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Database: UniProt
Entry: A0A2K5WID2_MACFA
LinkDB: A0A2K5WID2_MACFA
Original site: A0A2K5WID2_MACFA 
ID   A0A2K5WID2_MACFA        Unreviewed;       638 AA.
AC   A0A2K5WID2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Propionate--CoA ligase {ECO:0000256|ARBA:ARBA00029726};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
DE            EC=6.2.1.17 {ECO:0000256|ARBA:ARBA00012985};
GN   Name=ACSS2 {ECO:0000313|Ensembl:ENSMFAP00000036897.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000036897.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000036897.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000036897.2}
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=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; A0A2K5WID2; -.
DR   Ensembl; ENSMFAT00000011146.2; ENSMFAP00000036897.2; ENSMFAG00000037662.2.
DR   VEuPathDB; HostDB:ENSMFAG00000037662; -.
DR   GeneTree; ENSGT00940000156358; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000233100; Chromosome 10.
DR   Bgee; ENSMFAG00000037662; Expressed in colon and 13 other cell types or tissues.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP 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   CDD; cd05966; ACS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF126; ACETYL-COENZYME A SYNTHETASE, CYTOPLASMIC; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT   DOMAIN          14..63
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          71..429
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          520..598
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   638 AA;  71900 MW;  CE8BF04E021B5399 CRC64;
     MSEKINDIWA SISIAEFWGD IAKEFYWKTP CPGPFLRYNF DVTKGKIFIE WMKGASTNIC
     YNVLDRNVHE KKLGDKVAFY WEGNEPGETT QITYHELLVQ VCQFSNVLRK QGIQKGDRVA
     IYMPMIPELV VAMLACARIG ALHSIVFAGF SSESLCERIL DSSCSLLITT DAFYRGEKLV
     NLKELADEAL QKCQEKDFPV RCCIVVKHLG RAELGMGDSP SQSPPIKRSC PDVQISWNQG
     IDLWWHELMQ EAGDECEPEW CDAEDPLFIL YTSGSTGKPK GVVHTVGGYM LYVATTFKYV
     FDFHAEDVFW CTADIGWITG HSYVTYGPLA NGATSVLFEG IPTYPDVNRL WSIVDKYKVT
     KFYTAPTAIR LLMKFGDEPV TKHSRASLQV LGTVGEPINP EAWLWYHQVV GAQRCPIVDT
     FWQTETTFPF FGVAPAILNE SGEELEGEAE GYLVFKQPWP GIMRTVYGNH ERFETTYFKK
     FPGYYVTGDG CRRDQDGYYW ITGRIDDMLN VSGHLLSTAE VESALVEHEA VAEAAVVGHP
     HPVKGECLYC FVTLCDGHTF SPKLTEELKK QIREKIGPIA TPDYIQNAPG LPKTRSGKIM
     RRVLRKIAQN DHDLGDTSTV ADPSVISHLF SHRCLTIQ
//
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