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Database: UniProt
Entry: B2HML6_MYCMM
LinkDB: B2HML6_MYCMM
Original site: B2HML6_MYCMM 
ID   B2HML6_MYCMM            Unreviewed;       516 AA.
AC   B2HML6;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN   OrderedLocusNames=MMAR_5381 {ECO:0000313|EMBL:ACC43785.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43785.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC43785.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
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DR   EMBL; CP000854; ACC43785.1; -; Genomic_DNA.
DR   RefSeq; WP_012396882.1; NC_010612.1.
DR   AlphaFoldDB; B2HML6; -.
DR   STRING; 216594.MMAR_5381; -.
DR   KEGG; mmi:MMAR_5381; -.
DR   eggNOG; COG2146; Bacteria.
DR   eggNOG; COG2220; Bacteria.
DR   HOGENOM; CLU_525630_0_0_11; -.
DR   OrthoDB; 6988582at2; -.
DR   Proteomes; UP000001190; Chromosome.
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   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   PANTHER; PTHR15032; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR15032:SF4; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR   Pfam; PF13483; Lactamase_B_3; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT   DOMAIN          465..516
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   516 AA;  58140 MW;  BF3B3E47BF2DD797 CRC64;
     MQVTSVGHAG FLIQTQSGSI LCDPWVNPAY FASWFPFPDN SALDWDALGD CDYLYVSHLH
     KDHFDAENLR SHVNKDAVVL LPDFPVPDLR NELEKLGFHR FFETTDSVKH RLSGPRGDLD
     IMIIALRAPA DGPIGDSALV VSDGETTAFN MNDARPIELD MLASEFGHID VHLLQYSGAI
     WYPMVYDMPA RAKEAFGTQK RQRGMDRARQ YVAQVDATWV VPSAGPPCFL DPELRELNDD
     RSDPANIFPD QMVFLDQMRI HGHDRGLLMI PGSIADFTGS TLNSLSHPLP TEDVEAIFTT
     GKSAYIADYA DRMAPVIAAE RASWAPAEGE PLLEPLRALF EPIMLQSNEI CDGIGYPVEL
     VIGAETVVLD FPKRAVREPI PNEKFRYGFA IAPELVRTVL RDQEPDWVNT IFLSTRFQAW
     RVGGYNEYLY TFFKCLTDER IAYADGWFAE THDDSASITL DGWEIQRRCP HLKADLSKFG
     VVEGDTLTCN LHGWQWRLED GRCLTTRGHQ LRSSRK
//
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