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Database: UniProt
Entry: A0A095B7H7_9SPHN
LinkDB: A0A095B7H7_9SPHN
Original site: A0A095B7H7_9SPHN 
ID   A0A095B7H7_9SPHN        Unreviewed;       252 AA.
AC   A0A095B7H7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Extradiol ring-cleavage dioxygenase {ECO:0000313|EMBL:KGB58287.1};
GN   ORFNames=FG95_01029 {ECO:0000313|EMBL:KGB58287.1};
OS   Sphingopyxis sp. LC363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB58287.1, ECO:0000313|Proteomes:UP000029625};
RN   [1] {ECO:0000313|EMBL:KGB58287.1, ECO:0000313|Proteomes:UP000029625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC363 {ECO:0000313|EMBL:KGB58287.1,
RC   ECO:0000313|Proteomes:UP000029625};
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 (MAY-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:KGB58287.1}.
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DR   EMBL; JNFC01000011; KGB58287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095B7H7; -.
DR   STRING; 1120705.FG95_01029; -.
DR   PATRIC; fig|1120705.3.peg.1035; -.
DR   eggNOG; COG3384; Bacteria.
DR   Proteomes; UP000029625; 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:KGB58287.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029625};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          22..251
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   252 AA;  26597 MW;  5FD2F24963766FDB CRC64;
     MMALEPSPAR DFLAGLGAHL PRPRAILVVS AHHDAAYQGG RATVAASTAP PTIHDFGGFP
     DELFAMRYPA PGDPALAARV VELLAGRGLH VTADAARGLD HGAWVPLSLI YPDADIPVVQ
     LSIASNATPE WHYALGQALA PLRDEGVLIV GSGSITHNLR ALFSARPPID APAPAWVTDF
     TDWVAERMSV GAVDDVLNSV ERAPHGADNH PTPDHILPLF VAMGAGGTPL KGERLHRSVT
     YGLLAMDVYA FD
//
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