ID D6Y303_THEBD Unreviewed; 303 AA.
AC D6Y303;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Rieske (2Fe-2S) domain protein {ECO:0000313|EMBL:ADG86964.1};
GN OrderedLocusNames=Tbis_0232 {ECO:0000313|EMBL:ADG86964.1};
OS Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS 10125 / KCTC 9307 / NBRC 14880 / R51).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Thermobispora.
OX NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG86964.1, ECO:0000313|Proteomes:UP000006640};
RN [1] {ECO:0000313|EMBL:ADG86964.1, ECO:0000313|Proteomes:UP000006640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermobispora bispora DSM 43833.";
RL Submitted (JAN-2010) 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 ferredoxin component family. {ECO:0000256|ARBA:ARBA00038001}.
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DR EMBL; CP001874; ADG86964.1; -; Genomic_DNA.
DR RefSeq; WP_013130497.1; NC_014165.1.
DR AlphaFoldDB; D6Y303; -.
DR STRING; 469371.Tbis_0232; -.
DR KEGG; tbi:Tbis_0232; -.
DR eggNOG; COG2146; Bacteria.
DR HOGENOM; CLU_065805_0_0_11; -.
DR Proteomes; UP000006640; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd03467; Rieske; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR019251; DUF2231_TM.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR21496; FERREDOXIN-RELATED; 1.
DR PANTHER; PTHR21496:SF0; RIESKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF09990; DUF2231; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006640};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..298
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 303 AA; 32433 MW; F64B498B4F1DA136 CRC64;
MDEKTRPPRT HRLTRMVPSP EFLRGLERTT TLDAPIRAIS KTLRTRLGPG RLRDMLHGVP
FGHPLHPALA MVSLGCWVST AVLDVTKADP RASRALIATG LGTALPTAAA GITDWSTLHL
EQQRVGVFHA LSNLAAAALY TGSLLMRLGG RERTGRVLAF AGLGAVSIGG FLGGHLAYRQ
AAGANHAESV GHLTLLGWHD LCLLKDLPDG RPVRRQLGYI DLVVLRLGDT VHVLADGCSH
LAGPLHQGRV TVEEGEPCIV CPWHGSTFRV SDGSVVHGPA TSPQPAFETR LRHDGVVQVR
PAM
//
