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Database: UniProt
Entry: H6RV46_BLASD
LinkDB: H6RV46_BLASD
Original site: H6RV46_BLASD 
ID   H6RV46_BLASD            Unreviewed;       311 AA.
AC   H6RV46;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:CCG05765.1};
DE            EC=4.1.3.4 {ECO:0000313|EMBL:CCG05765.1};
GN   OrderedLocusNames=BLASA_4991 {ECO:0000313|EMBL:CCG05765.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG05765.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG05765.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG05765.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) 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; FO117623; CCG05765.1; -; Genomic_DNA.
DR   RefSeq; WP_014378626.1; NC_016943.1.
DR   AlphaFoldDB; H6RV46; -.
DR   STRING; 1146883.BLASA_4991; -.
DR   KEGG; bsd:BLASA_4991; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022138_3_2_11; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000007517; Chromosome.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; 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   Lyase {ECO:0000313|EMBL:CCG05765.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT   DOMAIN          12..278
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   311 AA;  31649 MW;  46ED71B7A1C648F9 CRC64;
     MFEFDLVLPT SVDVREVGMR DGLQLEAPVP LEAKLAMLEA LVATGVRRIE ATSFVSPKAV
     PALADADQVA AELTRWPEVH WSALVANPRG AVRAVDAGVA HLEYVVSASD GHSRANAGRS
     TAEAVAAVSE IAGLAHGAGG SLEVIIATAW DCPFDGRTPV ARTVDVARAA VTAGADQLCL
     GDTIGTTTPL RVVTLVGAVR RACPGIAVGV HFHDTRGTGQ ANALAAVQAG VTQLDASVGG
     LGGCPFAPGA SGNIATEELV YMLEESGVRT GLDLDALLAA ARVTEDAVGH ELPSSLYRAG
     GRSVPRPAGA S
//
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