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Database: UniProt
Entry: W3RL34_9BRAD
LinkDB: W3RL34_9BRAD
Original site: W3RL34_9BRAD 
ID   W3RL34_9BRAD            Unreviewed;       298 AA.
AC   W3RL34;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Citrate lyase {ECO:0000313|EMBL:ETR76923.1};
GN   ORFNames=X566_04215 {ECO:0000313|EMBL:ETR76923.1};
OS   Afipia sp. P52-10.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR76923.1, ECO:0000313|Proteomes:UP000018975};
RN   [1] {ECO:0000313|Proteomes:UP000018975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX   PubMed=25874801;
RA   Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA   Weingartl H.;
RT   "Identification of a novel afipia species isolated from an Indian flying
RT   fox.";
RL   PLoS ONE 10:E0121274-E0121274(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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:ETR76923.1}.
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DR   EMBL; AZSJ01000003; ETR76923.1; -; Genomic_DNA.
DR   RefSeq; WP_034463692.1; NZ_AZSJ01000003.1.
DR   AlphaFoldDB; W3RL34; -.
DR   STRING; 1429916.X566_04215; -.
DR   PATRIC; fig|1429916.3.peg.852; -.
DR   eggNOG; COG2301; Bacteria.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000018975; 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   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ETR76923.1};
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:UP000018975}.
FT   DOMAIN          4..232
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         67
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         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   298 AA;  32191 MW;  F29A851584BD513D CRC64;
     MNLRSWLFIP GDSDKKLGKA DAAGADALIL DIEDSVAASN KEIARAKVRA FLDQRPPGKR
     NSELWVRINP LDDPSSLKDL AAVVGGAPDG IMLPKIDGPA DVLRLSHHLE ALEIRDGVAP
     GHVRIMPVAT ETPVAPLRLN DFVSAKLPRL LGLTWGAEDL SAAIGAATNT DESGEWALTY
     RWARSTMLLA AKAVGIQAVE TLYVNFKDSE GLRKSCRAAA REGFTGRIAI HPDQVAIINE
     AFAPSAEDVD LARRVIAAFE AQSATGTVGL DGKMLDIPHL KQARKVLEMH EQYQRRGQ
//
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