ACD1_ARCFU
ID ACD1_ARCFU Reviewed; 685 AA.
AC O29057;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acetate--CoA ligase [ADP-forming] I {ECO:0000305};
DE EC=6.2.1.13 {ECO:0000269|PubMed:11790732};
DE AltName: Full=ADP-forming acetyl coenzyme A synthetase I {ECO:0000305};
DE Short=ACS I {ECO:0000305};
GN OrderedLocusNames=AF_1211 {ECO:0000312|EMBL:AAB90033.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP 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 reversible formation of acetate and ATP from
CC acetyl-CoA by using ADP and phosphate. Can use other substrates such as
CC propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be
CC involved primarily in the conversion of acetyl-CoA to acetate.
CC Participates in the degradation of branched-chain amino acids via
CC branched-chain-acyl-CoA esters. {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 -!- ACTIVITY REGULATION: Activity requires divalent metal cations.
CC {ECO:0000269|PubMed:11790732}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for acetyl-CoA {ECO:0000269|PubMed:11790732};
CC KM=7 uM for ADP {ECO:0000269|PubMed:11790732};
CC KM=110 uM for phosphate {ECO:0000269|PubMed:11790732};
CC KM=340 uM for acetate {ECO:0000269|PubMed:11790732};
CC KM=100 uM for phenylacetate {ECO:0000269|PubMed:11790732};
CC KM=133 uM for ATP {ECO:0000269|PubMed:11790732};
CC KM=27 uM for CoA {ECO:0000269|PubMed:11790732};
CC Note=kcat is 95 sec(-1) for acetyl-CoA. kcat is 70 sec(-1) for ADP.
CC kcat is 58 sec(-1) for phosphate. kcat is 138 sec(-1) for acetate.
CC kcat is 11.5 sec(-1) for phenylacetate. kcat is 150 sec(-1) for ATP.
CC kcat is 110 sec(-1) for CoA. {ECO:0000269|PubMed:11790732};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:11790732};
CC Temperature dependence:
CC Optimum temperature is 77 degrees Celsius.
CC {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; AE000782; AAB90033.1; -; Genomic_DNA.
DR PIR; B69401; B69401.
DR RefSeq; WP_010878706.1; NC_000917.1.
DR AlphaFoldDB; O29057; -.
DR SMR; O29057; -.
DR STRING; 224325.AF_1211; -.
DR PRIDE; O29057; -.
DR EnsemblBacteria; AAB90033; AAB90033; AF_1211.
DR GeneID; 1484435; -.
DR KEGG; afu:AF_1211; -.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_3_1_2; -.
DR OMA; CVPPIFI; -.
DR OrthoDB; 2789at2157; -.
DR PhylomeDB; O29057; -.
DR BioCyc; MetaCyc:AF_RS06130-MON; -.
DR BRENDA; 6.2.1.B11; 414.
DR SABIO-RK; O29057; -.
DR Proteomes; UP000002199; 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 GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 2.
DR InterPro; IPR014089; AcCoA-synth-alpha.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
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; 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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..685
FT /note="Acetate--CoA ligase [ADP-forming] I"
FT /id="PRO_0000430518"
FT DOMAIN 477..513
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 503..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 685 AA; 74698 MW; BFC4A6D8FE39942F CRC64;
MERLFYPKVV AVIGASPQEG KVGNTIMKNL RNFSGTVYAV NPKYREILGF PCYPSVLKIP
ENVDLAIIVV PAKLVPKAVE ECGRKDVEGA VVISAGFKEA GIEGAKLERE LVEVAERYGV
KLVGPNCLGM INTEIAMNAT FSRVAPEKGR IAFLSQSGAF ILAVLEWSKR NGVGFSKVVS
LGNKAMLDES DFLEYLAKDD STDVILIYME GVEDGRKFMR VAKSVARRKP VVVMKAGKSQ
SGAKAASSHT GSLAGSYEAY RAAFRQSGVI EASSVEELFD FALLLLKYRK AGNLAILTNS
GGPGVMAADA CDQFGVPLAN FNFETIRKLK EFLPAESNFY NPVDILGDAS AERFSRSLQI
LSEDENVDIV LTILTPTAQM DFLKAAESVV GKNAVCCFMG GESVDESERI LRSSGIPNFF
DPVRAVRAIS VLGRYSKISA KERVKEDLDV SVEREKAEEI IEKLLESGGR VVGAEGLPVL
EAYGIEVAPY GIARNVDEAR DIAESIGYPV VLKVVSPDVV HKSDVGGVKL NVGENDLEKA
FFEILSNVEG RMPKARIEGV LVQKMVDGGK ELIVGMKRDP QFGPMIMFGM GGVYVEVLKD
VSFRIAPITR REAHEMVREV KAYRILRGLR GEKPADIDAI ADLLLRVSKL SLDHPEVLEM
DLNPVKVFES GYAVVDFRMV LGEEV
