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Database: UniProt
Entry: A8U293_9PROT
LinkDB: A8U293_9PROT
Original site: A8U293_9PROT 
ID   A8U293_9PROT            Unreviewed;       318 AA.
AC   A8U293;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:EDP61665.1};
GN   ORFNames=BAL199_18516 {ECO:0000313|EMBL:EDP61665.1};
OS   alpha proteobacterium BAL199.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP61665.1, ECO:0000313|Proteomes:UP000003417};
RN   [1] {ECO:0000313|EMBL:EDP61665.1, ECO:0000313|Proteomes:UP000003417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL199 {ECO:0000313|EMBL:EDP61665.1,
RC   ECO:0000313|Proteomes:UP000003417};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP61665.1}.
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DR   EMBL; ABHC01000029; EDP61665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8U293; -.
DR   STRING; 331869.BAL199_18516; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000003417; 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:EDP61665.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW   Transferase {ECO:0000313|EMBL:EDP61665.1}.
FT   DOMAIN          13..280
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   318 AA;  33487 MW;  C25F325EA7B63095 CRC64;
     MAEVSPITAG HRVEVTEVGP RDGIQADATF VPTEHKIALI NRLTEAGVPR IEATSFVSPR
     AVPQLADAAE VMKGVKRSKS TVLAALVPNA RGAIRAAEAG VDQIVVFMSA SESHNLKNVN
     CTVAESLKAF EDVAKIAHDS GIPVHGAIAT SFGCPFEGDV PVAQVARIAR AYQDMGFVGM
     SFGDTTGMAT PPLVKERVLA VRDAAPRLSQ VLHFHNTRGI GLANVMAGLA VGVDRYESSI
     GGTGGCPFVP KATGNICTED LLYLLHEMGI ETGIDLRKLM GMASDMQSVL GRELPGQIMK
     AGLRLDLHPM ESVRTAVG
//
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