ID A0A160FQL1_9BURK Unreviewed; 455 AA.
AC A0A160FQL1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:ANB74964.1};
GN ORFNames=AYM40_21235 {ECO:0000313|EMBL:ANB74964.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB74964.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB74964.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB74964.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; CP014579; ANB74964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160FQL1; -.
DR STRING; 1804984.AYM40_21235; -.
DR KEGG; buz:AYM40_21235; -.
DR Proteomes; UP000076852; Chromosome 2.
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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
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.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT DOMAIN 65..175
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 455 AA; 50901 MW; EBC27A3EE3D9EB2B CRC64;
MEHICSHFDS PQANAISPVR FVRNVHAADP AALRELVDPG RVHSALYTSP EIFELEIEKI
FHSSWVYVGH ASEVPVAGDF RVRRLGTQPV IMVRGHDRVV RVLMNRCRHR GAAVCEVEAG
REKFFRCWFH GWTYDNTGKL VSVTDPEGYG PSFSLDDHSL TAAPRVAVYR DFVFASLSSD
VPPLEEYLGQ AAQMIDLLVD ASPDREIEVS AGVHKTVYNG NWKLVGMDGY HPHYVHASVV
SMWQRQADSG IGATHRADPF DGKAKTFTRD LGHGHAMLDM REHRVEHFSD YEKFLRGVTG
GAEYINALHA RDGADHAKLL LAIAGDPHIG VFPNMQIINN QIRIMVPLEA GRTEVLMFPV
LLKGVSPEIN TMRLRQHESF YGPAGAGSPD DAEIFERVQR GMNAQVDPWI DISRGIGREK
VELDGTIIGH ISDEVPQRGQ MRYWLKLMTK GAEIE
//
