ID   A0A1M5ERY5_9ACTN        Unreviewed;       317 AA.
AC   A0A1M5ERY5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SHF82025.1};
GN   ORFNames=SAMN05444351_0909 {ECO:0000313|EMBL:SHF82025.1};
OS   Geodermatophilus nigrescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1070870 {ECO:0000313|EMBL:SHF82025.1, ECO:0000313|Proteomes:UP000184471};
RN   [1] {ECO:0000313|EMBL:SHF82025.1, ECO:0000313|Proteomes:UP000184471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45408 {ECO:0000313|EMBL:SHF82025.1,
RC   ECO:0000313|Proteomes:UP000184471};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQVX01000001; SHF82025.1; -; Genomic_DNA.
DR   RefSeq; WP_073418798.1; NZ_FQVX01000001.1.
DR   AlphaFoldDB; A0A1M5ERY5; -.
DR   STRING; 1070870.SAMN05444351_0909; -.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000184471; 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:SHF82025.1};
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:UP000184471}.
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;  34452 MW;  1B38D7334AC960A6 CRC64;
     MAELRSRRSN LAVPGSNPRF LEKAKGLPAD QVFLDLEDAC APLAKPGARK NIVAALNEGG
     WGEKIRTVRV NDWTTEWTYR DVIEVVEGAG ANLDCIMLPK VVDAHQVAAL DFLLTQIEKA
     NGLEVGRIGI EAQIETAQGL INVNDIAFAS PRIETIIFGP ADFMASINMK SLVVGALHPD
     YPGDPFHYIL MQILMAARAR GVQAIDGPFL QVRDVDAFRE VAKRSAVLGF DGKWVLHPGQ
     IDAANEIYAP SQEDYDHAEL ILDAYDWYTS EAGGKKGSAM LGDEMIDEAS RKMALVIAGK
     GRAAGMSRTS SFTPPED
//