GMWGPNSYAW VLIQLATAQA GIILVSVNPA YQATELEYVL KKVGCKALVF
PKQFKTQQYY NILKQICPEV ENAQPGALKS QRLPDLTTVI SVDAPLPGTL LLDEVLAAGS
TQQHLEQLQH IQQFLSCHDP INIQFTSGTT GSPKGATLSH YNIVNNSSIL GERLKLHEKT
PEQLRMILPS PLYHCLGSVG GTMMCLMYGA TLILASPVFN GKKALEAISR ERGSFLYGTP
TMFVDILNQP DFSSYDISTM RGGVIAGSPA PPELIRAIIN KINMKDLVVA YGTTENSPVT
FANFPEDTVE QKAESVGRIM PHTEARIMNM EAGMLAELNT PGELCIRGYC VMLGYWGEPQ
KTGEAVDQDK WYRTGDIATM NEQGFCKIVG RSKDMIIRGG ENIYPAELED FFHTHPKVQE
VQVVGVKDDR MGEEICACIR LKDGEETTAE EMKAFCKGKI SHFKIPRYIV FVTNYPLTTS
GKIQKFKLRE QMERHLNL
