ID A0A1A2KUD4_9MYCO Unreviewed; 299 AA.
AC A0A1A2KUD4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=2,3-dihydroxybiphenyl 1,2-dioxygenase {ECO:0000313|EMBL:OBG81914.1};
GN ORFNames=A5699_07625 {ECO:0000313|EMBL:OBG81914.1};
OS Mycobacterium sp. E802.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834152 {ECO:0000313|EMBL:OBG81914.1, ECO:0000313|Proteomes:UP000092062};
RN [1] {ECO:0000313|EMBL:OBG81914.1, ECO:0000313|Proteomes:UP000092062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E802 {ECO:0000313|EMBL:OBG81914.1,
RC ECO:0000313|Proteomes:UP000092062};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBG81914.1}.
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DR EMBL; LZJD01000155; OBG81914.1; -; Genomic_DNA.
DR RefSeq; WP_067773994.1; NZ_LZJD01000155.1.
DR AlphaFoldDB; A0A1A2KUD4; -.
DR Proteomes; UP000092062; 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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07237; BphC1-RGP6_C_like; 1.
DR CDD; cd07252; BphC1-RGP6_N_like; 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; IPR037523; VOC.
DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR21366:SF34; IRON-DEPENDENT EXTRADIOL DIOXYGENASE; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR PROSITE; PS51819; VOC; 2.
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 5..120
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 142..270
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 299 AA; 33435 MW; E0370F7EAE5949D2 CRC64;
MSIKSLGYLR IEATDMAAWR EYGLKVLGMV EGSGKTEGAL YLRMDEFPAR LVIVPGEHDR
LLESGWETAN AAELQDIRTR LEANGTPYKE ATAAELADRR VDGMIIFEDP SGNRLEVFHG
VALEHRRVVS PYGHKFVTEE QGLGHVVLTT KDDAESLHFY RDVLGFYLRD SMRLPPQLVG
RPADGDPAWL RFLGVNPRHH SVAFMPGQTP SGIVHLMVEV ENSDDVGLCL DRALRRKVKM
SATLGRHVND KMLSFYMKTP GGFDVEFGCE GLEVDDDNWV ARESTAVSLW GHDFSVGFK
//