ACSM3_RAT
ID ACSM3_RAT Reviewed; 580 AA.
AC Q6SKG1; Q62742;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SA rat hypertension-associated protein;
DE Short=Protein SA;
DE Flags: Precursor;
GN Name=Acsm3; Synonyms=Sah;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SHR, and Wistar Kyoto;
RX PubMed=14739236; DOI=10.1093/nar/gkh197;
RA Rigatti R., Jia J.-H., Samani N.J., Eperon I.C.;
RT "Exon repetition: a major pathway for processing mRNA of some genes is
RT allele-specific.";
RL Nucleic Acids Res. 32:441-446(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-479.
RX PubMed=8535086; DOI=10.1007/bf00352385;
RA Gu L., Dene H., Rapp J.P.;
RT "Possible alternative splicing of the rat SA gene.";
RL Mamm. Genome 6:683-684(1995).
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; AY455861; AAR20710.1; -; Genomic_DNA.
DR EMBL; AY456695; AAR21570.1; -; Genomic_DNA.
DR EMBL; BC090325; AAH90325.1; -; mRNA.
DR EMBL; U19832; AAA95995.1; -; Genomic_DNA.
DR RefSeq; NP_150234.1; NM_033231.1.
DR AlphaFoldDB; Q6SKG1; -.
DR SMR; Q6SKG1; -.
DR STRING; 10116.ENSRNOP00000020039; -.
DR iPTMnet; Q6SKG1; -.
DR PhosphoSitePlus; Q6SKG1; -.
DR PaxDb; Q6SKG1; -.
DR PRIDE; Q6SKG1; -.
DR Ensembl; ENSRNOT00000020039; ENSRNOP00000020039; ENSRNOG00000032246.
DR GeneID; 24763; -.
DR KEGG; rno:24763; -.
DR UCSC; RGD:62086; rat.
DR CTD; 6296; -.
DR RGD; 62086; Acsm3.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000157930; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q6SKG1; -.
DR OMA; HAWSNLF; -.
DR OrthoDB; 683933at2759; -.
DR PRO; PR:Q6SKG1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000032246; Expressed in kidney and 18 other tissues.
DR Genevisible; Q6SKG1; RN.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
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:0015645; F:fatty acid ligase activity; ISO:RGD.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
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:0018729; F:propionate CoA-transferase activity; ISO:RGD.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:RGD.
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 Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..580
FT /note="Acyl-coenzyme A synthetase ACSM3, mitochondrial"
FT /id="PRO_0000306100"
FT BINDING 229..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 368..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT MOD_RES 100
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UNX5"
SQ SEQUENCE 580 AA; 65713 MW; E2F46C5C530D6278 CRC64;
MAMLLRARCF HRLAIPDPRR ILYKDYRTAI PQNFSNYESM KHDFKIEIPE YFNFAKDVLD
QWTNTEKTGK RLSNPAFWWV DGNGKEVRWS FEELGSLSRK FANILTEACS LQRGDRVMVI
LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KSKCIITDDT LAPAVDIVAA
KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH NELMAIYFTS GTTGPPKMIG
HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF
DSTSILQTLS KFPITVFCSA PTAYRMLIQN DITSYKFNSL KHCVSAGEPI NPEVMEQWKK
KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFN VEILDENGTI LPPGQEGDIA
VQVLPDRPFG LFTHYVDNPS KTASTLRGNF YITGDRGYMD EDGYFWFVAR SDDVILSSGY
RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKLHDQE QLKKEIQEHV
KKTTAPYKYP RKIEFIEELP KTVSGKVKRN ELRRKEWTTT
