ID   ACSA_PHYB8              Reviewed;         672 AA.
AC   Q01576;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
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;
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RX   PubMed=7914670; DOI=10.1007/bf00285455;
RA   Garre V., Murillo F.J., Torres-Martinez S.;
RT   "Isolation of the facA (acetyl-CoA synthetase) gene of Phycomyces
RT   blakesleeanus.";
RL   Mol. Gen. Genet. 244:278-286(1994).
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   -!- INDUCTION: By acetate.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; M94729; AAA53586.1; -; Genomic_DNA.
DR   PIR; S46276; S46276.
DR   AlphaFoldDB; Q01576; -.
DR   SMR; Q01576; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..672
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208418"
FT   BINDING         205..208
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         600
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   672 AA;  74775 MW;  DA6BCBA35252034E CRC64;
     MLDKTTIDGQ EDIVTHPVPK RLLNSAECPT PHVNSLEQYK SMWKESVEQP EKFFGNLGRE
     LLSWSKPFET VQYGSFEAGD VAWFLEGELN ASYNCVDRHA FKNPDKIAII HEGDEPDQVR
     RITYGELLRE VCRMANVLKG LGVRKGDPVA IYMPMIPETI VAILACARIG AIHSVVFAGF
     SAEILRDRVV DCATRVVLTS DEGRRGGKNI ATKCIVDEAL RDYENHSVEH VLVFRRTGSP
     VPWVQGRDVW WHEEMAKART FCSPEPMSAE DPLFLLYTSG STGTPKGILH TTGGYLLGVA
     ATVKYIFDYQ ENDIYACMAD IGWVTGHSYI VYGPLTLGAT TVLFESTPTY PNPSRFWQLI
     EKHKITQFYT APTAIRALQR LGDQWLDNID MSSLRVLGSV GEPINREAWD WYNEKVGKGR
     CAVVDTYWQT ETGSIIVSPL PGATPTKPGS ATLPFFGIDP VLLDPTTGKE LTATGQTGVL
     AIRKPRPSMA RSVYNNHSRF VETYLKPYPG YYFTGDGALR DDDGYIWIRG RVDDVINVSG
     HRLSTSEIES ALVNHEAVAE SAVVGAHDDL TGQCIHAFVS LKPHIQIADG LEKVLTLQVR
     KTIGPFAAPR RIYIVSDHPK TRSGKIMRRI LRKIVNGEHD QLGDISTLAD PSIVAVLINK
     VQRLNTEANI YI