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Database: UniProt
Entry: H0C3Q0_9BURK
LinkDB: H0C3Q0_9BURK
Original site: H0C3Q0_9BURK 
ID   H0C3Q0_9BURK            Unreviewed;       302 AA.
AC   H0C3Q0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:EHL20737.1};
GN   ORFNames=KYG_21204 {ECO:0000313|EMBL:EHL20737.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL20737.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL20737.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL20737.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; AGTS01000145; EHL20737.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0C3Q0; -.
DR   STRING; 512030.KYG_21204; -.
DR   PATRIC; fig|512030.4.peg.4172; -.
DR   Proteomes; UP000003485; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR043594; HMGL.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:EHL20737.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003485};
KW   Transferase {ECO:0000313|EMBL:EHL20737.1}.
FT   DOMAIN          1..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   302 AA;  32279 MW;  428FDE3B168BA4BF CRC64;
     MKIVEVGPRD GLQNEGKIVP TAMKLDLIER LVKAGLKNIE ATSFVSPKWV PQMGDHLQIM
     SGLPQYPGVF YSVLTPNLKG FEAAAQSGAT EVAVFAAASE AFSARNINCS IAESLERFEP
     VMQSAQSLGI KVRGYVSCVV GCPYEGKVDP ERVADVAERL FNMGCYEVSL GDTIGIGTPV
     DVQKVLESVA RRVPVHALAG HFHDTYGRAL MNIYASYQFG VRVFDSSVSG LGGCPYAKGA
     SGNVATEDVV FLMNSLGAHT GVDLEKLVDV SAWISTLLHR TPNSKVIGPV LAKRASEVLC
     IS
//
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