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Database: UniProt
Entry: A0A073JVH3_9BACI
LinkDB: A0A073JVH3_9BACI
Original site: A0A073JVH3_9BACI 
ID   A0A073JVH3_9BACI        Unreviewed;       303 AA.
AC   A0A073JVH3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:KEK18211.1};
GN   ORFNames=BAMA_06510 {ECO:0000313|EMBL:KEK18211.1};
OS   Bacillus manliponensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK18211.1, ECO:0000313|Proteomes:UP000027822};
RN   [1] {ECO:0000313|EMBL:KEK18211.1, ECO:0000313|Proteomes:UP000027822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK18211.1,
RC   ECO:0000313|Proteomes:UP000027822};
RA   Lai Q., Liu Y., Shao Z.;
RT   "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT   1A00708).";
RL   Submitted (JUN-2014) 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:KEK18211.1}.
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DR   EMBL; JOTN01000016; KEK18211.1; -; Genomic_DNA.
DR   RefSeq; WP_034641483.1; NZ_JOTN01000016.1.
DR   AlphaFoldDB; A0A073JVH3; -.
DR   STRING; 574376.BAMA_06510; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000027822; 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   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   Lyase {ECO:0000313|EMBL:KEK18211.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027822}.
FT   DOMAIN          7..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   303 AA;  33412 MW;  A3209F5B74B61BA2 CRC64;
     MKLPSFAFIK EVGPRDGLQN EKKIVGTKDK VKWIELLTEA GLSYIEVSSF VHPKWVPALA
     DAKDVFTMLE RNPHITYAAL VPNQQGLERA LLHNVDEVNV FLSASETHNK KNINKSMQEA
     LAVIEDVAKQ AQFAGKKVRG YVSTVFGCPY EGEVDIDVID ELCNQLFSYG IYEVSLGDTI
     GVGNPAQVER VLEHLLAKYD STKFAMHFHN TYGMALANVV KSLECGITVF DSSCGGLGGC
     PYAPGASGNI ATNDLVHMLH KMGVQTNVNE EKLLQASKFI QNKLDMPLPS NVYRALEHKL
     VSR
//
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