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Acetone carboxylase alpha subunit (EC 6.4.1.6)

 ACXB_XANP2              Reviewed;         776 AA.
Q8RM03; Q8L3A6;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
22-NOV-2017, entry version 67.
RecName: Full=Acetone carboxylase alpha subunit {ECO:0000312|EMBL:AAL17711.1};
EC=6.4.1.6;
Name=acxB {ECO:0000312|EMBL:AAL17711.1}; OrderedLocusNames=Xaut_3510;
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Xanthobacteraceae; Xanthobacter.
NCBI_TaxID=78245;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL17711.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND BLOCKAGE OF
N-TERMINUS.
PubMed=12003937; DOI=10.1128/JB.184.11.2969-2977.2002;
Sluis M.K., Larsen R.A., Krum J.G., Anderson R., Metcalf W.W.,
Ensign S.A.;
"Biochemical, molecular, and genetic analyses of the acetone
carboxylases from Xanthobacter autotrophicus strain Py2 and
Rhodobacter capsulatus strain B10.";
J. Bacteriol. 184:2969-2977(2002).
[2] {ECO:0000312|EMBL:ABS68739.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-1158 / Py2;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.,
Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J.,
Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
Ensigns S.A., Richardson P.;
"Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, AND MASS SPECTROMETRY.
PubMed=9237998; DOI=10.1073/pnas.94.16.8456;
Sluis M.K., Ensign S.A.;
"Purification and characterization of acetone carboxylase from
Xanthobacter strain Py2.";
Proc. Natl. Acad. Sci. U.S.A. 94:8456-8461(1997).
-!- FUNCTION: Catalyzes the carboxylation of acetone to form
acetoacetate. Has a reduced activity on butanone, and no activity
on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate,
phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene
oxide. {ECO:0000269|PubMed:9237998}.
-!- CATALYTIC ACTIVITY: Acetone + CO(2) + ATP + 2 H(2)O = acetoacetate
+ AMP + 2 phosphate. {ECO:0000269|PubMed:9237998}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:9237998};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9237998};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:9237998};
Note=Zn(2+). The heterohexamer contains tightly bound iron,
manganese and zinc ions. {ECO:0000269|PubMed:9237998};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.80 uM for acetone (in the presence of CO(2))
{ECO:0000269|PubMed:9237998};
KM=7.68 uM for acetone (in the absence of CO(2))
{ECO:0000269|PubMed:9237998};
KM=0.122 mM for ATP {ECO:0000269|PubMed:9237998};
KM=4.17 mM for CO(2) {ECO:0000269|PubMed:9237998};
Vmax=0.485 umol/min/mg enzyme toward acetone (in the presence of
CO(2)) {ECO:0000269|PubMed:9237998};
Vmax=0.616 umol/min/mg enzyme toward acetone (in the absence of
CO(2)) {ECO:0000269|PubMed:9237998};
Vmax=0.463 umol/min/mg enzyme toward ATP
{ECO:0000269|PubMed:9237998};
Vmax=0.225 umol/min/mg enzyme toward CO(2)
{ECO:0000269|PubMed:9237998};
pH dependence:
Optimum pH is 7.6. {ECO:0000269|PubMed:9237998};
-!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma
subunits. {ECO:0000269|PubMed:9237998}.
-!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12003937}.
-!- MASS SPECTROMETRY: Mass=85300; Method=MALDI; Range=1-776;
Evidence={ECO:0000269|PubMed:9237998};
-!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
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EMBL; AF251789; AAM20737.1; -; Genomic_DNA.
EMBL; AY055852; AAL17711.1; -; Genomic_DNA.
EMBL; CP000781; ABS68739.1; -; Genomic_DNA.
RefSeq; WP_012115485.1; NC_009720.1.
PDB; 5M45; X-ray; 1.87 A; A/D/G/J=1-776.
PDB; 5SVB; X-ray; 2.65 A; A/D=1-776.
PDB; 5SVC; X-ray; 2.70 A; A/D=1-776.
PDBsum; 5M45; -.
PDBsum; 5SVB; -.
PDBsum; 5SVC; -.
SMR; Q8RM03; -.
STRING; 78245.Xaut_3510; -.
EnsemblBacteria; ABS68739; ABS68739; Xaut_3510.
KEGG; xau:Xaut_3510; -.
eggNOG; ENOG4107TYC; Bacteria.
eggNOG; COG0146; LUCA.
HOGENOM; HOG000146365; -.
KO; K10854; -.
OMA; MGAAIKY; -.
OrthoDB; POG091H0N2T; -.
BioCyc; MetaCyc:MONOMER-13282; -.
Proteomes; UP000002417; Chromosome.
GO; GO:0018710; F:acetone carboxylase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043443; P:acetone metabolic process; IDA:UniProtKB.
InterPro; IPR003692; Hydantoinase_B.
Pfam; PF02538; Hydantoinase_B; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Ligase;
Nucleotide-binding; Reference proteome.
CHAIN 1 776 Acetone carboxylase alpha subunit.
/FTId=PRO_0000403052.
CONFLICT 13 14 AT -> QA (in Ref. 1; AAM20737).
{ECO:0000305}.
STRAND 16 18 {ECO:0000244|PDB:5SVB}.
HELIX 24 38 {ECO:0000244|PDB:5M45}.
HELIX 41 43 {ECO:0000244|PDB:5M45}.
HELIX 48 52 {ECO:0000244|PDB:5M45}.
HELIX 54 75 {ECO:0000244|PDB:5M45}.
HELIX 76 78 {ECO:0000244|PDB:5M45}.
HELIX 82 85 {ECO:0000244|PDB:5M45}.
STRAND 90 95 {ECO:0000244|PDB:5M45}.
STRAND 101 104 {ECO:0000244|PDB:5M45}.
STRAND 106 108 {ECO:0000244|PDB:5M45}.
HELIX 111 124 {ECO:0000244|PDB:5M45}.
TURN 125 131 {ECO:0000244|PDB:5M45}.
STRAND 138 141 {ECO:0000244|PDB:5M45}.
HELIX 144 146 {ECO:0000244|PDB:5M45}.
STRAND 153 162 {ECO:0000244|PDB:5M45}.
STRAND 165 175 {ECO:0000244|PDB:5M45}.
STRAND 177 179 {ECO:0000244|PDB:5SVB}.
STRAND 182 187 {ECO:0000244|PDB:5M45}.
STRAND 203 208 {ECO:0000244|PDB:5M45}.
HELIX 214 222 {ECO:0000244|PDB:5M45}.
STRAND 223 225 {ECO:0000244|PDB:5M45}.
HELIX 227 255 {ECO:0000244|PDB:5M45}.
HELIX 257 282 {ECO:0000244|PDB:5M45}.
STRAND 286 297 {ECO:0000244|PDB:5M45}.
HELIX 308 310 {ECO:0000244|PDB:5M45}.
STRAND 312 324 {ECO:0000244|PDB:5M45}.
STRAND 330 333 {ECO:0000244|PDB:5M45}.
STRAND 342 344 {ECO:0000244|PDB:5M45}.
HELIX 349 361 {ECO:0000244|PDB:5M45}.
TURN 362 364 {ECO:0000244|PDB:5M45}.
HELIX 373 376 {ECO:0000244|PDB:5M45}.
STRAND 378 381 {ECO:0000244|PDB:5M45}.
TURN 398 400 {ECO:0000244|PDB:5M45}.
HELIX 401 422 {ECO:0000244|PDB:5M45}.
HELIX 425 427 {ECO:0000244|PDB:5M45}.
STRAND 440 444 {ECO:0000244|PDB:5M45}.
STRAND 448 454 {ECO:0000244|PDB:5M45}.
HELIX 456 459 {ECO:0000244|PDB:5M45}.
STRAND 467 469 {ECO:0000244|PDB:5M45}.
STRAND 480 482 {ECO:0000244|PDB:5M45}.
HELIX 488 494 {ECO:0000244|PDB:5M45}.
STRAND 495 504 {ECO:0000244|PDB:5M45}.
STRAND 512 514 {ECO:0000244|PDB:5M45}.
STRAND 520 526 {ECO:0000244|PDB:5M45}.
STRAND 530 535 {ECO:0000244|PDB:5M45}.
STRAND 548 550 {ECO:0000244|PDB:5SVC}.
STRAND 559 564 {ECO:0000244|PDB:5M45}.
HELIX 567 573 {ECO:0000244|PDB:5M45}.
HELIX 591 593 {ECO:0000244|PDB:5M45}.
STRAND 598 603 {ECO:0000244|PDB:5M45}.
STRAND 610 612 {ECO:0000244|PDB:5M45}.
STRAND 617 621 {ECO:0000244|PDB:5M45}.
HELIX 631 633 {ECO:0000244|PDB:5M45}.
HELIX 636 644 {ECO:0000244|PDB:5M45}.
HELIX 652 657 {ECO:0000244|PDB:5M45}.
STRAND 661 663 {ECO:0000244|PDB:5M45}.
STRAND 669 671 {ECO:0000244|PDB:5M45}.
HELIX 673 690 {ECO:0000244|PDB:5M45}.
HELIX 694 706 {ECO:0000244|PDB:5M45}.
HELIX 712 724 {ECO:0000244|PDB:5M45}.
HELIX 726 735 {ECO:0000244|PDB:5M45}.
HELIX 746 748 {ECO:0000244|PDB:5M45}.
STRAND 749 751 {ECO:0000244|PDB:5M45}.
HELIX 762 764 {ECO:0000244|PDB:5M45}.
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


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