ID   A0A2K3UUR8_9DEIO        Unreviewed;       293 AA.
AC   A0A2K3UUR8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:PNY80278.1};
GN   ORFNames=CVO96_01885 {ECO:0000313|EMBL:PNY80278.1};
OS   Deinococcus koreensis.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2054903 {ECO:0000313|EMBL:PNY80278.1, ECO:0000313|Proteomes:UP000236379};
RN   [1] {ECO:0000313|EMBL:PNY80278.1, ECO:0000313|Proteomes:UP000236379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJW1-2 {ECO:0000313|EMBL:PNY80278.1,
RC   ECO:0000313|Proteomes:UP000236379};
RA   Choi A.;
RT   "Deinococcus koreensis sp. nov., a radiation-resistant bacterium isolated
RT   from river water.";
RL   Submitted (JAN-2018) 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:PNY80278.1}.
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DR   EMBL; PPPD01000001; PNY80278.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3UUR8; -.
DR   OrthoDB; 9786940at2; -.
DR   Proteomes; UP000236379; 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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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:PNY80278.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236379}.
FT   DOMAIN          9..223
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   293 AA;  30171 MW;  3A569FCCCF6DF221 CRC64;
     MTPFLARPRS VLFAPGNRPE LIAKLPRSGP DAVVIDLEDA IPGTAGAKAG ARPVARDAAR
     DLVAAAPHLA VFLRVNALHS PYFADDLGVL TPELAGVVVP KLESAADVEA VVEALEARGL
     SLPLLAGLET GAGVWNAREI LAHPAVRWAY FGAEDYTADL GGSRTPGGLE VLYARSQVAL
     AARLSGVPAL DIVVTALNDE PAFRADGALG RALGFVGKLC IHPAQVALAH ELFGPTSAEV
     ERARALLDAA HEAAASGHGA FSFEGQMVDE PMLVRARALV SSGDAAAEAG GRP
//