ID   C1CY49_DEIDV            Unreviewed;       130 AA.
AC   C1CY49;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative glyoxalase/bleomycin resistance protein/dioxygenase superfamily, putative lactoylglutathione lyase {ECO:0000313|EMBL:ACO47005.1};
GN   OrderedLocusNames=Deide_20000 {ECO:0000313|EMBL:ACO47005.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47005.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO47005.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001114; ACO47005.1; -; Genomic_DNA.
DR   RefSeq; WP_012694126.1; NC_012526.1.
DR   AlphaFoldDB; C1CY49; -.
DR   STRING; 546414.Deide_20000; -.
DR   PaxDb; 546414-Deide_20000; -.
DR   KEGG; ddr:Deide_20000; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_099500_2_0_0; -.
DR   OrthoDB; 9802805at2; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000313|EMBL:ACO47005.1};
KW   Lyase {ECO:0000313|EMBL:ACO47005.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ACO47005.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT   DOMAIN          3..122
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
SQ   SEQUENCE   130 AA;  14064 MW;  C4D5631976278B7F CRC64;
     MLRALETCLY ADDLALAEPF YTEVLGLTLH SKVAGRHLFY QLEGSMLLIF SPAGLAQTNG
     VPSHSGKAGG HACLAIARDQ TDGWEARLIS HGLEVTRYAW GDRGESLYFH DPAGNVLELA
     PPSIWGILDA
//