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Database: UniProt
Entry: A0A0J1BJX5_9SPHI
LinkDB: A0A0J1BJX5_9SPHI
Original site: A0A0J1BJX5_9SPHI 
ID   A0A0J1BJX5_9SPHI        Unreviewed;       286 AA.
AC   A0A0J1BJX5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:KLT65588.1};
GN   ORFNames=AB669_10985 {ECO:0000313|EMBL:KLT65588.1};
OS   Pedobacter sp. BMA.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT65588.1, ECO:0000313|Proteomes:UP000036014};
RN   [1] {ECO:0000313|EMBL:KLT65588.1, ECO:0000313|Proteomes:UP000036014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BMA {ECO:0000313|EMBL:KLT65588.1,
RC   ECO:0000313|Proteomes:UP000036014};
RA   Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT   "Pedobacter sp. BMA.";
RL   Submitted (JUN-2015) 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:KLT65588.1}.
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DR   EMBL; LECU01000005; KLT65588.1; -; Genomic_DNA.
DR   RefSeq; WP_047799350.1; NZ_LECU01000005.1.
DR   AlphaFoldDB; A0A0J1BJX5; -.
DR   STRING; 1663685.AB669_10985; -.
DR   PATRIC; fig|1663685.3.peg.2303; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000036014; 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:KLT65588.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036014}.
FT   DOMAIN          5..275
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   286 AA;  31184 MW;  5CB5B86EC3395424 CRC64;
     MSENKFKLVE CPRDAMQGLH DFVPTALKAQ YINLLLQVGF DTLDFGSFVS PKAIPQMADT
     AALLAKLDLS NTATQLLAIV ANIRGAETAA DYEQIDFLGF PFSVSETFQQ RNTNSSIPAS
     LATVEQMLSL CQKKNKTAVV YLSMGFGNPY GDVWNYEIVE KWTEILVSKG VKILSIADTV
     GVSTPEKIRE ILPTLISGYP DTEIGIHLHS TPADRLKKIE AAYQSGVKRI DAALKGFGGC
     PMAADDLTGN IATEDVISFL TAKGENLNLN MEKWHEAMIL SAQIFG
//
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