ACSF2_PONAB
ID ACSF2_PONAB Reviewed; 615 AA.
AC Q5R9G9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
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};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859419; CAH91591.1; -; mRNA.
DR RefSeq; NP_001125938.1; NM_001132466.1.
DR AlphaFoldDB; Q5R9G9; -.
DR SMR; Q5R9G9; -.
DR STRING; 9601.ENSPPYP00000009305; -.
DR GeneID; 100172872; -.
DR KEGG; pon:100172872; -.
DR CTD; 80221; -.
DR eggNOG; KOG1177; Eukaryota.
DR InParanoid; Q5R9G9; -.
DR OrthoDB; 386992at2759; -.
DR Proteomes; UP000001595; 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..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..615
FT /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT /id="PRO_0000315796"
FT BINDING 263..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 182
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 182
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 398
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 478
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 510
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 570
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 570
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 599
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
SQ SEQUENCE 615 AA; 68067 MW; B6368C62636F83B5 CRC64;
MAVYVGMLRL GRLCAGSSGV LGARVALSRS WQEARLQGVR FLSSREVDRM VSLPIGGLSY
VQGCTKKHLN SKTVGQCLDT TAQRVPEREA LVVLHEDVRL TFGQLKEEVD KAASGLLSIG
LCKGDRLGMW GPNSYAWVLM QLATAQAGII LVSVNPAYQA MELEYVLKKV GCKALVFPKQ
FKTQQYYNIL KQICPEVDNA QPGGLKSQRL PDLTTVISVD APLPGTLLLD EVVAAGSTRQ
HLDQLQYNQQ FLSCHDPINI QFTSGTTGSP KGATLSHYNI VNNSNMLGER LKLHEKTPEQ
LRMILPSPLY HCLGSVGGTM MCLMYGATLI LASPVFNGKK ALEAISRERG SFLYGTPTMF
VDILNQPDFS SYDISTMCGG VIAGSPAPPE LIRAIINKIN MKDLVVAYGT PENSPVTFAH
FPEDTVEQKA ESVGRIMPHT EARIMNMEAG TLAELNTPGE LCIRGYCVML GYWGEPQKTE
EAVDQDKWYR TGDVATMNEQ GFCKIVGRSK DMIIRGGENI YPAELEDFFH THPKVQEVQV
VGVKDDRMGE EICACIRLKD GEETTVEEIK AFCKGKISHF KIPRYIVFVT NYPLTISGKI
QKFKLREQME RHLNL
