ID A0A1I6V3C8_9PSEU Unreviewed; 452 AA.
AC A0A1I6V3C8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Benzoate/toluate 1,2-dioxygenase alpha subunit {ECO:0000313|EMBL:SFT08230.1};
GN ORFNames=SAMN05660874_05558 {ECO:0000313|EMBL:SFT08230.1};
OS Saccharopolyspora flava.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=95161 {ECO:0000313|EMBL:SFT08230.1, ECO:0000313|Proteomes:UP000198852};
RN [1] {ECO:0000313|EMBL:SFT08230.1, ECO:0000313|Proteomes:UP000198852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44771 {ECO:0000313|EMBL:SFT08230.1,
RC ECO:0000313|Proteomes:UP000198852};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOZX01000015; SFT08230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6V3C8; -.
DR STRING; 95161.SAMN05660874_05558; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000198852; 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 CDD; cd03542; Rieske_RO_Alpha_HBDO; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017639; Benzo_1-2-diOase_lsu.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR NCBIfam; TIGR03229; benzo_1_2_benA; 1.
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.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:SFT08230.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 51..148
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 452 AA; 50934 MW; 9A3CA6874574B1F3 CRC64;
MTEMLNHVAA VVADAVVEDR EAGVYRANRR IFTDEEIFEL EMKHIFEGNW IYLAHESQLP
NPGDYFTTYI GRQPVVITRD KDGELHCLIN ACAHRGAMIC RRKADNRSTL TCPFHGWTFR
NDGKLLKVKD PDGAGYPETF DRDGSHDMTK VARFESYRGF LFGSLNPDVV PLAEHLGDTT
TVIDMLVDQS PEGLEVLRGA STYTYDGNWK VQAENGADGY HVTATHWNYA ATTARRGTGE
SKNSTKTLDA GSWGKSGGGY WSYPNGHLCL WTWAGNPQDR PLWPRMDELK QKYGEAKGEF
MVRGSRNLCL YPNVYLMDQF STQIRHFRPI APDKTEVTIY CIAPKGESAE ARAWRIRQYE
DFFNASGMAT PDDLEEFRSC QLTFRATAAP WNDMSRGAEH WLTGPDEVAE ALGMHGVISA
GQKNEDEGLY PVQHGYWQQT MRAAIAAERA AQ
//