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Database: UniProt
Entry: A0A2K6FQC3_PROCO
LinkDB: A0A2K6FQC3_PROCO
Original site: A0A2K6FQC3_PROCO 
ID   A0A2K6FQC3_PROCO        Unreviewed;       558 AA.
AC   A0A2K6FQC3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Acyl-CoA synthetase short-chain family member 3, mitochondrial {ECO:0000256|ARBA:ARBA00040004};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
DE            EC=6.2.1.17 {ECO:0000256|ARBA:ARBA00012985};
DE   AltName: Full=Acetate--CoA ligase 3 {ECO:0000256|ARBA:ARBA00042755};
DE   AltName: Full=Propionate--CoA ligase {ECO:0000256|ARBA:ARBA00029726};
GN   Name=ACSS3 {ECO:0000313|Ensembl:ENSPCOP00000016178.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000016178.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000016178.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000787};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC         Evidence={ECO:0000256|ARBA:ARBA00000787};
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:0000256|ARBA:ARBA00036650};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC         Evidence={ECO:0000256|ARBA:ARBA00036650};
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:0000256|ARBA:ARBA00001884};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC         Evidence={ECO:0000256|ARBA:ARBA00001884};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   AlphaFoldDB; A0A2K6FQC3; -.
DR   STRING; 379532.ENSPCOP00000016178; -.
DR   Ensembl; ENSPCOT00000026800.1; ENSPCOP00000016178.1; ENSPCOG00000019847.1.
DR   GeneTree; ENSGT00940000157479; -.
DR   OMA; FIMGRTD; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 1.
DR   Pfam; PF16177; ACAS_N; 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   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT   DOMAIN          62..116
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          123..347
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          442..520
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   558 AA;  60586 MW;  5A78F3C19C0823D7 CRC64;
     MKPSWLQCRK VTGAGGLGGP LPGSSPARGA GAARRAFVAP GPWGGLGGRG CRALTSGSVG
     EYKTHFAASV ADPERFWGQA AEQISWYKPW TKTLENRHPP STSWFVEGVL NICYNAIDRH
     IENGKGDKIA IIYDSPVTNT KATITYKEVL EQVSKLAGVL VKHGIKKGDT VVIYMPMIPQ
     AMYTMLACAR IGAIHSLIFG GFASKELSSR IDHVKVCALF GEIYSQLALK LYRHKGSFIL
     IETVPLAPDR DLDWDEEMAK AQSHDCVPVL SEHPLYILYT SGTTGLPKGV VRPTGGYAVM
     LNWTMSSIYG LKPGEVWWAA SDLGWVVGHS YICYGPLIHG NTTVLYETLE WSKKVFRVPV
     LDHWWQTGEG GSGSSCLAAA SSKVEPTSRC AKDSGQGKGA PRLGYYDTMD AGYMDEEGYL
     YVMSRVDDVI NVAGHRISAG AIEESVLSHG TVADCAVVGK EDPLKGHVPL ALCVLKKDIN
     VTEEKVLEEI VKHVRQNIGP VAAFRNAVFV KQLPKTRSGK IPRSALSALV NGKPYKVTST
     IEDPSIFGHI EEVLKQAL
//
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