ID   A0A2S4M254_9BURK        Unreviewed;       287 AA.
AC   A0A2S4M254;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Citrate lyase subunit beta/citryl-CoA lyase {ECO:0000313|EMBL:POR48717.1};
GN   ORFNames=B0G62_1132 {ECO:0000313|EMBL:POR48717.1};
OS   Paraburkholderia eburnea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR48717.1, ECO:0000313|Proteomes:UP000237381};
RN   [1] {ECO:0000313|EMBL:POR48717.1, ECO:0000313|Proteomes:UP000237381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18070 {ECO:0000313|EMBL:POR48717.1,
RC   ECO:0000313|Proteomes:UP000237381};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JAN-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:POR48717.1}.
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DR   EMBL; PQGA01000013; POR48717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4M254; -.
DR   Proteomes; UP000237381; 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:POR48717.1};
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:UP000237381}.
FT   DOMAIN          21..224
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   287 AA;  30978 MW;  46577F85D1CB3C99 CRC64;
     MPSEHHGMHG DDSARHAFSA QSYLFVPGSR PERFGRALES GADAVIIDLE DAVEPAAKEA
     ARENIANWVS RKHPVLVRIN GRATPWFEQD AKLGALDGVA GIVLPKAESA GDVAATIAIA
     RRRVSVYPLI ESALGMWHAM AIAKAPFVRR LMFGTLDFVA EMGMPDDGEP LNHYRSQLAL
     ISRVAGIETP VDGVTPDIHD IARIGRDALN GKRLGFGGKL CIHPQQIEAV HNVFRPGEQE
     LAWAARVAEA ASHADAGAIT VDGKMVDRPV LLRAQQILAL AEVLKKH
//