ACDA2_PYRFU
ID ACDA2_PYRFU Reviewed; 457 AA.
AC Q8U3D6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Acetate--CoA ligase [ADP-forming] II subunit alpha {ECO:0000305};
DE EC=6.2.1.13 {ECO:0000269|PubMed:8830684};
DE AltName: Full=ADP-forming acetyl coenzyme A synthetase II subunit alpha {ECO:0000305};
DE Short=ACS II subunit alpha {ECO:0000305};
GN Name=acdAII {ECO:0000303|PubMed:10482538};
GN OrderedLocusNames=PF0532 {ECO:0000312|EMBL:AAL80656.1};
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 1-39, 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 alpha subunit family.
CC {ECO:0000305}.
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DR EMBL; AE009950; AAL80656.1; -; Genomic_DNA.
DR RefSeq; WP_011011649.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U3D6; -.
DR SMR; Q8U3D6; -.
DR STRING; 186497.PF0532; -.
DR PRIDE; Q8U3D6; -.
DR EnsemblBacteria; AAL80656; AAL80656; PF0532.
DR GeneID; 41712334; -.
DR KEGG; pfu:PF0532; -.
DR PATRIC; fig|186497.12.peg.556; -.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_3_2; -.
DR OMA; ICVVPTF; -.
DR OrthoDB; 15044at2157; -.
DR PhylomeDB; Q8U3D6; -.
DR SABIO-RK; Q8U3D6; -.
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 Gene3D; 3.40.50.261; -; 2.
DR InterPro; IPR014089; AcCoA-synth-alpha.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_dom.
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; PF19045; Ligase_CoA_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 TIGRFAMs; TIGR02717; AcCoA-syn-alpha; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..457
FT /note="Acetate--CoA ligase [ADP-forming] II subunit alpha"
FT /id="PRO_0000430522"
SQ SEQUENCE 457 AA; 49263 MW; F28D69E0412EC53A CRC64;
MLDYFFNPRG IAVIGASNDP KKLGYEVFKN LKEYQGGKVY PVNVREEEVQ GVKAYKSVKE
IPGEVDLAII VVPKKFVKQT LIECGEKGVK GVVIITAGFG ETGEEGKREE KELVEIAHKY
GMRIIGPNCV GIMNTHANLN ATFITVAKKG NVAFISQSGA LGAGIVYKTI KEDIGFSKFI
SVGNMADLDF ADLMEYLADT QEDKAIALYI EGIKDGRRFI EVAKKVTKKK PVIALKAGKS
ESGSRAAASH TGSLAGSWKI YEAAFKQSGV LVANTIDEML SMARAFTQPL PKGNRVAIMT
NAGGPGVLTA DEIDKRGLKL ANLEEKTIEE LRSFLPPMAA VKNPVDMIAS ARGEDYYRTA
KLLLQDPNVD ILIAICVVPT FAGMTPTEHA EGIIRAVKEV NNGKPVLALF MAGYVSEKAK
ELLEKNGIPT YERPEDVAAA AYALVQQAKN VGGGVNG
