ID B2MV36_9NOCA Unreviewed; 443 AA.
AC B2MV36;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Dibenzofuran dioxygenase alpha subunit {ECO:0000313|EMBL:ACC85681.1};
GN Name=dbfA1 {ECO:0000313|EMBL:ACC85681.1};
OS Rhodococcus sp. HA01.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=522341 {ECO:0000313|EMBL:ACC85681.1};
RN [1] {ECO:0000313|EMBL:ACC85681.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HA01 {ECO:0000313|EMBL:ACC85681.1};
RX PubMed=18441103; DOI=10.1128/AEM.00226-08;
RA Aly H.A., Huu N.B., Wray V., Junca H., Pieper D.H.;
RT "Two angular dioxygenases contribute to the metabolic versatility of
RT dibenzofuran-degrading Rhodococcus sp. strain HA01.";
RL Appl. Environ. Microbiol. 74:3812-3822(2008).
RN [2] {ECO:0000313|EMBL:ACC85681.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HA01 {ECO:0000313|EMBL:ACC85681.1};
RA Aly H.A.H., Nguyen H.B., Wray V., Howard J., Pieper D.H.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; EU622791; ACC85681.1; -; Genomic_DNA.
DR AlphaFoldDB; B2MV36; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW Dioxygenase {ECO:0000313|EMBL:ACC85681.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 50..146
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 443 AA; 49566 MW; EF539CFB6D44DB94 CRC64;
MTSISERPVD VAAAGLHDLV KPDEGSVSRT VFVDEAIYRK ELDRVFTKTW LFIGHESQLS
EPGDYLTNFM GEDPVIATRG ADGVIRVMLN SCAHRGMAVC STDAGSSKFF RCPYHGWTYS
NNGDLIGVPR ADTVYHGELD KSRLGLKAVP RVENYKGFIF ANWDEDAIPL VDYLGADQLW
YLDLAFEAPL GGLEVIGPTM KFRIKANWKL AAENFAGDDY HVLYTHGSAF QIGFLPDYDT
LGDYIAYFGH GHGMGDISKP GRAYQNDVGM AQFLGPEAIE YVNAVHERLK ARVSPLQAEM
HGLGQGNIFP NLSWIKFGVF HVFGLFQWHP RGPGEIEVWQ TALFDRDAPQ SVKDFARTQM
SQENAAAGIF GQDDGENFEQ ITESARGVVS QTRDFNYAMG LGHEGEIHEE GYPGHLGPHY
SEQNHRNFYR YWLELMTTPG EQK
//
