ID ACSM3_PONAB Reviewed; 586 AA.
AC Q5REV5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM3, mitochondrial;
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q3UNX5};
DE AltName: Full=Acyl-CoA synthetase medium-chain family member 3;
DE AltName: Full=Butyrate--CoA ligase 3;
DE AltName: Full=Butyryl-coenzyme A synthetase 3;
DE AltName: Full=Middle-chain acyl-CoA synthetase 3;
DE AltName: Full=Propionate--CoA ligase;
DE EC=6.2.1.17 {ECO:0000250|UniProtKB:Q3UNX5};
DE AltName: Full=Protein SA homolog;
DE Flags: Precursor;
GN Name=ACSM3; Synonyms=SAH;
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: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism (By similarity).
CC Capable of activating medium-chain fatty acids with a preference for
CC isobutyrate among fatty acids with 2-6 carbon atoms (By similarity).
CC {ECO:0000250|UniProtKB:Q3UNX5}.
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:Q3UNX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456215; EC=6.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoate + ATP + CoA = 2-methylpropanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:46176, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57338, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46177;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutanoate + ATP + CoA = 2-methylbutanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:46180, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:48946, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57336, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46181;
CC Evidence={ECO:0000250|UniProtKB:Q3UNX5};
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:Q53FZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000250|UniProtKB:Q53FZ2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q53FZ2}.
CC Mitochondrion matrix {ECO:0000250|UniProtKB:Q3UNX5}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CR857411; CAH89702.1; -; mRNA.
DR RefSeq; NP_001124772.1; NM_001131300.1.
DR AlphaFoldDB; Q5REV5; -.
DR SMR; Q5REV5; -.
DR STRING; 9601.ENSPPYP00000008096; -.
DR Ensembl; ENSPPYT00000008431.3; ENSPPYP00000008096.2; ENSPPYG00000007161.3.
DR GeneID; 100171624; -.
DR KEGG; pon:100171624; -.
DR CTD; 6296; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000157930; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q5REV5; -.
DR OMA; HAWSNLF; -.
DR OrthoDB; 5474118at2759; -.
DR TreeFam; TF354287; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043759; F:methylbutanoate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05928; MACS_euk; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR43605:SF7; ACYL-COENZYME A SYNTHETASE ACSM3, MITOCHONDRIAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..586
FT /note="Acyl-coenzyme A synthetase ACSM3, mitochondrial"
FT /id="PRO_0000306099"
FT BINDING 235..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 374..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT MOD_RES 106
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT MOD_RES 157
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UNX5"
SQ SEQUENCE 586 AA; 66060 MW; A923438898F18582 CRC64;
MLACVTMKML RHAKCFQRLA IFGSVRALHK DNRTATPQNF SNYESMKQDF KLGIPEYFNF
AKDVLDQWTD KEKAGKKPSN PAFWWINRNG EEVRWSFEEL GSLSRKFANI LSEACSLQRG
DRVILILPRV PEWWLANVAC LRTGTVLIPG TTQLTQKDIL YRLQSSKANC IITNDVLAPA
VDAVAPKCEN LHSKLIVSEN SREGWGNLKE MMKHASDSHT CVKTKHNEIM AIFFTSGTSG
YPKMTAHTHS SFGLGLSVNG RFWLDLTPSD VMWNTSDTGW AKSAWSSVFS PWIQGACVFT
HHLPRFEPTS ILQTLSKYPI TVFCSAPTVY RMLVQNDMAS YKFKSLKHCV SAGEPITPDV
TEKWRNKTGL DIYEGYGQTE TVLICGNFKG MKIKPGSMGK PSPAFDVKIV DVNGNVLPPG
QEGDIGIQVL PNRPFGLFTH YVDNPSKTAS TLRGNFYITG DRGYMDEDGY FWFVARADDV
ILSSGYRIGP FEVENALNEH PSVAESAVVS SPDPIRGEVV KAFVVLNPDY KSHDQEQLIK
EIQEHVKKTT APYKYPRKVE FIQELPKTIS GKTKRNELRK KEWKTI
//
