ID   A0A432DPX6_9BURK        Unreviewed;       272 AA.
AC   A0A432DPX6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RTZ44715.1};
GN   ORFNames=EKL30_09155 {ECO:0000313|EMBL:RTZ44715.1};
OS   Candidimonas sp. SYP-B2681.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Candidimonas.
OX   NCBI_TaxID=2497686 {ECO:0000313|EMBL:RTZ44715.1, ECO:0000313|Proteomes:UP000288599};
RN   [1] {ECO:0000313|EMBL:RTZ44715.1, ECO:0000313|Proteomes:UP000288599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SYP-B2681 {ECO:0000313|EMBL:RTZ44715.1,
RC   ECO:0000313|Proteomes:UP000288599};
RA   Zhang M.-Y., Zhang Y.-X.;
RT   "Candidimonas lamiisoli sp. nov., a novel bacterium can accelerate seed
RT   germination.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:RTZ44715.1}.
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DR   EMBL; RYDV01000003; RTZ44715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432DPX6; -.
DR   OrthoDB; 348111at2; -.
DR   Proteomes; UP000288599; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:RTZ44715.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288599}.
FT   DOMAIN          6..213
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   272 AA;  28883 MW;  E360CBCACB4953B6 CRC64;
     MQQQIRSALF VPATRPERFS KALGAGADAV IIDLEDAVEH GLKDEAREHL RDFASANPQA
     SFWVRINGAT TSWFNADLAI CAAHQNITAV LLPKAESALQ IQQVAQSGKT VLPIVESARG
     VLALEQMAAQ QAVDRLSFGS LDLMLELGTA PDTVGAALLL NHIRCQILLH SSANGLAAPL
     DGVYPNFSDH DGLSQLAAQV RDMGFGGMLC IHPAQVAAIH AAFAPTAADT EWAKRIIEVA
     DATGSSAFQV DGKMVDAPVI ERAHQILRRV AG
//