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Database: UniProt
Entry: A8L1P4_FRASN
LinkDB: A8L1P4_FRASN
Original site: A8L1P4_FRASN 
ID   A8L1P4_FRASN            Unreviewed;       296 AA.
AC   A8L1P4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:ABW13116.1};
GN   ORFNames=Franean1_3719 {ECO:0000313|EMBL:ABW13116.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW13116.1};
RN   [1] {ECO:0000313|EMBL:ABW13116.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW13116.1};
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., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA   Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT   "Complete sequence of Frankia sp. EAN1pec.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; CP000820; ABW13116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8L1P4; -.
DR   STRING; 298653.Franean1_3719; -.
DR   KEGG; fre:Franean1_3719; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022138_3_2_11; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
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:ABW13116.1}.
FT   DOMAIN          3..270
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   296 AA;  30920 MW;  809EDD106C17483C CRC64;
     MAITICEVGP RDGLQNEKTP LSTETKVTLI QRAVAGGVRR VEVTAFVHPK RVPQMADAEE
     VMAQVPRDSG VSYIGLVLNR RGFERAARAG VDEVNMVVLA TETFSERNQG MTVEASLRAW
     AEIAGLAHEA GIRPSVTLSA AFGCPFEGEV SPDRVRDLAR RVVESGPAEI ALADTIGVGV
     PTQVTELVAA VRDVAPGVAL RCHFHNTRNT GYANAVAAVS AGVETLDASA GGIGGCPFAP
     AATGNIATED LVYLLDRMGV ATGVDLRQLA ATGRWIGEQL GIDVPALLGR AGTFPG
//
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