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Database: UniProt
Entry: Q1AVQ6_RUBXD
LinkDB: Q1AVQ6_RUBXD
Original site: Q1AVQ6_RUBXD 
ID   Q1AVQ6_RUBXD            Unreviewed;       434 AA.
AC   Q1AVQ6;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Rieske (2Fe-2S) region {ECO:0000313|EMBL:ABG04522.1};
GN   OrderedLocusNames=Rxyl_1560 {ECO:0000313|EMBL:ABG04522.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04522.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG04522.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
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DR   EMBL; CP000386; ABG04522.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1AVQ6; -.
DR   STRING; 266117.Rxyl_1560; -.
DR   KEGG; rxy:Rxyl_1560; -.
DR   eggNOG; COG4638; Bacteria.
DR   HOGENOM; CLU_026244_3_0_11; -.
DR   PhylomeDB; Q1AVQ6; -.
DR   Proteomes; UP000006637; 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: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   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; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43756:SF5; 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   4: Predicted;
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:UP000006637}.
FT   DOMAIN          64..145
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  49901 MW;  B106FD2470727EC8 CRC64;
     MTIDRVDKQV AANPKPKTPE DFTREETYRL TRLPVELAST LLPEAYTSPE FFDIEKERVF
     AKSWIPVGFV SQVREPGRTI VAEVAGRSII IARDKSGKLR AFHNVCRHRA ARLLDEGCHV
     VRNNRIRCPY HSWTYDLEGK CLGTPLFEGS DIPEEGRTAF DMSGVKGFDK ADYGLLPVRV
     DSWGFLVFVN LDPETIPLKK YLGDLPERFS SYQLEEWRVV RQKTYDIAAN YKLIGENFME
     YYHLPWVHPE LVKVSRMEDH YRWQGPGMYM GFCTTPISQN TEAGGWQGLP PISSLSKEEA
     VSARFIWLFP NTAVNILPNH SFVMITRPDG PGHTVEDTFI LSHPESLANP EAEEKLDQLA
     RFWDLVNVQD IEIVERVQQG ISNPEYRGGR MCYRFEEPLH RYQNMVIDKM AGIERVPPGD
     DEEMVRMFDS NTDS
//
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