ID A0A0S3F2T8_9SPHN Unreviewed; 401 AA.
AC A0A0S3F2T8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:ALR22041.1};
GN ORFNames=ATN00_18770 {ECO:0000313|EMBL:ALR22041.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR22041.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR22041.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR22041.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; CP013264; ALR22041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3F2T8; -.
DR STRING; 1332080.ATN00_18770; -.
DR KEGG; sbd:ATN00_18770; -.
DR OrthoDB; 7458380at2; -.
DR Proteomes; UP000056968; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00680; RHO_alpha_C; 1.
DR CDD; cd03469; Rieske_RO_Alpha_N; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000056968}.
FT DOMAIN 56..163
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 401 AA; 45739 MW; E7F8E398C6E7C270 CRC64;
MLNARLLSIR EDSERESGRA DYPQDFPALP PVPVGRYVEQ DFYDLEMKHL WPRTWLYAGH
ASEIPEPGCY KLFEQLGQSV IVSRGEGGEI RAFHNICRHR ASALVVEDSG KTRRFVCPYH
SWSYDLDGGL IGVPEERDFK CLDKAERGLK RVHCETMRGM IFINLDGNAP PLEEYFASTL
RELEGFPLED MVVNAVISVE MECNWKAALD NFLEAYHINT IHAKSIAPYL DSRSFNISLF
RGGHARFATR KRGAGTIFGK DLAIPQGPSE IFRTHTIALP MFPNSFIAVD PVGFGWQSWW
PVGMNRTVMT FTLMGWRDDV NRGPGFREAM VEQVKAIANE DVHLFPRLQR SLESGAVSSL
LLGYQERALY WYQEEIDRRI GPQNIPQHLR IEQILAPFTA D
//
