ID   A0A158K4P5_9BURK        Unreviewed;       294 AA.
AC   A0A158K4P5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:SAL76108.1};
GN   ORFNames=AWB66_05334 {ECO:0000313|EMBL:SAL76108.1};
OS   Caballeronia telluris.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326475 {ECO:0000313|EMBL:SAL76108.1, ECO:0000313|Proteomes:UP000054717};
RN   [1] {ECO:0000313|EMBL:SAL76108.1, ECO:0000313|Proteomes:UP000054717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22936 {ECO:0000313|EMBL:SAL76108.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FCNZ02000028; SAL76108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158K4P5; -.
DR   STRING; 326475.AWB66_05334; -.
DR   Proteomes; UP000054717; 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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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:SAL76108.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054717}.
FT   DOMAIN          11..226
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   294 AA;  31835 MW;  729020F8B7557D2C CRC64;
     MNALSTRRIR RSMLLTPAHR RDRVVGAMNL PVDSFAFDLE DGVPPGRRDE AREILSQVLP
     TLETGERERV VRINAPGTDD CLHDLDALPL EHLDAVLVPK VESAEQMRAL DVLLTAREGG
     RGAPIRLIVT LETPRGVLNA LAIGDASPRC CAFFFGSGDY TMETGAAITP TALLWARSTI
     VAAAGALRID AIDAPYLAGL RDPQGTFEDA ARSRELGFSG KVVFHPAQIE PVHRAFTPDA
     GEVARARRII DAFEQVKASG EGTAIVDGEF VAIDLVPRMH RVIEIAGYDA RRSA
//