ID A0A0D6TFN0_9RHOB Unreviewed; 287 AA.
AC A0A0D6TFN0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:KIX19044.1};
GN ORFNames=SY26_02680 {ECO:0000313|EMBL:KIX19044.1};
OS Paracoccus sp. 228.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX19044.1, ECO:0000313|Proteomes:UP000032743};
RN [1] {ECO:0000313|EMBL:KIX19044.1, ECO:0000313|Proteomes:UP000032743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=361 {ECO:0000313|EMBL:KIX19044.1,
RC ECO:0000313|Proteomes:UP000032743};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-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:KIX19044.1}.
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DR EMBL; JYGY01000001; KIX19044.1; -; Genomic_DNA.
DR RefSeq; WP_045999152.1; NZ_JYGY01000001.1.
DR AlphaFoldDB; A0A0D6TFN0; -.
DR STRING; 1192054.SY26_02680; -.
DR PATRIC; fig|1603292.4.peg.546; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000032743; 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:KIX19044.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032743}.
FT DOMAIN 5..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 287 AA; 29899 MW; CEAA0E92B0D97129 CRC64;
MAEHVRIFEM GPRDGLQNEK RLIPTADKIA LVDLLSQAGF ADIEVTSFVP AAWVPQMADG
AEVMAGITRR PGTRYAVLTP NLRGYQAARA AQADTVAVFA SASEGFSRAN LNASIADSLA
RMAPVAAQAQ ADGVTLRGYV SVVTDCPFDG PVAPAAVARV AAALRDMGCQ QISLGDTIGQ
GRPETIDAML AAVLEELPAG RLAGHYHDTA GRALQNVDVS LERGLRVFDA AVGGLGGCPY
APGAAGNVAT EALARHLDRR GFAHGLDMDI ITRAAAMARA LRETPDA
//
