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Database: UniProt
Entry: Q8TZY8
LinkDB: Q8TZY8
Original site: Q8TZY8 
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   16-JAN-2019, entry version 83.
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;
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   [2]
RP   PROTEIN SEQUENCE OF 1-30, 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   [3]
RP   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).
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 phenylacetyl-CoA, indoleacetyl-CoA and
CC       isobutyryl-CoA, but not succinyl-CoA. Seems to be involved
CC       primarily in the degradation of aryl-CoA esters to the
CC       corresponding acids. Participates in the conversion of acetyl-CoA
CC       to acetate and in the degradation of branched-chain amino acids
CC       via branched-chain-acyl-CoA esters. {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.
CC         kcat is 117 sec(-1) for phosphate. kcat is 42 sec(-1) for
CC         acetyl-CoA. kcat is 8 sec(-1) for isobutyryl-CoA. kcat is 138
CC         sec(-1) for phenylacetyl-CoA. kcat is 68 sec(-1) for ATP. kcat
CC         is 27 sec(-1) for GTP. kcat is 70 sec(-1) for CoA. kcat is 67
CC         sec(-1) for acetate. kcat is 22 sec(-1) for isobutyrate. kcat is
CC         66 sec(-1) for indoleacetate. kcat is 89 sec(-1) for
CC         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}.
DR   EMBL; AE009950; AAL81961.1; -; Genomic_DNA.
DR   RefSeq; WP_011012977.1; NC_003413.1.
DR   ProteinModelPortal; Q8TZY8; -.
DR   SMR; Q8TZY8; -.
DR   STRING; 186497.PF1837; -.
DR   PRIDE; Q8TZY8; -.
DR   EnsemblBacteria; AAL81961; AAL81961; PF1837.
DR   GeneID; 1469716; -.
DR   KEGG; pfu:PF1837; -.
DR   PATRIC; fig|186497.12.peg.1908; -.
DR   eggNOG; arCOG01338; Archaea.
DR   eggNOG; COG1042; LUCA.
DR   HOGENOM; HOG000132014; -.
DR   KO; K22224; -.
DR   OMA; EDPQFGH; -.
DR   OrthoDB; 65977at2157; -.
DR   BioCyc; PFUR186497:G1FZR-1896-MONOMER; -.
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; -; 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; Direct protein sequencing; Ligase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    236       Acetate--CoA ligase [ADP-forming] II
FT                                subunit beta.
FT                                /FTId=PRO_0000430523.
FT   DOMAIN       26     62       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND      52     63       ATP. {ECO:0000255|PROSITE-
FT                                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
//
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