ACSS3_BOVIN
ID ACSS3_BOVIN Reviewed; 686 AA.
AC A7MB45;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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; BC151332; AAI51333.1; -; mRNA.
DR RefSeq; NP_001095607.1; NM_001102137.2.
DR RefSeq; XP_010803057.1; XM_010804755.2.
DR AlphaFoldDB; A7MB45; -.
DR SMR; A7MB45; -.
DR STRING; 9913.ENSBTAP00000024880; -.
DR PaxDb; A7MB45; -.
DR Ensembl; ENSBTAT00000024880; ENSBTAP00000024880; ENSBTAG00000018694.
DR Ensembl; ENSBTAT00000081091; ENSBTAP00000059006; ENSBTAG00000018694.
DR GeneID; 531552; -.
DR KEGG; bta:531552; -.
DR CTD; 79611; -.
DR VEuPathDB; HostDB:ENSBTAG00000018694; -.
DR VGNC; VGNC:25572; ACSS3.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000157479; -.
DR InParanoid; A7MB45; -.
DR OMA; YVFVMGR; -.
DR OrthoDB; 288915at2759; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000018694; Expressed in oviduct epithelium and 103 other tissues.
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_0000320623"
FT BINDING 226..229
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 424..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 445..450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 517
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14DH7"
FT MOD_RES 523
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14DH7"
SQ SEQUENCE 686 AA; 74805 MW; 0EE74B4DD3E71FE0 CRC64;
MKPSWLQCRK VTGAGGLGGS LPASSPARGA GPARRAYVAP GPRGALGGRG CRALSSGGGE
YKTHFAASVT DPERFWGKAA EQISWYKPWT KTLENRHSPS TSWFVEGMLN ICYNAIDRHI
ENGKGDKIAI IYDSPVTNTK ATITYKEVLE QVSKLAGVLV KHGVKKGDTV VIYMPMIPQA
MYAMLACARI GAIHSLIFGG FASKELSTRI DHAKPKLVIT ASFGIEPGRK VEYVPLVEEA
LRIGQHKPDK VLIYNRPHTD MVPLAPGYYL DWDEELSKAQ SHDCVPVLSE HPLYILYTSG
TTGLPKGVVR PTGGYAVMLN WSMSSIYGLK PGEVWWAASD LGWVVGHSYI CYGPLLHGNT
TVLYEGKPVG TPDAGAYFRV LAEHGVAALF TAPTAIRAIR QQDPGAALGK QYSLTRFKTL
FVAGERCDVE TLEWSKKVFR VPVLDHWWQT ETGSPITASC IGLGNSKTPP PGQAGKSVPG
YNVMILDDNM QKLKARCLGN IVVKLPLPPG AFSGLWKNQE AFKHLYFEKF PGYYDTMDAG
YMDEEGYVYV MSRVDDVINV AGHRISAGAL EESILSLGIV ADCAVVGKED SLKGHIPLAL
CVLKKDINTT EEHVLEEIVK HVRQTIGPVA AFRKAVFVKQ LPKTRSGKIP RSTLSALVNG
KPYKVSPTIE DPGIFEHIEA MLKQAS
