ACSS3_PONAB
ID ACSS3_PONAB Reviewed; 686 AA.
AC Q5REB8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Acyl-CoA synthetase short-chain family member 3, mitochondrial;
DE EC=6.2.1.1 {ECO:0000250|UniProtKB:A0A0G2K047};
DE AltName: Full=Acetate--CoA ligase 3;
DE AltName: Full=Propionate--CoA ligase;
DE EC=6.2.1.17 {ECO:0000250|UniProtKB:A0A0G2K047};
DE Flags: Precursor;
GN Name=ACSS3;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of acetyl-CoA from short-chain fatty
CC acids (By similarity). Propionate is the preferred substrate but can
CC also utilize acetate and butyrate with a much lower affinity.
CC {ECO:0000250|UniProtKB:A0A0G2K047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000250|UniProtKB:A0A0G2K047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC Evidence={ECO:0000250|UniProtKB:A0A0G2K047};
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:A0A0G2K047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000250|UniProtKB:A0A0G2K047};
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:A0A0G2K047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000250|UniProtKB:A0A0G2K047};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:A0A0G2K047}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CR857614; CAH89889.1; -; mRNA.
DR RefSeq; NP_001124881.1; NM_001131409.1.
DR AlphaFoldDB; Q5REB8; -.
DR SMR; Q5REB8; -.
DR STRING; 9601.ENSPPYP00000005476; -.
DR GeneID; 100171746; -.
DR KEGG; pon:100171746; -.
DR CTD; 79611; -.
DR eggNOG; KOG1175; Eukaryota.
DR InParanoid; Q5REB8; -.
DR OrthoDB; 288915at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0003987; F:acetate-CoA ligase activity; 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:0050218; F:propionate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR032387; ACAS_N.
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; PF16177; ACAS_N; 1.
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; Ligase; Lipid metabolism; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..686
FT /note="Acyl-CoA synthetase short-chain family member 3,
FT mitochondrial"
FT /id="PRO_0000320626"
FT BINDING 227..230
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 425..427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 446..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 518
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14DH7"
FT MOD_RES 524
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14DH7"
SQ SEQUENCE 686 AA; 74669 MW; 91D3B2635CE7DC21 CRC64;
MKPSWLQCHK VTSAGGLGGP LPGSSPARGA SAALRALVVP GPRGGLGGRG CRALSSGSGS
EYKTHFAASV TDPERFWGKA AEQISWYKPW TKTLENKHSP STSWFVEGML NVCYNAVDRH
IENGKGDKIA IIYDSPVTNT KATFTYKEVL EQVSKLAGVL VKHGIKKGDT VVIYMPMIPQ
AMYTMLACAR IGAIHSLIFG GFASKELSSR IDHVKPKVVV TASFGIEPGR RVEYVPLVEE
ALKIGQHKPD KILIYNRPNM EAVPLAPGRD LDWDEEMAKA QSHDCVPVLS EHPLYILYTS
GTTGLPKGVI RPTGGYAVML NWSMSSIYGL QPGEVWWAAS DLGWVVGHSY ICYGPLLHGN
TTVLYEGKPV GTPDAGAYFR VLAEHGVAAL FTAPTAIRAI RQQDPGAALG KQYSLTRFKT
LFVAGERCDV ETLEWSKNVF RVPVLDHWWQ TETGSPITAS CVGLGNSKTP PPGQAGKSVP
GYNVMILDDN MQKLKARCLG NIVVKLPLPP GAFSGLWKNQ EAFKHLYFEK FPGYYDTMDA
GYMDEEGYVY VMSRVDDVIN VAGHRISAGA IEESILSHGT VADCAVVGKE DPLKGHVPLA
LCVLRKDINA TEEQVLEEIV KHVRQNIGPV AAFRNAVFVK QLPKTRSGKI PRSALSAIVN
GKPYKITSTI EDPSIFGHVE EMLKQA
