ID A0A109IJU7_9ACTN Unreviewed; 457 AA.
AC A0A109IJU7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Benzoate/toluate 1,2-dioxygenase alpha subunit {ECO:0000313|EMBL:SCG46066.1};
GN ORFNames=GA0070623_1319 {ECO:0000313|EMBL:SCG46066.1};
OS Micromonospora rifamycinica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG46066.1, ECO:0000313|Proteomes:UP000198226};
RN [1] {ECO:0000313|EMBL:SCG46066.1, ECO:0000313|Proteomes:UP000198226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG46066.1,
RC ECO:0000313|Proteomes:UP000198226};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; LT607752; SCG46066.1; -; Genomic_DNA.
DR RefSeq; WP_067309077.1; NZ_LT607752.1.
DR AlphaFoldDB; A0A109IJU7; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000198226; Chromosome i.
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; cd03469; Rieske_RO_Alpha_N; 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, ECO:0000313|EMBL:SCG46066.1};
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}.
SQ SEQUENCE 457 AA; 50276 MW; D93EFBBF83B84074 CRC64;
MAQQTPVRPL GAAGAMIDED WEALRFRVHR SAYRDPEVFR TEVDRIWNHT WLYLGHETEI
PKPGDFKTRT LGGRPLIFCR DAEGQVRAFF NACTHRGTVL CRHSEGNTKF FQCFYHAWAF
SNSGDLAALP GDDAYPDDPA FRASMALRQV PRLQIHEGFV FVAFDADVPD LLTHLGPAAH
YMSLTAKIGE HGMTTLPGVQ LYSVKGNWKL AVENAMDGYH FAPTHNTFVG YLRETGFAVT
DDDQYAYDLG GGHGLLVLTG HNGRIGMVWE PRFGDEEKTR TVAKRRELEA RLGPELAAEV
ADASRILFVF PNLLLFDLEA LTIRQLEPVA ADRTDVRAWQ FVEVGEPESV RALRIKTMVS
FVGPGGLATP DDIEAYEAVQ RGITATADAV DPAHDWSDMS RGMANEKQGN QGRSIDEGAM
RSFWRRWAEV VGASTSVAGD PPAGTPAAGP ATGGAGK
//
