ID   A0A286H0Z3_9ACTN        Unreviewed;       317 AA.
AC   A0A286H0Z3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SOE01443.1};
GN   ORFNames=SAMN06272739_3164 {ECO:0000313|EMBL:SOE01443.1};
OS   Blastococcus haudaquaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOE01443.1, ECO:0000313|Proteomes:UP000219482};
RN   [1] {ECO:0000313|Proteomes:UP000219482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2017) 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; OCNK01000003; SOE01443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286H0Z3; -.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000219482; 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:SOE01443.1};
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:UP000219482}.
FT   DOMAIN          9..238
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   317 AA;  34291 MW;  BDF73EE2CEA8D1CE CRC64;
     MAELRSRRSN LAVPGSNPRF LEKAKGLPAD QVFLDLEDAC APLAKPGARK NIVAALNEGG
     WGDKIRTVRV NDWTTEWTFQ DVLEVVGGAG AELDCIMLPK VQDAAQVKAL DLLLTQIEKA
     NGLEVGRIGI EAQIETAQGL INVNDIAFAS DRIETIIFGP ADFMASINMK SLVVGALHPD
     YPGDPFHYIL MQILMAARAR GVQAIDGPFL QVRDVPAFEE VAKRSAMLGF DGKWVLHPGQ
     IDAANEIYAP SQEDYDHAEL ILDAYDWATS EAGGKKGSAM LGDEMIDEAS RKMALVIAGK
     GRAAGMERTS SFTPPEQ
//