ID   ACS2_ZYGBA              Reviewed;         675 AA.
AC   Q96VC7;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Acetyl-coenzyme A synthetase 2;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase 2;
DE   AltName: Full=Acyl-activating enzyme 2;
GN   Name=ACS2;
OS   Zygosaccharomyces bailii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4954;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ISA 1307;
RX   PubMed=12514054; DOI=10.1128/aem.69.1.649-653.2003;
RA   Rodrigues F., Luovico P., Sousa M.J., Steensma H.Y., Corte-Real M.,
RA   Leao C.;
RT   "The spoilage yeast Zygosaccharomyces bailii forms mitotic spores: a
RT   screening method for haploidization.";
RL   Appl. Environ. Microbiol. 69:649-653(2003).
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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AJ314837; CAC41017.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96VC7; -.
DR   SMR; Q96VC7; -.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..675
FT                   /note="Acetyl-coenzyme A synthetase 2"
FT                   /id="PRO_0000208422"
FT   BINDING         206..209
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         401..403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         425..430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         516
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         531
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         539
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         542
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         604
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   675 AA;  74508 MW;  A19D1E670263F619 CRC64;
     MTVKEHKVVH EAQNVEALHA PEHFYKSQPG PSYIKDMKQY KEMYKQSVED PENFFGEKAR
     ELLDWDRPFT RSKYGSLENG DVTWFLNGEL NAAYNCVDRH AFANPDKPAL IYEADEEADN
     RMITFSELLR QVSRVAGVLQ SWGVKKGDTV AVYLPMIPEA VVAMLAIARL GAIHSVVFAG
     FSAGSLKDRV VDAGCKVVIT CDEGKRGGKT VHTKKIVDEG LNGISLVSHI LVFQRTGSEG
     IPMTAGRDYW WHEETAKQRS YLPPVPCNSE DPLFLLYTSG STGSPKGVVH STAGYLLGAA
     MTTRYVFDIH PEDVLFTAGD VGWITGHTYA LYGPLVLGTA SIIFESTPAY PDYGRYWRII
     QRHKATHFYV APTALRLIKR VGEAEIPKYD ISSLRVLGSV GEPISPELWE WYYEKVGNKN
     CVICDTMWQT ESGSHLIAPQ AGAVPTKPGS ATVPFFGVDA CIIDPVTGIE LQGNDVEGVL
     AVKSSWPSMA RSVWQNHHRY VDTYLKPYPG YYFTGDGAGR DHDGYYWIRG RVDDVVNVSG
     HRLSTAEIEA SLTNHDNVSE SAVVGIADEL TGQSVIAFVS LKDGSSRESS AVVAMRRELV
     LQVRGEIGPF AAPKCVILVK DLPKTRSGKI MRRVLRKVAS NEADQLGDLS TMANSEVVPS
     IIAAVDEQFF AEKKK