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Database: UniProt
Entry: A0A2C9T3J2_9MYCO
LinkDB: A0A2C9T3J2_9MYCO
Original site: A0A2C9T3J2_9MYCO 
ID   A0A2C9T3J2_9MYCO        Unreviewed;       422 AA.
AC   A0A2C9T3J2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Ring-hydroxylating oxygenase subunit alpha {ECO:0000313|EMBL:GAY18607.1};
GN   ORFNames=MSZK_53330 {ECO:0000313|EMBL:GAY18607.1};
OS   Mycobacterium sp. shizuoka-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY18607.1, ECO:0000313|Proteomes:UP000223528};
RN   [1] {ECO:0000313|EMBL:GAY18607.1, ECO:0000313|Proteomes:UP000223528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA   Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA   Hoshino Y.;
RT   "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAY18607.1}.
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DR   EMBL; BEWG01000109; GAY18607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9T3J2; -.
DR   OrthoDB; 5243643at2; -.
DR   Proteomes; UP000223528; Unassembled WGS sequence.
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   CDD; cd08879; RHO_alpha_C_AntDO-like; 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: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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223528}.
FT   DOMAIN          47..145
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   422 AA;  47542 MW;  9C6392D1A8707DCF CRC64;
     MTSVIDPAAG TAGRYDRLIR PDRVHGSMYT DPAIFAEELR KIWYRSWVFV GHESEVARPN
     DYVRKKLGLQ DVIMTRDRDG QIHLLLNRCS HRGNQVCENA KGNSSTFRCP FHGWTFRNTG
     ELIGFPFFKG YGQRQLDMPM GRVPRMDSYR GFVFGSFAPD GPSLREHLGA AAGEIDRLCQ
     LSPDGTVELN AGWLQHQTRA NWKLVVENET DGYHPQFVHG AILGVTQSTI GPLYSDSSTA
     VTRDLGNGHS ENDLRPEFRK FATPMRWFGT TESRVPEYVA AMRARHGEAA EKILIEGAPH
     VMIFPNLFIA EIQVFNLQPV SVAECVQYST AVQLVGAPEL NKRLVSQCLA SVGPAGMLLA
     DDTEMYERNQ QGLEALTPEW LDVRRGLNRE RVDEQGFTIG TNTDETGMRA FWSHYKQLME
     QD
//
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