ID A0A3Q2DJ79_CYPVA Unreviewed; 680 AA.
AC A0A3Q2DJ79;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-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};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000019293.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000019293.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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, ECO:0000256|RuleBase:RU361147}.
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DR RefSeq; XP_015228504.1; XM_015373018.1.
DR AlphaFoldDB; A0A3Q2DJ79; -.
DR STRING; 28743.ENSCVAP00000019293; -.
DR Ensembl; ENSCVAT00000028428.1; ENSCVAP00000019293.1; ENSCVAG00000022663.1.
DR GeneID; 107083643; -.
DR KEGG; cvg:107083643; -.
DR CTD; 84532; -.
DR GeneTree; ENSGT00940000165253; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000265020; 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:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
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 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; IPR011904; Ac_CoA_lig.
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 NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF83; ACETYL-COENZYME A SYNTHETASE; 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, ECO:0000256|RuleBase:RU361147};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, 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:UP000265020}.
FT DOMAIN 54..109
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 111..500
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 559..638
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 680 AA; 75716 MW; 805354E250674592 CRC64;
MWLPCRCAAK YVAASFSRGV SASFLHALRR NRSSWNAAAF MPESSGFEGV SGRDALHDYS
VSHSESFWAA VARQRLSWIR PFDVVQDCDL SQGRISWFEG GKLNVSVNCL DRHVHTCPER
VALIWERDEQ GSEVRYTYKE LLEMTCRLGN LLRRQGVKKG DCVTIYMPTC PLAVASMLAC
ARIGAAHNVV FAGFSAEALA ERIRDAQSST VITVNQGVRG GKITELKRTV DAAVRSCPSV
QQVFVAMRTE KQVEMTDRDF VLEEEMLKED VVCEPAPMDS EDVLFLLYTS GSTGKPKGLV
HTQAGYLLYA AFTHRYVFGY HDGDVFGCVA DIGWITGHSY TVYGPLANGG TTVLFESTPV
YPDPGRYWEM VERLRINQFY GAPTAIRLLI KYGDQWVKKY DRSSLTTLGS VGEPINTEAW
EWYNRVVGEG RCPVVDTWWQ TETGGICIAP KPSEPDAEIV PGMAMRPFFG IKPVLMDTEG
KVLTSNNTSG ALCMAQPWPG MARTIHNNHQ RFIETYFQPY PGYFFTGDGA YRSEKGYYQI
TGRLDDVINV SGHRIGTAEI EDVVNQCPAV AESAVIGYSH SIKGQGVYAF VVLKKGVDIQ
EADISKQLNN MVSEKIAKYA CPEFVQFAKR LPKTRSGKIM RRVLRKVVEC DLDSLGDLST
LDDPAAVQEI IKGHEKLLSK
//