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Database: UniProt
Entry: E7FHP1
LinkDB: E7FHP1
Original site: E7FHP1 
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   16-JAN-2019, entry version 46.
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,
RP   SUBUNIT, AND GENE NAME.
RX   PubMed=10482538;
RA   Musfeldt M., Selig M., Schonheit P.;
RT   "Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic
RT   Archaeon pyrococcus furiosus: identification, cloning, separate
RT   expression of the encoding genes, acdAI and acdBI, in Escherichia
RT   coli, and in vitro reconstitution of the active heterotetrameric
RT   enzyme from its recombinant 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;
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
RT   P. horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-27, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL 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),
RT   an 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
CC       from acetyl-CoA by using ADP and phosphate. Can use other
CC       substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA,
CC       but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems
CC       to be involved primarily in the conversion of acetyl-CoA to
CC       acetate. Participates in the degradation of branched-chain amino
CC       acids via branched-chain-acyl-CoA esters.
CC       {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,
CC         ECO:0000269|PubMed:8830684, 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.
CC         kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for
CC         acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82
CC         sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1)
CC         for CoA. kcat is 65 sec(-1) for acetate. kcat is 55 sec(-1) for
CC         isobutyrate. {ECO:0000269|PubMed:8830684};
CC       pH dependence:
CC         Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684).
CC         Optimum 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}.
DR   EMBL; AJ240062; CAB46517.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81911.1; -; Genomic_DNA.
DR   PIR; T48662; T48662.
DR   RefSeq; WP_011012928.1; NC_003413.1.
DR   ProteinModelPortal; E7FHP1; -.
DR   SMR; E7FHP1; -.
DR   STRING; 186497.PF1787; -.
DR   PRIDE; E7FHP1; -.
DR   EnsemblBacteria; AAL81911; AAL81911; PF1787.
DR   GeneID; 1469666; -.
DR   KEGG; pfu:PF1787; -.
DR   PATRIC; fig|186497.12.peg.1858; -.
DR   eggNOG; arCOG01340; Archaea.
DR   eggNOG; COG1042; LUCA.
DR   HOGENOM; HOG000132014; -.
DR   KO; K22224; -.
DR   OMA; KPDADLW; -.
DR   OrthoDB; 65977at2157; -.
DR   BioCyc; MetaCyc:MONOMER-11823; -.
DR   BioCyc; PFUR186497:G1FZR-1845-MONOMER; -.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    232       Acetate--CoA ligase [ADP-forming] I
FT                                subunit beta.
FT                                /FTId=PRO_0000430521.
FT   DOMAIN       27     63       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND      53     64       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   CONFLICT     20     20       P -> R (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     23     23       E -> Q (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     25     25       E -> A (in Ref. 3; AA sequence).
FT                                {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
//
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