ACXC_XANP2
ID ACXC_XANP2 Reviewed; 168 AA.
AC Q8RM02;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Acetone carboxylase gamma subunit {ECO:0000312|EMBL:AAL17712.1};
DE EC=6.4.1.6;
GN Name=acxC {ECO:0000312|EMBL:AAL17712.1}; OrderedLocusNames=Xaut_3511;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL17712.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, AND
RP IDENTIFICATION.
RX PubMed=12003937; DOI=10.1128/jb.184.11.2969-2977.2002;
RA Sluis M.K., Larsen R.A., Krum J.G., Anderson R., Metcalf W.W., Ensign S.A.;
RT "Biochemical, molecular, and genetic analyses of the acetone carboxylases
RT from Xanthobacter autotrophicus strain Py2 and Rhodobacter capsulatus
RT strain B10.";
RL J. Bacteriol. 184:2969-2977(2002).
RN [2] {ECO:0000312|EMBL:ABS68740.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MASS SPECTROMETRY.
RX PubMed=9237998; DOI=10.1073/pnas.94.16.8456;
RA Sluis M.K., Ensign S.A.;
RT "Purification and characterization of acetone carboxylase from Xanthobacter
RT strain Py2.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8456-8461(1997).
CC -!- FUNCTION: Catalyzes the carboxylation of acetone to form acetoacetate.
CC Has a reduced activity on butanone, and no activity on 2-pentatone, 3-
CC pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate,
CC acetaldehyde, propionaldehyde and propylene oxide.
CC {ECO:0000269|PubMed:9237998}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetone + 2 ATP + 3 H2O + hydrogencarbonate = acetoacetate + 2
CC AMP + 4 H(+) + 4 phosphate; Xref=Rhea:RHEA:18385, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:15347, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456215; EC=6.4.1.6;
CC Evidence={ECO:0000269|PubMed:9237998};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:9237998};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9237998};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:9237998};
CC Note=Zn(2+). The heterohexamer contains tightly bound iron, manganese
CC and zinc ions. {ECO:0000269|PubMed:9237998};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.80 uM for acetone (in the presence of CO(2))
CC {ECO:0000269|PubMed:9237998};
CC KM=7.68 uM for acetone (in the absence of CO(2))
CC {ECO:0000269|PubMed:9237998};
CC KM=0.122 mM for ATP {ECO:0000269|PubMed:9237998};
CC KM=4.17 mM for CO(2) {ECO:0000269|PubMed:9237998};
CC Vmax=0.485 umol/min/mg enzyme toward acetone (in the presence of
CC CO(2)) {ECO:0000269|PubMed:9237998};
CC Vmax=0.616 umol/min/mg enzyme toward acetone (in the absence of
CC CO(2)) {ECO:0000269|PubMed:9237998};
CC Vmax=0.463 umol/min/mg enzyme toward ATP
CC {ECO:0000269|PubMed:9237998};
CC Vmax=0.225 umol/min/mg enzyme toward CO(2)
CC {ECO:0000269|PubMed:9237998};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:9237998};
CC -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC {ECO:0000269|PubMed:9237998}.
CC -!- MASS SPECTROMETRY: Mass=19600; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9237998};
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DR EMBL; AY055852; AAL17712.1; -; Genomic_DNA.
DR EMBL; CP000781; ABS68740.1; -; Genomic_DNA.
DR RefSeq; WP_012115486.1; NC_009720.1.
DR PDB; 5M45; X-ray; 1.87 A; C/F/I/L=1-168.
DR PDB; 5SVB; X-ray; 2.65 A; C/F=1-168.
DR PDB; 5SVC; X-ray; 2.70 A; C/F=1-168.
DR PDBsum; 5M45; -.
DR PDBsum; 5SVB; -.
DR PDBsum; 5SVC; -.
DR AlphaFoldDB; Q8RM02; -.
DR SMR; Q8RM02; -.
DR STRING; 78245.Xaut_3511; -.
DR EnsemblBacteria; ABS68740; ABS68740; Xaut_3511.
DR KEGG; xau:Xaut_3511; -.
DR eggNOG; COG4647; Bacteria.
DR HOGENOM; CLU_1641736_0_0_5; -.
DR OMA; VIKCSCG; -.
DR OrthoDB; 1584977at2; -.
DR PhylomeDB; Q8RM02; -.
DR BioCyc; MetaCyc:MON-13283; -.
DR Proteomes; UP000002417; Chromosome.
DR GO; GO:0018710; F:acetone carboxylase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043443; P:acetone metabolic process; IDA:UniProtKB.
DR InterPro; IPR016750; Aceto_COase_bsu/gsu.
DR Pfam; PF08882; Acetone_carb_G; 1.
DR PIRSF; PIRSF019217; Acetone_carboxlyase_gsu; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12003937"
FT CHAIN 2..168
FT /note="Acetone carboxylase gamma subunit"
FT /evidence="ECO:0000269|PubMed:12003937"
FT /id="PRO_0000403053"
FT CONFLICT 6
FT /note="S -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5SVB"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:5M45"
SQ SEQUENCE 168 AA; 19774 MW; 60B4487B6CE0B62F CRC64;
MAYTRSKIVD LVDGKIDPDT LHQMLSTPKD PERFVTYVEI LQERMPWDDK IILPLGPKLF
IVQQKVSKKW TVRCECGHDF CDWKDNWKLS ARVHVRDTPQ KMEEIYPRLM APTPSWQVIR
EYFCPECGTL HDVEAPTPWY PVIHDFSPDI EGFYQEWLGL PVPERADA
