ACDA1_PYRFU
ID ACDA1_PYRFU Reviewed; 462 AA.
AC E7FI45; Q7LWY1; Q9Y8L1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Acetate--CoA ligase [ADP-forming] I subunit alpha {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 alpha {ECO:0000305};
DE Short=ACS I subunit alpha {ECO:0000305};
GN Name=acdAI {ECO:0000303|PubMed:10482538};
GN OrderedLocusNames=PF1540 {ECO:0000312|EMBL:AAL81664.1};
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 2-47, 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 2-33, 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 alpha subunit family.
CC {ECO:0000305}.
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DR EMBL; AJ240061; CAB46516.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81664.1; -; Genomic_DNA.
DR PIR; T48661; T48661.
DR RefSeq; WP_011012687.1; NC_018092.1.
DR AlphaFoldDB; E7FI45; -.
DR SMR; E7FI45; -.
DR IntAct; E7FI45; 45.
DR STRING; 186497.PF1540; -.
DR PRIDE; E7FI45; -.
DR EnsemblBacteria; AAL81664; AAL81664; PF1540.
DR GeneID; 41713359; -.
DR KEGG; pfu:PF1540; -.
DR PATRIC; fig|186497.12.peg.1606; -.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_3_2; -.
DR OMA; GPNIFGY; -.
DR OrthoDB; 15044at2157; -.
DR PhylomeDB; E7FI45; -.
DR BioCyc; MetaCyc:MON-11822; -.
DR BRENDA; 6.2.1.13; 5243.
DR SABIO-RK; E7FI45; -.
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 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; Cytoplasm; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8830684,
FT ECO:0000269|PubMed:9119024"
FT CHAIN 2..462
FT /note="Acetate--CoA ligase [ADP-forming] I subunit alpha"
FT /id="PRO_0000430520"
FT CONFLICT 2
FT /note="S -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 49965 MW; 756BB577C8112504 CRC64;
MSLEALFNPK SVAVIGASAK PGKIGYAIMK NLIEYGYEGK IYPVNIKGGE IEINGRKFKV
YKSVLEIPDE VDMAVIVVPA KFVPQVLEEC GQKGVKVVPI ISSGFGELGE EGKKVEQQLV
ETARKYGMRI LGPNIFGVVY TPAKLNATFG PTDVLPGPLA LISQSGALGI ALMGWTILEK
IGLSAVVSVG NKADIDDADL LEFFKDDENT RAILIYMEGV KDGRRFMEVA KEVSKKKPII
VIKAGRSERG AKAAASHTGS LAGSDKVYSA AFKQSGVLRA YTIGEAFDWA RALSNLPEPQ
GDNVVIITNG GGIGVMATDA AEEEGLHLYD NLEELKIFAN HMPPFGSYKN PVDLTGMADG
KSYEGAIRDA LAHPEMHSIA VLYCQTAVLD PRELAEIVIR EYNESGRKKP LVVAIVGGIE
AKEAIDMLNE NGIPAYPEPE RAIKALSALY KWSKWKAKHK EK
