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Database: UniProt
Entry: A0A085EQC7_9BURK
LinkDB: A0A085EQC7_9BURK
Original site: A0A085EQC7_9BURK 
ID   A0A085EQC7_9BURK        Unreviewed;       261 AA.
AC   A0A085EQC7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Extradiol ring-cleavage dioxygenase class III enzyme subunit B domain-containing protein {ECO:0000259|Pfam:PF02900};
GN   ORFNames=FG94_05063 {ECO:0000313|EMBL:KFC61422.1};
OS   Massilia sp. LC238.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC61422.1, ECO:0000313|Proteomes:UP000028601};
RN   [1] {ECO:0000313|EMBL:KFC61422.1, ECO:0000313|Proteomes:UP000028601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC238 {ECO:0000313|EMBL:KFC61422.1,
RC   ECO:0000313|Proteomes:UP000028601};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000256|ARBA:ARBA00007581}.
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:KFC61422.1}.
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DR   EMBL; JNNN01000083; KFC61422.1; -; Genomic_DNA.
DR   RefSeq; WP_036217448.1; NZ_JNNN01000083.1.
DR   AlphaFoldDB; A0A085EQC7; -.
DR   STRING; 1502852.FG94_05063; -.
DR   PATRIC; fig|1502852.3.peg.4978; -.
DR   eggNOG; COG3384; Bacteria.
DR   OrthoDB; 9790889at2; -.
DR   Proteomes; UP000028601; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProt.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR   Gene3D; 3.40.830.10; LigB-like; 1.
DR   InterPro; IPR014436; Extradiol_dOase_DODA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   PANTHER; PTHR30096:SF0; 4,5-DOPA DIOXYGENASE EXTRADIOL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR   Pfam; PF02900; LigB; 1.
DR   PIRSF; PIRSF006157; Doxgns_DODA; 1.
DR   SUPFAM; SSF53213; LigB-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..260
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   261 AA;  27967 MW;  75A0DA1B35DB6F3C CRC64;
     MPRLPALFIS HGSPMLALQD SPARRFLEQL GATLPRPRAV LAVSAHWETI GAPAVSLAQQ
     PATIHDFGGF PRALFEIRYP APGAPGLAER ALSLLEQAGI QAGRSAGRGL DHGAWVPLRL
     MYPDADVPVT QLSILQGGDP AAHLRIGQAL GALRDEGVLV LASGSLTHNL HEYRGQAVEA
     PAPAWVEDFA RWMQASLENG DQAELLDYRR RAPNAVRNHP TDEHLLPLFV ALGAGGPQAR
     ATRLHASVEH GVLAMDAYAF E
//
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