ID J8PRR1_SACAR Unreviewed; 713 AA.
AC J8PRR1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN ORFNames=SU7_0004 {ECO:0000313|EMBL:EJS44840.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS44840.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS44840.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
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|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU361147}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJS44840.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALIE01000002; EJS44840.1; -; Genomic_DNA.
DR AlphaFoldDB; J8PRR1; -.
DR HOGENOM; CLU_000022_3_6_1; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000006968; Chromosome I.
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 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:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361147};
KW Reference proteome {ECO:0000313|Proteomes:UP000006968}.
FT DOMAIN 76..137
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 139..527
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 590..675
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 79229 MW; 5BCE7DD18B713365 CRC64;
MSPSAVQSSN PQEQSSKIDE LKAHMSHSSS GTQQKKEQEY EHLTSVKIVP QRPISERLQP
EIATHYSPHL DGLQDYQRLH KESIEDPAKF FGSKATQFLN WSKPFDQVFI PDPKTGRPSF
QNNAWFLNGQ LNACYNCVDR HALRTPEKKA IIFEADEPGQ GYSITYKELL EEVCQVAQVL
TYSMGVRKGD TVAVYMPMVP EAIITLLAIS RIGAIHSVVF AGFSSNSLRD RINDGDSKVV
ITTDESNRGG KVIETKRIVD DALRETPGVR HVLVYKKTNN PSVAFHAPRD LDWATEKKKY
KTYYPCTPVD SEDPLFLLYT SGSTGAPKGV QHSTAGYLLG ALLTMRYTFD THQEDIFFTA
GDIGWITGHT YVVYGPLLYG CTTLVFEGTP AYPDYSRYWD VIDKNKVTQF YVAPTALRLL
KRAGDSFIEN HSLKSLRCLG SVGEPIAAEV WEWYSEKIGK NEIPIVDTYW QTESGSHLVT
PLAGGVTPMK PGSASFPFFG IDAVVLDPNT GEEINSTHAE GVLAVKAAWP SFARTIWKNH
DRYLDTYLNP YPGYYFTGDG AAKDKDGYIW ILGRVDDVVN VSGHRLSTAE IEAAIIEDPI
VAECAVVGFN DDLTGQAVAA FVVLKNKSSW STATDDELQD IKKHLVFTVR KDIGPFAAPK
LIILVDDLPK TRSGKIMRRI LRKILAGESD QLGDVSTLSN PGIVRHLIDS VKL
//
