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Database: UniProt
Entry: C6XJA3_HIRBI
LinkDB: C6XJA3_HIRBI
Original site: C6XJA3_HIRBI 
ID   C6XJA3_HIRBI            Unreviewed;       320 AA.
AC   C6XJA3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:ACT59198.1};
GN   OrderedLocusNames=Hbal_1509 {ECO:0000313|EMBL:ACT59198.1};
OS   Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hirschia.
OX   NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT59198.1, ECO:0000313|Proteomes:UP000002745};
RN   [1] {ECO:0000313|Proteomes:UP000002745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC   {ECO:0000313|Proteomes:UP000002745};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; CP001678; ACT59198.1; -; Genomic_DNA.
DR   RefSeq; WP_015827348.1; NC_012982.1.
DR   AlphaFoldDB; C6XJA3; -.
DR   STRING; 582402.Hbal_1509; -.
DR   KEGG; hba:Hbal_1509; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022138_3_2_5; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000002745; Chromosome.
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:ACT59198.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002745};
KW   Transferase {ECO:0000313|EMBL:ACT59198.1}.
FT   DOMAIN          3..275
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   320 AA;  33613 MW;  0FB8E74DEE788819 CRC64;
     MNILISEVGP RDGLQNVSSI MPTTAKKAWI DAAFAAGIRE IEVGSFVPAK LLPQLADTNE
     IVSYARQIEG LTVAALVPNS HGARNAINAG THKITLPLSC SESHSIANLR RTHEQVLAEA
     RSIANMIAEL PAKSRPHFEG SLSTAFGCTI EGNVPEDKVI ELAEALMEAG CDEVGLADTT
     GYANPTSVKE LIKKIWGAVG QEALTGIHLH NTRGLGLANA YAALEVGLTT FDSSLGGLGG
     CPFAPGASGN LVTEDLVYMF EAMGISTGID LESLFSVRRL VQESLPSEEF YGFAPEAGLP
     LGFSPTTPSL PNNQLAGSRS
//
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