ID A0A2K5Y6C0_MANLE Unreviewed; 574 AA.
AC A0A2K5Y6C0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN Name=ACSS1 {ECO:0000313|Ensembl:ENSMLEP00000011107.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000011107.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000011107.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|RuleBase:RU361147};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|RuleBase:RU361147}.
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DR AlphaFoldDB; A0A2K5Y6C0; -.
DR Ensembl; ENSMLET00000034529.1; ENSMLEP00000011107.1; ENSMLEG00000029721.1.
DR GeneTree; ENSGT00940000158550; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF110; ACETYL-COENZYME A SYNTHETASE 2-LIKE, MITOCHONDRIAL; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 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|RuleBase:RU361147};
KW Ligase {ECO:0000256|RuleBase:RU361147};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361147};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 57..113
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 115..507
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 574 AA; 62583 MW; 0B0C2DA708BC86D9 CRC64;
MAARSLGRGV GRLLGSLRGL SGQPARPLCR VSAQRRAASG PSGSAPAVAA ASQPGSYPAL
SAQAAREPAA FWGPLARDTL LWDTPYHTVW DCDFSTGKIG WFLGGQLNVS VNCLDQHVWK
SPESVALIWE RDEPGTEVRI TYRELLETTC RLANTLKRHG VCRGDCVAIY MPVSPLAVAA
MLACARIGAV HTVVFAGFSA ASLAGRINDA KCKVVITFNQ GLRGGRVMEL KKIVDEAVKH
CPTVQRVLVA HRTDNKVHMG DLDIPLEQEM AKEDPVCAPE SMGSEDVLFM LYTSGSTGMP
KGIVHTQAGY LLYAALTHKL VFDHRPGDIF GCVADIGWIT GHSYVVYGPL CNGATSVLFE
STPVYPNAGR YWETVERLKI NQFYGAPTAV RLLLKYGDAW VKKYDRSSLR TLGSVGEPIN
CEAWEWLHRV VGDSRCTLVD TWWQTETGGI CIAPRPSEEG AEILPGMAMR PFFGIVPVLM
DEKGSVVEGS NVSGALCISQ AWPGMARTIY GDHQRFVDAY FKAYPGYYFT GDGAHRTEGG
YYQITGRMDD VINTLQIGGL FREAIRNSGD LLEH
//