ID   ACD_METJA               Reviewed;         704 AA.
AC   Q58010;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Acetate--CoA ligase [ADP-forming] {ECO:0000305};
DE            EC=6.2.1.13 {ECO:0000269|PubMed:11790732};
DE   AltName: Full=ADP-forming acetyl coenzyme A synthetase {ECO:0000305};
DE            Short=ACS {ECO:0000305};
GN   OrderedLocusNames=MJ0590 {ECO:0000312|EMBL:AAB98580.1};
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=11790732; DOI=10.1128/jb.184.3.636-644.2002;
RA   Musfeldt M., Schoenheit P.;
RT   "Novel type of ADP-forming acetyl coenzyme A synthetase in
RT   hyperthermophilic archaea: heterologous expression and characterization of
RT   isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the
RT   methanogen Methanococcus jannaschii.";
RL   J. Bacteriol. 184:636-644(2002).
CC   -!- FUNCTION: Catalyzes the formation of acetate and ATP from acetyl-CoA by
CC       using ADP and phosphate. Can also use butyryl-CoA, but not
CC       phenylacetyl-CoA. Cannot catalyze the reverse reaction.
CC       {ECO:0000269|PubMed:11790732}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate;
CC         Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456216; EC=6.2.1.13;
CC         Evidence={ECO:0000269|PubMed:11790732};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=37 uM for acetyl-CoA {ECO:0000269|PubMed:11790732};
CC         KM=15 uM for ADP {ECO:0000269|PubMed:11790732};
CC         KM=470 uM for phosphate {ECO:0000269|PubMed:11790732};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11790732}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the acetate CoA
CC       ligase alpha subunit family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the acetate CoA
CC       ligase beta subunit family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98580.1; -; Genomic_DNA.
DR   PIR; F64373; F64373.
DR   RefSeq; WP_010870094.1; NC_000909.1.
DR   AlphaFoldDB; Q58010; -.
DR   SMR; Q58010; -.
DR   STRING; 243232.MJ_0590; -.
DR   EnsemblBacteria; AAB98580; AAB98580; MJ_0590.
DR   GeneID; 1451455; -.
DR   KEGG; mja:MJ_0590; -.
DR   eggNOG; arCOG01340; Archaea.
DR   HOGENOM; CLU_007415_3_1_2; -.
DR   InParanoid; Q58010; -.
DR   OMA; SFMSQSG; -.
DR   OrthoDB; 2789at2157; -.
DR   PhylomeDB; Q58010; -.
DR   BRENDA; 6.2.1.B11; 3260.
DR   SABIO-RK; Q58010; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 2.
DR   InterPro; IPR014089; AcCoA-synth-alpha.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR043938; Ligase_CoA_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF19045; Ligase_CoA_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 2.
DR   TIGRFAMs; TIGR02717; AcCoA-syn-alpha; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..704
FT                   /note="Acetate--CoA ligase [ADP-forming]"
FT                   /id="PRO_0000106948"
SQ   SEQUENCE   704 AA;  78172 MW;  A60E5F19DA1B2C58 CRC64;
     MWGRDYELKY ISYPKSVAII GASKTEGKVG YAIMKNLKDF NGKIYPINPK YDEIFGIKCY
     KSVLDVEDDI DLAVIVVPNI VVPKVLEECG KKGVKGAVII TAGFSEVGNY ELENKIKEIA
     KRYNIRIIGP NCLGIMNTHI NLNATFAKVF PPKGGVSIIS QSGAVLNAIL DIAPLLNIGF
     SKVVSIGNKA DIQESDLLEY FLDDEDTKIV VLYIEGLKDK RFLKVAKKLS KKKPIIALKS
     GRTEVGKKAA KSHTGSLAGE DVIYEAAFKE AGIIRAYTFE ELVDLIHLFS TQPTISSNEI
     GIITNAGGFG VLAADSCVDY NMKLSNFEKS TIEKLKNILP PTANISNPLD IIGDATPERY
     KKVIEVLAED SNVKGLLVIL TPQEMTKPLE VAKSIIEVKN SHKEFKNKPL ITSFVGGVSV
     KGAKSYLRKN GIPAYITPEN GVKALSHLYK YSLMKVKEDY DEYLENIKEE FIKITEENKE
     IIKELLSNPN EYTAKKLLSI YGLPVPKGYL AKNEDEALEY CKKLGKCVMK IVSPQIIHKT
     EAGGVIINPK NPKEAFKKLI ENAKEYAKRM GIDNLIIEGV LVEEFIEKDM MEIIIGAKRD
     DIFGSVVMVG LGGVFVEVLK DVSFGISPIT RDFAHEMLRE LKSYKVLEGV RGRPKRDINF
     IVDTLIKIGV FMDIHKEIKE LDLNPVFVFN EKEGGCIGDA RIIK