ID A0A0A8JJG7_BACSX Unreviewed; 300 AA.
AC A0A0A8JJG7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Hydroxymethylglutaryl-coa lyase {ECO:0000313|EMBL:BAQ10616.1};
GN ORFNames=OXB_2145 {ECO:0000313|EMBL:BAQ10616.1};
OS Bacillus sp. (strain OxB-1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ10616.1, ECO:0000313|Proteomes:UP000031651};
RN [1] {ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAQ10616.1, ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ10616.1,
RC ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL Genome Announc. 3:e00025-15(2015).
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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DR EMBL; AP013294; BAQ10616.1; -; Genomic_DNA.
DR RefSeq; WP_041074235.1; NZ_AP013294.1.
DR AlphaFoldDB; A0A0A8JJG7; -.
DR STRING; 98228.OXB_2145; -.
DR KEGG; baco:OXB_2145; -.
DR HOGENOM; CLU_022138_3_2_9; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000031651; Chromosome.
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:BAQ10616.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031651}.
FT DOMAIN 8..273
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 300 AA; 32617 MW; D1D11BDEAE18456C CRC64;
MFILPNNVTI IEVGPRDGLQ NEKKFVETQE KLGFIKALQQ AGIQEMELTS FVSPKWVPQM
ADAKEIVAET PRVGRQFVLA PNAKGAELAL EADAQSVAVF VGVSNSFNKK NINRSTEEAL
DALEPVIAKL KQDNIFVRAC ISTAFYCPYE GKMDIEDVVS LCKRFVSMGA DELSVADTIG
KANPRESFAL FSRLKEELPN VLITAHFHDT RKMAIANIYA ALQAGVDRFD MSAGGLGGCP
FAPGATGNVA TEDVVHLLDT LGIETGVDVK QVCEAVALIA PHVSRPIETG MYRLFVNDQL
//
