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
//