ID   A0A142LLB5_9PROT        Unreviewed;       281 AA.
AC   A0A142LLB5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:AMS33011.1};
GN   ORFNames=AEM42_12670 {ECO:0000313|EMBL:AMS33011.1};
OS   Betaproteobacteria bacterium UKL13-2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS33011.1, ECO:0000313|Proteomes:UP000075227};
RN   [1] {ECO:0000313|Proteomes:UP000075227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Driscoll C.B.;
RL   Submitted (JUL-2015) 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; CP012157; AMS33011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142LLB5; -.
DR   STRING; 1690485.AEM42_12670; -.
DR   KEGG; beb:AEM42_12670; -.
DR   Proteomes; UP000075227; 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: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:AMS33011.1};
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:UP000075227}.
FT   DOMAIN          1..212
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   281 AA;  30642 MW;  50AD4A499A7F73A1 CRC64;
     MLYVPGCFTR FLNKARGLKV DSVIFDLGDS VLVENKALSR TQVVEAILSG GYGRRELVVR
     VNDLDSPWGQ DDVNAITKIG VDAVLFPNIE SRQDVLDALA ALDAAGGSHL PIMVMIESPL
     AVLRAEDIAS ASDRIACLIL ATSDLITQLH GRKTPDRIPL QYSLAHVLLV GRAYKRAVVD
     GISIDIKDMH SFEMACRLTR DLGFDGKSLV HPNQLAYCND AFTPKATEIT FAYEVIQALE
     TAHQAGRGTI MLNGRLVEQH HVAASKRIIA LAQMIKELEA A
//