ACXA_XANP2
ID ACXA_XANP2 Reviewed; 717 AA.
AC Q8RM04; Q8L3A7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Acetone carboxylase beta subunit {ECO:0000312|EMBL:AAL17710.1};
DE EC=6.4.1.6;
GN Name=acxA {ECO:0000312|EMBL:AAL17710.1}; OrderedLocusNames=Xaut_3509;
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:AAL17710.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND BLOCKAGE OF
RP N-TERMINUS.
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:ABS68738.1}
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 -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12003937}.
CC -!- MASS SPECTROMETRY: Mass=78300; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9237998};
CC -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
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DR EMBL; AF251789; AAM20736.1; -; Genomic_DNA.
DR EMBL; AY055852; AAL17710.1; -; Genomic_DNA.
DR EMBL; CP000781; ABS68738.1; -; Genomic_DNA.
DR RefSeq; WP_012115484.1; NC_009720.1.
DR PDB; 5M45; X-ray; 1.87 A; B/E/H/K=1-717.
DR PDB; 5SVB; X-ray; 2.65 A; B/E=2-717.
DR PDB; 5SVC; X-ray; 2.70 A; B/E=1-717.
DR PDBsum; 5M45; -.
DR PDBsum; 5SVB; -.
DR PDBsum; 5SVC; -.
DR AlphaFoldDB; Q8RM04; -.
DR SMR; Q8RM04; -.
DR STRING; 78245.Xaut_3509; -.
DR EnsemblBacteria; ABS68738; ABS68738; Xaut_3509.
DR KEGG; xau:Xaut_3509; -.
DR eggNOG; COG0145; Bacteria.
DR HOGENOM; CLU_002157_1_2_5; -.
DR OMA; HAMTVSV; -.
DR OrthoDB; 327092at2; -.
DR PhylomeDB; Q8RM04; -.
DR BioCyc; MetaCyc:MON-13281; -.
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:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0043443; P:acetone metabolic process; IDA:UniProtKB.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR008040; Hydant_A_N.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365; PTHR11365; 1.
DR Pfam; PF05378; Hydant_A_N; 1.
DR Pfam; PF01968; Hydantoinase_A; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..717
FT /note="Acetone carboxylase beta subunit"
FT /id="PRO_0000403051"
FT CONFLICT 352
FT /note="A -> R (in Ref. 1; AAM20736)"
FT /evidence="ECO:0000305"
FT STRAND 11..29
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5SVB"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 183..187
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:5SVC"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 433..458
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 467..474
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 475..482
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 500..507
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 510..522
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 528..555
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 564..573
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 580..583
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:5SVB"
FT HELIX 592..609
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 621..632
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 654..662
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 665..673
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 682..690
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 702..706
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:5M45"
SQ SEQUENCE 717 AA; 78509 MW; AF30CD9B7078A283 CRC64;
MNVPVGHLRN VQVLGIDAGG TMTDTFFVDQ DGDFVVGKAQ STPQNEALGL IASSEDGLAN
WGMSLHEALA QLQTGVYSGT AMLNRVVQRK GLKCGLIVNR GMEDFHRMGR AVQSHLGYAY
EDRIHLNTHR YDPPLVPRHL TRGVVERTDM IGTQVIPLRE DTARDAARDL IAADAEGIVI
SLLHSYKNPE NERRVRDIVL EEVEKSGKKI PVFASADYYP VRKETHRTNT TILEGYAAEP
SRQTLSKISN AFKERGTKFD FRVMATHGGT ISWKAKELAR TIVSGPIGGV IGAKYLGEVL
GYKNIACSDI GGTSFDVALI TQGEMTIKND PDMARLVLSL PLVAMDSVGA GAGSFIRLDP
YTRAIKLGPD SAGYRVGVCW KESGIETVTI SDCHMVLGYL NPDNFLGGAV KLDRQRSVDA
IKAQIADPLG LSVEDAAAGV IELLDSDLRD YLRSMISGKG YSPASFVCFS YGGAGPVHTY
GYTEGLGFED VIVPAWAAGF SAFGCAAADF EYRYDKSLDI NMPTETPDTD KEKAAATLQA
AWEELTKNVL EEFKLNGYSA DQVTLQPGYR MQYRGQLNDL EIESPLAQAH TAADWDQLTD
AFNATYGRVY AASARSPELG YSVTGAIMRG MVPIPKPKIP KEPEEGETPP ESAKIGTRKF
YRKKRWVDAQ LYHMESLRPG NRVMGPAVIE SDATTFVVPD GFETWLDGHR LFHLREV
