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Database: UniProt
Entry: A0A0T2YQV0_9BURK
LinkDB: A0A0T2YQV0_9BURK
Original site: A0A0T2YQV0_9BURK 
ID   A0A0T2YQV0_9BURK        Unreviewed;       344 AA.
AC   A0A0T2YQV0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Rieske (2Fe-2S) protein {ECO:0000313|EMBL:KRC01338.1};
GN   ORFNames=ASE11_06950 {ECO:0000313|EMBL:KRC01338.1};
OS   Hydrogenophaga sp. Root209.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRC01338.1, ECO:0000313|Proteomes:UP000050889};
RN   [1] {ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|Proteomes:UP000050889};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC01338.1, ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|EMBL:KRC01338.1,
RC   ECO:0000313|Proteomes:UP000050889};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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:KRC01338.1}.
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DR   EMBL; LMIE01000022; KRC01338.1; -; Genomic_DNA.
DR   RefSeq; WP_056272099.1; NZ_LMIE01000022.1.
DR   AlphaFoldDB; A0A0T2YQV0; -.
DR   STRING; 1736490.ASE11_06950; -.
DR   OrthoDB; 9790995at2; -.
DR   Proteomes; UP000050889; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044270; P:cellular nitrogen compound catabolic process; IEA:UniProt.
DR   GO; GO:1901565; P:organonitrogen compound catabolic process; IEA:UniProt.
DR   CDD; cd08878; RHO_alpha_C_DMO-like; 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; IPR044043; VanA_C_cat.
DR   PANTHER; PTHR21266:SF61; 3-KETOSTEROID-9-ALPHA-MONOOXYGENASE, OXYGENASE COMPONENT; 1.
DR   PANTHER; PTHR21266; IRON-SULFUR DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF19112; VanA_C; 1.
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   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          7..107
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   344 AA;  38369 MW;  8C90DD0F37327A3A CRC64;
     MFPKNTWYVG ATPSELDGKP LGRKICGESI VFFRGPDNKV AAVEDFCPHR GAPLSLGKVE
     NGKLVCGYHG LEMGCDGKTV AMPCQRVGGF PAVRTYPVVE RYGFIWVWPG DAQEADPSKI
     HHLAWADDPE WAYSGGLYHV KCDYRLMIDN LMDLTHETYL HPNSIGQKEI DESPPKTRMD
     GDCAITERYM EGIMAPPFWR AGLRGNNLAD DVPVDRWQIC RFYPPSHVLI DVGVAHAGKG
     GFNADPKVKA SSTVIDFITP ETESSTWYFW GMARNFNAQD QALSEQIRTS LSKVFSEDLQ
     MLEMQQQNLE RNAGRKLLSL NIDGGGVQAR RIIDRLLVAE KSAA
//
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