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Database: UniProt
Entry: D7CBL5_STRBB
LinkDB: D7CBL5_STRBB
Original site: D7CBL5_STRBB 
ID   D7CBL5_STRBB            Unreviewed;       192 AA.
AC   D7CBL5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:ADI12892.1};
GN   OrderedLocusNames=SBI_09774 {ECO:0000313|EMBL:ADI12892.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI12892.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI12892.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI12892.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; CP002047; ADI12892.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7CBL5; -.
DR   STRING; 749414.SBI_09774; -.
DR   KEGG; sbh:SBI_09774; -.
DR   PATRIC; fig|749414.3.peg.10058; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_1414429_0_0_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
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:ADI12892.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT   DOMAIN          1..156
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          49..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   192 AA;  19954 MW;  5D24C2A6BFE753B3 CRC64;
     MPSGATNLVP PLAEERPVLL FGLRHTQQRQ HRPGHEGFPG CHAGGRVDRA RGGRPDSALP
     RDRVHLPVRG AGGSGPRVAA VTDRRVALHG HDTWGQGVAN ALAAAENGAT LLDGALGGLG
     GCPFAPGASG NTASEDLLFA LRPDWLTPQV LADLVAEGED LLMELGEPNR SKAAQGIRSK
     SSAFPWAVGP RI
//
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