ID   A0A2M9D326_9MICO        Unreviewed;       284 AA.
AC   A0A2M9D326;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Citrate lyase subunit beta/citryl-CoA lyase {ECO:0000313|EMBL:PJJ78571.1};
GN   ORFNames=CLV85_2146 {ECO:0000313|EMBL:PJJ78571.1};
OS   Salinibacterium amurskyense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Salinibacterium.
OX   NCBI_TaxID=205941 {ECO:0000313|EMBL:PJJ78571.1, ECO:0000313|Proteomes:UP000231742};
RN   [1] {ECO:0000313|EMBL:PJJ78571.1, ECO:0000313|Proteomes:UP000231742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16400 {ECO:0000313|EMBL:PJJ78571.1,
RC   ECO:0000313|Proteomes:UP000231742};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) 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:PJJ78571.1}.
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DR   EMBL; PGFH01000002; PJJ78571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9D326; -.
DR   OrthoDB; 4322898at2; -.
DR   Proteomes; UP000231742; 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:PJJ78571.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          20..221
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         77
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   284 AA;  30538 MW;  B3295BE78D750DAE CRC64;
     MSESTTDHPT THEVSAEIAR SWLLVAATRP EDFDAAERSR ADQIILDVED AVDPRLKPGA
     RDAVVEWLSN GGSGWVRIND RASDFWSDDV DALAGLPGLR GVMLAKAEAA AHVSETFDRL
     KGVTPVIALV ESALGIEEAV SIARARGAYR LAFGSGDYRR DTGASADDLA MAYPRSRLVI
     ASRVGNLPGP IDGPTVGTSH PVLREQGDMA VSLGMTGKLC LDIEQLPIIN EVISPTRSDV
     AWARDFLEDF EARGRVIRDG SDLPRLGRAQ KIDKLARAFG VEPA
//