ID ACDB2_PYRFU Reviewed; 236 AA.
AC Q8TZY8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Acetate--CoA ligase [ADP-forming] II subunit beta {ECO:0000305};
DE EC=6.2.1.13 {ECO:0000269|PubMed:8830684};
DE AltName: Full=ADP-forming acetyl coenzyme A synthetase II subunit beta {ECO:0000305};
DE Short=ACS II subunit beta {ECO:0000305};
GN Name=acdBII {ECO:0000303|PubMed:10482538};
GN OrderedLocusNames=PF1837 {ECO:0000312|EMBL:AAL81961.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8830684; DOI=10.1128/jb.178.20.5897-5903.1996;
RA Mai X., Adams M.W.;
RT "Purification and characterization of two reversible and ADP-dependent
RT acetyl coenzyme A synthetases from the hyperthermophilic archaeon
RT Pyrococcus furiosus.";
RL J. Bacteriol. 178:5897-5903(1996).
RN [3]
RP GENE NAME.
RX PubMed=10482538; DOI=10.1128/jb.181.18.5885-5888.1999;
RA Musfeldt M., Selig M., Schonheit P.;
RT "Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic
RT Archaeon pyrococcus furiosus: identification, cloning, separate expression
RT of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro
RT reconstitution of the active heterotetrameric enzyme from its recombinant
RT subunits.";
RL J. Bacteriol. 181:5885-5888(1999).
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 phenylacetyl-CoA, indoleacetyl-CoA and isobutyryl-CoA, but not
CC succinyl-CoA. Seems to be involved primarily in the degradation of
CC aryl-CoA esters to the corresponding acids. Participates in the
CC conversion of acetyl-CoA to acetate and in the degradation of branched-
CC chain amino acids via branched-chain-acyl-CoA esters.
CC {ECO:0000269|PubMed:8830684}.
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:8830684};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=61 uM for ADP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=236 uM for GDP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=580 uM for phosphate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=26 uM for acetyl-CoA (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=12 uM for isobutyryl-CoA (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=4 uM for phenylacetyl-CoA (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=326 uM for ATP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=770 uM for GTP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=74 uM for CoA (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=10700 uM for acetate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=5800 uM for isobutyrate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=2000 uM for indoleacetate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=768 uM for phenylacetate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC Note=kcat is 115 sec(-1) for ADP. kcat is 21 sec(-1) for GDP. kcat is
CC 117 sec(-1) for phosphate. kcat is 42 sec(-1) for acetyl-CoA. kcat is
CC 8 sec(-1) for isobutyryl-CoA. kcat is 138 sec(-1) for phenylacetyl-
CC CoA. kcat is 68 sec(-1) for ATP. kcat is 27 sec(-1) for GTP. kcat is
CC 70 sec(-1) for CoA. kcat is 67 sec(-1) for acetate. kcat is 22 sec(-
CC 1) for isobutyrate. kcat is 66 sec(-1) for indoleacetate. kcat is 89
CC sec(-1) for phenylacetate. {ECO:0000269|PubMed:8830684};
CC pH dependence:
CC Optimum pH is 9.0 (at 80 degrees Celsius).
CC {ECO:0000269|PubMed:8830684};
CC Temperature dependence:
CC Optimum temperature is above 90 degrees Celsius (at pH 8.0).
CC {ECO:0000269|PubMed:8830684};
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000269|PubMed:8830684}.
CC -!- SIMILARITY: Belongs to the acetate CoA ligase beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AE009950; AAL81961.1; -; Genomic_DNA.
DR RefSeq; WP_011012977.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TZY8; -.
DR SMR; Q8TZY8; -.
DR STRING; 186497.PF1837; -.
DR PaxDb; 186497-PF1837; -.
DR GeneID; 41713656; -.
DR KEGG; pfu:PF1837; -.
DR PATRIC; fig|186497.12.peg.1908; -.
DR eggNOG; arCOG01338; Archaea.
DR HOGENOM; CLU_063044_1_1_2; -.
DR OrthoDB; 18103at2157; -.
DR PhylomeDB; Q8TZY8; -.
DR SABIO-RK; Q8TZY8; -.
DR Proteomes; UP000001013; 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; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..236
FT /note="Acetate--CoA ligase [ADP-forming] II subunit beta"
FT /id="PRO_0000430523"
FT DOMAIN 26..62
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 52..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 236 AA; 26444 MW; 6B171459C420EBBA CRC64;
MKGEALKIIE EVLAQGRTAM VEYEAKQVLK AYGLPVPEEK LAKTLDEALK YAEEIGYPVA
MKLMSPQILH KSDAKVVMLN IKSPEELKKK WEEIHENARK YRPDAEIFGV LIAPMLKPGR
EVIIGVTEDP QFGHAIMFGL GGIFVEILKD VTFRIIPITE KDARKMITEI KAYPILAGAR
GEEPADIEAI VDMLLKVSKL VDDLKDYIKE MDLNPVFVYR KGEGAVVVDA RIILKG
//
