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Database: UniProt
Entry: A0A0G3IJT2_9MYCO
LinkDB: A0A0G3IJT2_9MYCO
Original site: A0A0G3IJT2_9MYCO 
ID   A0A0G3IJT2_9MYCO        Unreviewed;       438 AA.
AC   A0A0G3IJT2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:AKK27843.1};
GN   ORFNames=AB431_15425 {ECO:0000313|EMBL:AKK27843.1};
OS   Mycobacterium sp. EPa45.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK27843.1, ECO:0000313|Proteomes:UP000035237};
RN   [1] {ECO:0000313|Proteomes:UP000035237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA   Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA   Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT   "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT   Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL   Genome Announc.0:0-0(2015).
RN   [2] {ECO:0000313|EMBL:AKK27843.1, ECO:0000313|Proteomes:UP000035237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPa45 {ECO:0000313|EMBL:AKK27843.1,
RC   ECO:0000313|Proteomes:UP000035237};
RX   PubMed=26184940;
RA   Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA   Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT   "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT   Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT   Consortium.";
RL   Genome Announc. 3:e00782-15(2015).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR   EMBL; CP011773; AKK27843.1; -; Genomic_DNA.
DR   RefSeq; WP_047330667.1; NZ_CP011773.1.
DR   AlphaFoldDB; A0A0G3IJT2; -.
DR   STRING; 1545728.AB431_15425; -.
DR   KEGG; mye:AB431_15425; -.
DR   PATRIC; fig|1545728.4.peg.3137; -.
DR   OrthoDB; 5243643at2; -.
DR   Proteomes; UP000035237; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051213; F:dioxygenase activity; 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   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR043266; RHO_NdoB-like_C.
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:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43756; 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   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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}.
FT   DOMAIN          37..147
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   438 AA;  49386 MW;  75B0D822D71679F2 CRC64;
     METIGSTTAS AATIDSSAFY DEAVYQRELE VVFKRSWLFV GHESMIPNPG DFRTTYMADD
     AVIVCRDKAS NVRVLLNKCR HRGNKVCQFD KGNANIFRCS YHGWSYDTAG RLRSVPLSDS
     VYGPQFDKSS MGLVSPRVAT HKGLIFACWD DSAPPLREYL GEDLLWYLDN FLLGTDPKGL
     QVVPGLHRYL MPVNWKLLAE NFGGDQYHFA ATHGSVAALS NAGQTARIDF SIDKGQHYSV
     VLNGCAPHGL LQLAIGDNFY QDDLAHAETL GSEVVDWLTE RQRRQNERLG TYPVQPYSFH
     VANIFPNFSM IGMGTAFYGR GFIMWQPRGP RLTEVWEWCL VENSAPRAAK ERMVFVLSQR
     QSAAGLVTPD DHENFERLSD ALATGVARDV PFNYSLGEDV EPLDSLITEL PGNVRPQISE
     SYQREFYRHW RRAMTEPV
//
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