ID C4L0L3_EXISA Unreviewed; 267 AA.
AC C4L0L3;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Glyoxalase/bleomycin resistance protein/dioxygenase {ECO:0000313|EMBL:ACQ70876.1};
GN OrderedLocusNames=EAT1b_1952 {ECO:0000313|EMBL:ACQ70876.1};
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ70876.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ70876.1, ECO:0000313|Proteomes:UP000000716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX PubMed=21460088; DOI=10.1128/JB.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954,
CC ECO:0000256|RuleBase:RU000683};
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00008784, ECO:0000256|RuleBase:RU000683}.
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DR EMBL; CP001615; ACQ70876.1; -; Genomic_DNA.
DR RefSeq; WP_015880435.1; NC_012673.1.
DR AlphaFoldDB; C4L0L3; -.
DR STRING; 360911.EAT1b_1952; -.
DR KEGG; eat:EAT1b_1952; -.
DR eggNOG; COG2514; Bacteria.
DR HOGENOM; CLU_059557_0_0_9; -.
DR OrthoDB; 9792626at2; -.
DR Proteomes; UP000000716; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07255; VOC_BsCatE_like_N; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR PANTHER; PTHR43279; CATECHOL-2,3-DIOXYGENASE; 1.
DR PANTHER; PTHR43279:SF1; CATECHOL-2,3-DIOXYGENASE; 1.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|RuleBase:RU000683};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU000683};
KW Iron {ECO:0000256|RuleBase:RU000683};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000683}.
FT DOMAIN 7..121
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 267 AA; 29833 MW; BF2308B169219D3E CRC64;
MKIEKIELGP VTLRVRDIEQ VTRFYVDVIG MSVLEESEEH ITLGTKERPL VILHSVPQAK
TNPRAAGLFH LAILFPNRIE LGSMLAHLIE RRVEVGQGDH LVSEAFYLSD PEGNGIELYA
DRPKDQWTYE ANGHVKMATE PVDYESMLQA AANRPFTGLP IGTTMGHVHF KVRSIEAAKR
FYHDRLGFSI TTDSYPGALF LAADGYHHHI GTNVWARPSD PMGMETGLES WTLLVNEDTN
RALGGTSSEW TLTDEDGITV HIKRTDA
//
