ACDB1_PYRFU
ID ACDB1_PYRFU Reviewed; 232 AA.
AC E7FHP1; Q7LWX9; Q9Y8L0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Acetate--CoA ligase [ADP-forming] I subunit beta {ECO:0000305};
DE EC=6.2.1.13 {ECO:0000269|PubMed:10482538, ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024};
DE AltName: Full=ADP-forming acetyl coenzyme A synthetase I subunit beta {ECO:0000305};
DE Short=ACS I subunit beta {ECO:0000305};
GN Name=acdBI {ECO:0000303|PubMed:10482538};
GN OrderedLocusNames=PF1787 {ECO:0000312|EMBL:AAL81911.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP AND 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).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-27, 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 [4]
RP PROTEIN SEQUENCE OF 1-24, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=9119024; DOI=10.1111/j.1432-1033.1997.00561.x;
RA Glasemacher J., Bock A.K., Schmid R., Schoenheit P.;
RT "Purification and properties of acetyl-CoA synthetase (ADP-forming), an
RT archaeal enzyme of acetate formation and ATP synthesis, from the
RT hyperthermophile Pyrococcus furiosus.";
RL Eur. J. Biochem. 244:561-567(1997).
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 isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-
CC CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily
CC in the conversion of acetyl-CoA to acetate. Participates in the
CC degradation of branched-chain amino acids via branched-chain-acyl-CoA
CC esters. {ECO:0000269|PubMed:10482538, ECO:0000269|PubMed:8830684,
CC ECO:0000269|PubMed:9119024}.
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:10482538, ECO:0000269|PubMed:8830684,
CC ECO:0000269|PubMed:9119024};
CC -!- ACTIVITY REGULATION: Activity is dependent on magnesium.
CC {ECO:0000269|PubMed:9119024}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for ADP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=60 uM for ADP (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:9119024};
CC KM=132 uM for GDP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=396 uM for phosphate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=200 uM for phosphate (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:9119024};
CC KM=25 uM for acetyl-CoA (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=17 uM for acetyl-CoA (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:9119024};
CC KM=29 uM for isobutyryl-CoA (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=477 uM for ATP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=80 uM for ATP (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:9119024};
CC KM=430 uM for GTP (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=18 uM for CoA (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=30 uM for CoA (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:9119024};
CC KM=1100 uM for acetate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC KM=660 uM for acetate (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:9119024};
CC KM=457 uM for isobutyrate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:8830684};
CC Note=kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat
CC is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA.
CC kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP.
CC kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1) for CoA. kcat is 65
CC sec(-1) for acetate. kcat is 55 sec(-1) for isobutyrate.
CC {ECO:0000269|PubMed:8830684};
CC pH dependence:
CC Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684). Optimum
CC pH is 7.0 (at 55 degrees Celsius) (PubMed:9119024).
CC {ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024};
CC Temperature dependence:
CC Optimum temperature is above 90 degrees Celsius.
CC {ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024};
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000269|PubMed:10482538, ECO:0000269|PubMed:8830684,
CC ECO:0000269|PubMed:9119024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9119024}.
CC -!- SIMILARITY: Belongs to the acetate CoA ligase beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AJ240062; CAB46517.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81911.1; -; Genomic_DNA.
DR PIR; T48662; T48662.
DR RefSeq; WP_011012928.1; NC_018092.1.
DR AlphaFoldDB; E7FHP1; -.
DR SMR; E7FHP1; -.
DR STRING; 186497.PF1787; -.
DR EnsemblBacteria; AAL81911; AAL81911; PF1787.
DR GeneID; 41713605; -.
DR KEGG; pfu:PF1787; -.
DR PATRIC; fig|186497.12.peg.1858; -.
DR eggNOG; arCOG01338; Archaea.
DR HOGENOM; CLU_063044_1_1_2; -.
DR OMA; FGPAIMF; -.
DR OrthoDB; 65977at2157; -.
DR PhylomeDB; E7FHP1; -.
DR BioCyc; MetaCyc:MON-11823; -.
DR BRENDA; 6.2.1.13; 5243.
DR SABIO-RK; E7FHP1; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..232
FT /note="Acetate--CoA ligase [ADP-forming] I subunit beta"
FT /id="PRO_0000430521"
FT DOMAIN 27..63
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 53..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT CONFLICT 20
FT /note="P -> R (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="E -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 25878 MW; 1C00A9AFD2A121D1 CRC64;
MDRVAKAREI IEKAKAENRP LVEPEAKEIL KLYGIPVPEF KVARNEEEAV KFSGEIGYPV
VMKIVSPQII HKSDAGGVKI NIKNDEEARE AFRTIMQNAR NYKPDADLWG VIIYRMLPLG
REVIVGMIRD PQFGPAVMFG LGGIFVEILK DVSFRVAPIT KEDALEMIRE IKAYPILAGA
RGEKPVNIEA LADIIVKVGE LALELPEIKE IDINPIFAYE DSAIAVDARM IL
