ID   G2ZYM0_9RALS            Unreviewed;       326 AA.
AC   G2ZYM0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Putative citrate lyase {ECO:0000313|EMBL:CCA84375.1};
DE            EC=4.1.3.- {ECO:0000313|EMBL:CCA84375.1};
GN   ORFNames=RALSY_10344 {ECO:0000313|EMBL:CCA84375.1};
OS   Ralstonia syzygii R24.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA84375.1};
RN   [1] {ECO:0000313|EMBL:CCA84375.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA84375.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA84375.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA84375.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) 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; FR854086; CCA84375.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2ZYM0; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.960; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR040186; Citramalyl-CoA_lyase.
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; PTHR11105:SF0; CITRAMALYL-COA LYASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11105; CITRATE LYASE SUBUNIT BETA-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:CCA84375.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          46..239
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   326 AA;  35493 MW;  18F643CF18E855FB CRC64;
     MHPTEVLFQD DAAPAQLPVC DHYAGAEKLM RKSLALQQAL GPVFDITLDC EDGAAVGQER
     AHAELAAQLI NSDYNRFNRV GVRIHDPNHD AWAQDVDILV GQAGRRLAYV TVPKVRDVVE
     VARVTDRVNQ AAKAAGIARH LPIHVLIETH GALAQVFDIA SLVQVECLSF GLMDFVSAHN
     GAIPGTAMGS PAQFEHPLVR RALTDISAAC HAHGKVPSHN VSTDIKRPDR AGTDAARARN
     EFGYLRKWSI HPDQIGPIVA AFRPSHDEVA QAATILTAAQ DASWGPIQHE GRLHDRASYR
     YWWAVLQRAH TTGVTVPPEA AARFFG
//