ACD2_ARCFU
ID ACD2_ARCFU Reviewed; 673 AA.
AC O28341;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acetate--CoA ligase [ADP-forming] II {ECO:0000305};
DE EC=6.2.1.13 {ECO:0000269|PubMed:11790732};
DE AltName: Full=ADP-forming acetyl coenzyme A synthetase II {ECO:0000305};
DE Short=ACS II {ECO:0000305};
GN OrderedLocusNames=AF_1938 {ECO:0000312|EMBL:AAB89317.1};
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 conversion of a variety of acids to
CC the corresponding acyl-CoA esters. Shows the highest activity with the
CC aryl acids, indoleacetate and phenylacetate, as compared to acetate. In
CC the reverse direction, phenylacetyl-CoA is the best substrate. Seems to
CC be involved primarily in the degradation of aryl-CoA esters to the
CC corresponding acids. Participates in the degradation of branched-chain
CC amino acids via branched-chain-acyl-CoA esters.
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 -!- ACTIVITY REGULATION: Activity requires divalent metal cations.
CC {ECO:0000269|PubMed:11790732}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for phenylacetyl-CoA {ECO:0000269|PubMed:11790732};
CC KM=2580 uM for acetate {ECO:0000269|PubMed:11790732};
CC KM=1240 uM for indole-3-acetate {ECO:0000269|PubMed:11790732};
CC KM=2500 uM for phenylacetate {ECO:0000269|PubMed:11790732};
CC KM=30 uM for ATP {ECO:0000269|PubMed:11790732};
CC KM=530 uM for CoA {ECO:0000269|PubMed:11790732};
CC Note=kcat is 2.3 sec(-1) for phenylacetyl-CoA. kcat is 1.84 sec(-1)
CC for acetate. kcat is 3.45 sec(-1) for indole-3-acetate. kcat is 3
CC sec(-1) for phenylacetate. kcat is 3 sec(-1) for ATP. kcat is 2.9
CC sec(-1) for CoA. {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 beta subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the acetate CoA
CC ligase alpha subunit family. {ECO:0000305}.
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DR EMBL; AE000782; AAB89317.1; -; Genomic_DNA.
DR PIR; A69492; A69492.
DR RefSeq; WP_010879431.1; NC_000917.1.
DR AlphaFoldDB; O28341; -.
DR SMR; O28341; -.
DR STRING; 224325.AF_1938; -.
DR PRIDE; O28341; -.
DR EnsemblBacteria; AAB89317; AAB89317; AF_1938.
DR GeneID; 24795682; -.
DR KEGG; afu:AF_1938; -.
DR eggNOG; arCOG01338; Archaea.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_2_2; -.
DR OMA; MAKINEW; -.
DR OrthoDB; 10768at2157; -.
DR PhylomeDB; O28341; -.
DR BioCyc; MetaCyc:AF_RS09735-MON; -.
DR BRENDA; 6.2.1.B11; 414.
DR SABIO-RK; O28341; -.
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; 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 PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..673
FT /note="Acetate--CoA ligase [ADP-forming] II"
FT /id="PRO_0000430519"
FT DOMAIN 9..45
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 35..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 673 AA; 74412 MW; 428E559838806B00 CRC64;
MLLLEHESKA LLEKYGIKTA KCIFCETEEQ AVKAAKEIGF PVVMKVAGRE IVHKSDVGGV
ILNVKSEDEV REVFQRLMSI PKAEGVNIQP QLEKGIEVIV GVAENEQFGS VAMFGLGGVF
VEVLKDVSFR LLPLTRRDAE EMVREVKGYK LLEGYRRVKG DVGAVVDLLL KLNEVVERES
IVEMDLNPVF VYERGAVVAD ARIVVGERKR FDYTIPDLRD LFYPKSVAVI GASRTVGKPG
FNIVWNLKQN GFMGKIYPVN PNADKILELK CYPSILDIPD EVDMAIIAVP AKIVPEVMAE
CAQKGIKGAV IVSSGFSEEG EKGAEYERRV LEIAKKHGIR IFGPNTTGVL NTENGFITSF
AIQPVIKKGN IGIIAQTGLF LGIMMDIVTS NHPSIGFSKI VGMGNKIDVE DYEVLDFLLK
DEQTKVIGIY MEGIKNGRAF YDVASSAEKP IVVFKSGRTE YGQKAAMSHT ASICGDDDVF
DAVCRQANLV RVYSFDELFD VTKAFSLQPL PKGDRVAIIH YTGSGCVQGS DAAYFAGLKL
AEFSKDTVDK ISEVTPEWHN VNNPIDIWPM VEYYGAFKAY QTAIEAVMED EGVDSVIACV
WANRLINADF EPDYKSLKKY GKPIYFCVEG ARDVVFDHKN ALELNGIPVY TNVINAVNVL
GKVTKYAKRR IQS
