ID   A0A1A0NAB0_9MYCO        Unreviewed;       298 AA.
AC   A0A1A0NAB0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:OBA94236.1};
GN   ORFNames=A5662_19730 {ECO:0000313|EMBL:OBA94236.1};
OS   Mycobacteriaceae bacterium 1482268.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae.
OX   NCBI_TaxID=1834080 {ECO:0000313|EMBL:OBA94236.1, ECO:0000313|Proteomes:UP000091934};
RN   [1] {ECO:0000313|EMBL:OBA94236.1, ECO:0000313|Proteomes:UP000091934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1482268.1 {ECO:0000313|EMBL:OBA94236.1,
RC   ECO:0000313|Proteomes:UP000091934};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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:OBA94236.1}.
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DR   EMBL; LZSH01000363; OBA94236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A0NAB0; -.
DR   Proteomes; UP000091934; 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:OBA94236.1};
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          1..219
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   298 AA;  31963 MW;  D086FA761E88CD7F CRC64;
     MIEKAKTLPA DEVFLDLEDA VAPDAKEEAR TRVATALADS GWAGQLRGVR VNDWTTPWTY
     ADIIEVVSTA GACIDIIVLP KVTDVSHITA LDLLLSQLET THGLPVGRIG IEAQIENAQG
     LTNIDAIAAG PRVQALVLGP ADMAASLNMR TLEVGEQPEG YDVGDAHHHV LMRILIAART
     HGVLAIDGPY LKVRDVDAFR RVAGRSAALG YDGKWVLHPD QIAAGNDLFS PRQADYDHAE
     LILEAYEWHT SRAGGARGAV MLGDEMIDEA SRKMALVIAG KGRAAGMTRK AEPFQPPS
//