ID   A0A0H2KQA3_9MICO        Unreviewed;       285 AA.
AC   A0A0H2KQA3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Citrate lyase {ECO:0000313|EMBL:KLN35700.1};
GN   ORFNames=FB00_05280 {ECO:0000313|EMBL:KLN35700.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN35700.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN35700.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN35700.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-2014) 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:KLN35700.1}.
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DR   EMBL; JNBQ01000003; KLN35700.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2KQA3; -.
DR   STRING; 264251.FB00_05280; -.
DR   PATRIC; fig|264251.5.peg.1084; -.
DR   Proteomes; UP000035265; 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:KLN35700.1};
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:UP000035265}.
FT   DOMAIN          14..223
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   285 AA;  28844 MW;  F4951CE89FDD324F CRC64;
     MVSHDGGLGL GPALLFCPGD RPDRFAKAAD RADAVILDLE DAVAAASKDA ARRAVVEASA
     TLDPARTVVR VNAVGTPEHA LDVAALADTR LRTVMVAKSG PELLGSLAAL ATTLPGVRVL
     ALCETAAGVL AAPELARRPE VVALMWGAED LVASLGGTSS RRPDGSYRDV ARHARSAVLL
     AAGAAGKAAV DAVHVDVGDL DGLRAEAEDA AASGFAATAC IHPSHVPVIR AAYAPTPEQV
     TAARALLDAA AANPGGPDAV FTHDGRMVDG PVLRHAEAVL RRAGT
//