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Database: UniProt
Entry: A0A0M5LWR7_9PSEU
LinkDB: A0A0M5LWR7_9PSEU
Original site: A0A0M5LWR7_9PSEU 
ID   A0A0M5LWR7_9PSEU        Unreviewed;       377 AA.
AC   A0A0M5LWR7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Iron-sulfur protein {ECO:0000313|EMBL:ALE84907.1};
GN   ORFNames=XF36_18660 {ECO:0000313|EMBL:ALE84907.1};
OS   Pseudonocardia sp. HH130629-09.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE84907.1, ECO:0000313|Proteomes:UP000062082};
RN   [1] {ECO:0000313|EMBL:ALE84907.1, ECO:0000313|Proteomes:UP000062082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE84907.1,
RC   ECO:0000313|Proteomes:UP000062082};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
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DR   EMBL; CP011868; ALE84907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M5LWR7; -.
DR   KEGG; pseh:XF36_18660; -.
DR   PATRIC; fig|1641402.3.peg.4007; -.
DR   Proteomes; UP000062082; 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; cd08887; RHO_alpha_C_3; 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; 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; 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.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062082}.
FT   DOMAIN          43..150
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   377 AA;  42404 MW;  5E2E9D49C74303EB CRC64;
     MFDHLDNGTT DMAPGVLEID PGVYRDPELA ARERAELFGY VPIIAAHGTE LPKPNDYLTV
     QLPNNEVVLV RQRDGQVRAF VNTCRHRGAR LVNEDSGNRR FFSCRYHGWS YGGDGSLRAI
     ADGSTFGEMD TTCLGLKEVP AEERHGFVWA VDSAAPGRKI DVGEWLGPDL DASLGAMEMD
     RYHCHRAGNF DLEINWKVLM DAFLDGYHIA YAHTGTVAPY FHNNAQTWQP MGRHGRMVSA
     RRSIDTIRGQ DPATVDVNRH LTVAHFLMPN MSVLRQPDHL EVLNFVPAPH TAVGTRMQMR
     ILTREPATTD ELTARWEKNW TILQAVLQDE DIVVNEGLQK AVSNTDIGPL HFGRNEIANQ
     HFHRWMAAAL ADPRHWG
//
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