ID A0A0C1CNU2_9FLAO Unreviewed; 449 AA.
AC A0A0C1CNU2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Benzene 1,2-dioxygenase {ECO:0000313|EMBL:KIA85731.1};
GN ORFNames=OA85_10725 {ECO:0000313|EMBL:KIA85731.1};
OS Flavobacterium sp. AED.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA85731.1, ECO:0000313|Proteomes:UP000031403};
RN [1] {ECO:0000313|EMBL:KIA85731.1, ECO:0000313|Proteomes:UP000031403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AED {ECO:0000313|EMBL:KIA85731.1,
RC ECO:0000313|Proteomes:UP000031403};
RA Gale A.N., Newman J.D.;
RT "Flavobacterium sp. AED Genome.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KIA85731.1}.
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DR EMBL; JSYM01000002; KIA85731.1; -; Genomic_DNA.
DR RefSeq; WP_039109746.1; NZ_JSYM01000002.1.
DR AlphaFoldDB; A0A0C1CNU2; -.
DR STRING; 1423323.OA85_10725; -.
DR OrthoDB; 9800776at2; -.
DR Proteomes; UP000031403; 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 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, ECO:0000313|EMBL:KIA85731.1};
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}.
FT DOMAIN 48..138
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 449 AA; 51611 MW; CA45FDC293B1911B CRC64;
MEKLNKEYVE SLLQHDVAEG LYRHKRESFT NPELFELEMK YIFEKNWIYL AHESQITELN
DYFTTYIGRQ SIFISRNKEG ELNAFINACS HRGAQLCRYK KGNKSTYTCP FHGWTFNNSG
KLLKVKDGKG AGYPEQFNTN GSHDLKKVAR FESYKGFLFG SLNPDSSSLE EYLGDTVKII
DQMVDQSEFG LEVLNGSSTY TYDANWKLQM ENGADGYHVS SVHWNYVATM GNRKEEGVQA
VDPNGWSKSV GGVYGFENGH MLLWTKMLNP EVRPLYSQLD RLNTTLGEEK TNFIINETRN
LAIYPNVYLM DQFSTQIRVL RPIAVDKTEV TIYCFAPKNE PAADRALRLR QYEDFFNVTG
MGTPDDLEEF RSCQESYLSK GMAWNDVSRG AEHWVYGPDE HATAMGINPK LSGNRSEDEG
LFLMQHEYWA DEMKKALNSE ELINLENNL
//
