ID   A0A1D7NLA2_9SPHN        Unreviewed;       300 AA.
AC   A0A1D7NLA2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:AOL94466.1};
GN   ORFNames=BG023_111535 {ECO:0000313|EMBL:AOL94466.1};
OS   Porphyrobacter sp. LM 6.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX   NCBI_TaxID=1896196 {ECO:0000313|EMBL:AOL94466.1, ECO:0000313|Proteomes:UP000094080};
RN   [1] {ECO:0000313|EMBL:AOL94466.1, ECO:0000313|Proteomes:UP000094080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM 6 {ECO:0000313|EMBL:AOL94466.1,
RC   ECO:0000313|Proteomes:UP000094080};
RA   Hentchel K., Vargas G., Fiebig A., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of southern
RT   Lake Michigan.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP017113; AOL94466.1; -; Genomic_DNA.
DR   RefSeq; WP_069309920.1; NZ_CP017113.1.
DR   AlphaFoldDB; A0A1D7NLA2; -.
DR   STRING; 1896196.BG023_111535; -.
DR   KEGG; porl:BG023_111535; -.
DR   PATRIC; fig|1896196.3.peg.1528; -.
DR   Proteomes; UP000094080; Chromosome.
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:AOL94466.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          12..239
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         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   300 AA;  31628 MW;  F970C2DED915980E CRC64;
     MTHIAPTPPR MRSWLFAPGD SEKKMGKAIA GSADIALLDL EDSVSPENKA AARAMVAEVI
     ATADNRARLW VRINPVSSAD CIADLAAILP SRPGGVFLPK AEGAADITRL HHYLTALEAA
     NGIPQGHTLI AALVTETAAA MFKTGDYAGD YPGRERLVAM SWGAEDLSSA LGAREQRGSD
     GEYSHTYEMA RSLCLIGASA AGVAAIETVQ PEFRDLDALA ERARRVRAQG FRGMLAIHPA
     QVDPINAAFT PSAEELAHAR AVVQAFAEHP GAGVVALDGA MLDRPHLALA QRLLAEAGEK
//