ID   ACSA_CRYPV              Reviewed;         694 AA.
AC   Q27549;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=ACS;
OS   Cryptosporidium parvum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=5807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KSU-1;
RX   PubMed=8636846; DOI=10.2307/3284079;
RA   Khramtsov N.V., Blunt D.S., Montelone B.A., Upton S.J.;
RT   "The putative acetyl-CoA synthetase gene of Cryptosporidium parvum and a
RT   new conserved protein motif in acetyl-CoA synthetases.";
RL   J. Parasitol. 82:423-427(1996).
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}.
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; U24082; AAC47128.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q27549; -.
DR   SMR; Q27549; -.
DR   VEuPathDB; CryptoDB:cgd1_3710; -.
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..694
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208410"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         229..232
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         423..425
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         447..452
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         536
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         551
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         559
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         562
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         628
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   694 AA;  77971 MW;  5BA42E16E9AEE63C CRC64;
     MSDKRPRSPC SNNNDELNDS SVLTENMDTV ATRSKNLPFH ETYKSKPTPA DKPYRVDGID
     KYKELYEQSI RDPEGFWSQM ARKELRWLRD FTKVRSSGTC LQDRLAWFLN GKLNVCDNCV
     DRWAEIQPNT TALIWEGDDP SSIRHISYIE LFRNVCKMAN VLKRFGIKKG DSVGIYMPMI
     PETIYTMLAC ARIGAVHMVV FAGFAAQNLL ERLVNARCKI VVTADQGSRG KKIINLKDVV
     DKALEKIPEI KTCIVFRHLN GPIEFVKGRD FDGETLMRSE KPYCPLEDMD SEDPLFYLYT
     SGSTGTPKGV QHSTAGYLLY AAVTQKYLFN IHPGDIFGCA GDIGWITGHS YLVYAPLCNG
     ITTLIFEGVP TYPNAGRYWE MVERHRITHF YAAPTAIRTL KRLGDDFVKK HDRSSLRVLG
     SVGEPINPSA WRWYHSVVGE ERCSIVDTYW QTETGGIVIA PIPGCFDTKP GSATFPFFGI
     EPAILDPDTG KEIDGPGSGV LCIKNSWPGM FRGIFGAHYL HEIYTKPFPK YYFTGDGVLR
     DQDGYLWITG RIDDTINVSG HRLSSKEIED ALTNHFGIAE AAAVAIDHDV KGNALVCFVV
     LKDSGNRTFD LNNSSPHPFE YELRMCVRTQ IGPVATPDHI IVVENIPKTR SGKVVRRLLR
     KIATGCNDYG DISTVANPEC IKSIESSWAQ YLKR