ID   ACSA_PENCH              Reviewed;         669 AA.
AC   P36333;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Acetyl-coenzyme A synthetase;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase;
DE   AltName: Full=Acyl-activating enzyme;
GN   Name=facA; Synonyms=acuA;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8103029; DOI=10.1016/0378-1119(93)90429-7;
RA   Martinez-Blanco H., Orejas M., Reglero A., Luengo J.M., Penalva M.A.;
RT   "Characterisation of the gene encoding acetyl-CoA synthetase in Penicillium
RT   chrysogenum: conservation of intron position in plectomycetes.";
RL   Gene 130:265-270(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7765289; DOI=10.1007/bf00242947;
RA   Gouka R.J., van Hartingsveldt W., Bovenberg R.A., van Zeijl C.M.,
RA   van den Hondel C.A., van Gorcom R.F.;
RT   "Development of a new transformant selection system for Penicillium
RT   chrysogenum: isolation and characterization of the P. chrysogenum acetyl-
RT   coenzyme A synthetase gene (facA) and its use as a homologous selection
RT   marker.";
RL   Appl. Microbiol. Biotechnol. 38:514-519(1993).
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   -!- PATHWAY: Ketone degradation; acetoin degradation.
CC   -!- PATHWAY: Antibiotic biosynthesis; penicillin biosynthesis.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; S54801; AAC60546.1; -; Genomic_DNA.
DR   EMBL; L09598; AAA02921.1; -; Unassigned_DNA.
DR   PIR; JN0781; JN0781.
DR   AlphaFoldDB; P36333; -.
DR   SMR; P36333; -.
DR   PRIDE; P36333; -.
DR   OMA; DHWWHDL; -.
DR   PhylomeDB; P36333; -.
DR   UniPathway; UPA00040; -.
DR   UniPathway; UPA00474; -.
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:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   GO; GO:0042318; P:penicillin biosynthetic process; IEA:UniProtKB-UniPathway.
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   Acetoin catabolism; ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..669
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208417"
FT   BINDING         211..214
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         404..406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         428..433
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         519
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         534
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         542
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         545
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         602
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   669 AA;  74287 MW;  7C05220D321D736C CRC64;
     MSDGPIQPPK PAVVHEAHEV DTFHVPKAFH DKHPSGTHIK DIEEYKKLYE ESIKSPDTFW
     ARMARELLTF DKDFETTHHG SFENGDNAWF VEGRLNASFN CVDRHALKNP DKVAIIYEAD
     EPNEGRKITY GELMREVSRV AWTLKERGVK KGDTVGIYLP MIPEAVIAFL ACSRIGAVHS
     VVFAGFSSDS LRDRVLDASS KVIITSDEGK RGGKIIGTKK IVDEAMKQCP DVHTVLVYKR
     TGAEVPWTAG RDIWWHEEVE KYPNYLAPES VSSEDPLFLL YTSGSTGKPK GVMHTTAGYL
     LGAAMTGKYV FDIHDDDRYF CGGDVGWITG HTYVVYAPLL LGCATVVFES TPAYPNFSRY
     WDVIDKHDVT QFYVAPTALR LLKRAGDEHI HHKMHSLRIL GSVGEPIAAE VWKWYFECVG
     KEEAHICDTY WQTETGSHVI TPLGGITPTK PGSASLPFFG IEPAIIDPVS GEEIVGNDVE
     GVLAFKQPWP SMARTVWGAH KRYMDTYLNV YKGYYFTGDG AGRDHDGYYW IRGRVDDVVN
     VSGHRLSTAE IEAALLEHPS VAEAAVVGIA DELTGQAVNA FVSLKEGKPT EQISKDLAMQ
     VRKSIGPFAA PKAVFVVDDL PKTRSGKIMR RILRKILSGE EDSLGDTSTL SDPSVVDKII
     ETVHSARQK