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Database: UniProt
Entry: A0A0J1FLU5_9BURK
LinkDB: A0A0J1FLU5_9BURK
Original site: A0A0J1FLU5_9BURK 
ID   A0A0J1FLU5_9BURK        Unreviewed;       273 AA.
AC   A0A0J1FLU5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Dioxygenase {ECO:0000313|EMBL:KLU20688.1};
GN   ORFNames=EOS_39935 {ECO:0000313|EMBL:KLU20688.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU20688.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU20688.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
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:KLU20688.1}.
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DR   EMBL; AEJF01000245; KLU20688.1; -; Genomic_DNA.
DR   RefSeq; WP_047897758.1; NZ_AEJF01000245.1.
DR   AlphaFoldDB; A0A0J1FLU5; -.
DR   PATRIC; fig|908627.4.peg.8941; -.
DR   Proteomes; UP000035963; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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   Dioxygenase {ECO:0000313|EMBL:KLU20688.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          12..260
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   273 AA;  29910 MW;  52C799C310277B2B CRC64;
     MPSESSARMP VMFFGHGSPM NAIDDNRATQ AWKAMGEAAG TPRAILMISA HWMTRGTAVT
     AMHKPRTIHD FGAFPKALFD QRYPAPGDPE LAKRVAELLL PTPVALDGNW GFDHGTWSVL
     VKAFPRADIP VVQLSMNRAG NARFHYELGR ALRPLRDEGI LIAASGNVVH NLPAMDWGSP
     TIGFDWAQRF HDHVLKAIID DEPDQVIDYQ RAGEAAARSI PTPEHYWPFL YALGARHADD
     PVKVETNFLE YGSLSMLSFI LGGSAGVSTP ALT
//
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