ACXB_XANP2
ID ACXB_XANP2 Reviewed; 776 AA.
AC Q8RM03; Q8L3A6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Acetone carboxylase alpha subunit {ECO:0000312|EMBL:AAL17711.1};
DE EC=6.4.1.6;
GN Name=acxB {ECO:0000312|EMBL:AAL17711.1}; OrderedLocusNames=Xaut_3510;
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:AAL17711.1}
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:ABS68739.1}
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=85300; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9237998};
CC -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF251789; AAM20737.1; -; Genomic_DNA.
DR EMBL; AY055852; AAL17711.1; -; Genomic_DNA.
DR EMBL; CP000781; ABS68739.1; -; Genomic_DNA.
DR RefSeq; WP_012115485.1; NC_009720.1.
DR PDB; 5M45; X-ray; 1.87 A; A/D/G/J=1-776.
DR PDB; 5SVB; X-ray; 2.65 A; A/D=1-776.
DR PDB; 5SVC; X-ray; 2.70 A; A/D=1-776.
DR PDBsum; 5M45; -.
DR PDBsum; 5SVB; -.
DR PDBsum; 5SVC; -.
DR AlphaFoldDB; Q8RM03; -.
DR SMR; Q8RM03; -.
DR STRING; 78245.Xaut_3510; -.
DR EnsemblBacteria; ABS68739; ABS68739; Xaut_3510.
DR KEGG; xau:Xaut_3510; -.
DR eggNOG; COG0146; Bacteria.
DR HOGENOM; CLU_020413_2_0_5; -.
DR OMA; KYRGGCG; -.
DR OrthoDB; 1018930at2; -.
DR PhylomeDB; Q8RM03; -.
DR BioCyc; MetaCyc:MON-13282; -.
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; IPR003692; Hydantoinase_B.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365; PTHR11365; 2.
DR Pfam; PF02538; Hydantoinase_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..776
FT /note="Acetone carboxylase alpha subunit"
FT /id="PRO_0000403052"
FT CONFLICT 13..14
FT /note="AT -> QA (in Ref. 1; AAM20737)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5SVB"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 54..75
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 125..131
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5SVB"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 227..255
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 257..282
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 312..324
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 349..361
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:5M45"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 401..422
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 488..494
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 495..504
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:5SVC"
FT STRAND 559..564
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 567..573
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 636..644
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 652..657
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 673..690
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 694..706
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 712..724
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 726..735
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 746..748
FT /evidence="ECO:0007829|PDB:5M45"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:5M45"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:5M45"
SQ SEQUENCE 776 AA; 86342 MW; E3F999C5885094E0 CRC64;
MNVTVDQSTL AGATRGIVRG GETLKEHRDR LMAATKATGR YAGLKTLELR EREPILYNKL
FSRLRAGVVD ARETAKKIAA SPIVEQEGEL CFTLYNAAGD SLLTSTGIII HVGTMGAAIK
YMIENNWEAN PGVHDKDIFC NNDSLIGNVH PCDIHTIVPI FWEGELIGWV GGVTHVIDTG
AVGPGSMATG QVQRFGDGYS ITCRKVGAND TLFRDWLHES QRMVRTTRYW MLDERTRIAG
CHMIRKLVEE VVAEEGIEAY WKFAYEAVEH GRLGLQARIK AMTIPGTYRQ VGFVDVPYAH
EDVRVPSDFA KLDTIMHAPC EMTIRRDGTW RLDFEGSSRW GWHTYNAHQV SFTSGIWVMM
TQTLIPSEMI NDGAAYGTEF RLPKGTWMNP DDRRVAFSYS WHFLVSAWTA LWRGLSRSYF
GRGYLEEVNA GNANTSNWLQ GGGFNQYDEI HAVNSFECAA NGTGATAVQD GLSHAAAIWN
PEGDMGDMEI WELAEPLVYL GRQIKASSGG SGKYRGGCGF ESLRMVWNAK DWTMFFMGNG
HISSDWGLMG GYPAASGYRF AAHKTNLKEL IASGAEIPLG GDTDPENPTW DAMLPDAQIK
RDKQAITTEE MFSDYDLYLN YMRGGPGFGD PLDREPQAVA DDINGGYVLE RFAGEVYGVV
VRKGADGQYG VDEAGTAAAR AQIRKDRLAK SVPVSEWMKG EREKILAKDA GTQVRQMFAA
SFKLGPRFEK DFRTFWSLPD SWTLPEEEIG VPTYGSRYSM DISELPDVHT VQFVEE
