ID G7UVG8_PSEUP Unreviewed; 452 AA.
AC G7UVG8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Rieske (2Fe-2S) domain-containing protein {ECO:0000313|EMBL:AER57629.1};
GN OrderedLocusNames=DSC_14925 {ECO:0000313|EMBL:AER57629.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER57629.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER57629.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER57629.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; CP003093; AER57629.1; -; Genomic_DNA.
DR RefSeq; WP_014161802.1; NC_016147.2.
DR AlphaFoldDB; G7UVG8; -.
DR STRING; 1045855.DSC_14925; -.
DR KEGG; psd:DSC_14925; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_1_6; -.
DR OrthoDB; 9769355at2; -.
DR Proteomes; UP000005870; Chromosome.
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 CDD; cd08879; RHO_alpha_C_AntDO-like; 1.
DR CDD; cd03542; Rieske_RO_Alpha_HBDO; 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; 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 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:UP000005870}.
FT DOMAIN 54..151
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 452 AA; 50982 MW; BC0B574F0E6C4A0C CRC64;
MSAIIENKTD LEQLLATAVQ DDPVAGLYRC RRDIFTDPDL FELEIKHLFE SNWVYLAHES
QIPNNNDYFT TYIGRQPVVI TRDKAGELHA LINACAHRGA MLCRRKHGNK GSFTCPFHGW
TFSNTGKLLK VKDEKTTQYP PQFGEHGSHD LKRVARLQSY RGFLFGSLSE QVAPLEDFLG
ETRIIIDQIV DQAPDGLEVL RGSSSYIYDG NWKLQMENGC DGYHVSSVHW NYAATMGRRK
QTGTKAVDAN GWSKSVGGVY GFDNGHILLW TNSLNPEVRP VWNRREELAA RLGAAKAEFI
TRQTRNLCLY PNVYLMDQFS TQIRVTRPIA VDKTEVTIYC FGIKGESAQD RATRIRQYED
FFNVSGMGTA DDLEEFRACQ NGYAGTAAAW NDLSRGAPLW VQGADENARK MGIKPLLSGN
RSEDEGLFVR QHEYWARAMR QALAREATGD AA
//
