ID A0A1W9JRK1_9PROT Unreviewed; 450 AA.
AC A0A1W9JRK1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Benzoate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:OQW74537.1};
GN ORFNames=BVN33_07660 {ECO:0000313|EMBL:OQW74537.1};
OS Proteobacteria bacterium ST_bin13.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978761 {ECO:0000313|EMBL:OQW74537.1, ECO:0000313|Proteomes:UP000192661};
RN [1] {ECO:0000313|EMBL:OQW74537.1, ECO:0000313|Proteomes:UP000192661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin13 {ECO:0000313|EMBL:OQW74537.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW74537.1}.
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DR EMBL; MSXQ01000010; OQW74537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9JRK1; -.
DR Proteomes; UP000192661; 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};
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..121
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 450 AA; 50564 MW; ABADCFD391F1BE10 CRC64;
MNHPLRDRIE TAVVDDPESG QFRCRRDIFT DPALFDLEMK HIFERNWVYL AHESQVANAN
DFFTSWIGRV PVVLIRQKSG TLDAFVNACS HRGAKLCRRR RGNQPLLVCP FHGWSFKTDG
SLLRAKDAST GAYPATFAQD GSHDLTRVAR FESYRGFLFG SMDPEAGPLE EYLGETRVVI
DQIVDQAPES LEILPGNSTY IFDGNWKLQM ENGCDGYHVS SVHANYSATM ARRADGGTKA
VDANGWSKAV SGVYGFEHGH ILLWTRVLNP EVRPIWSQRA GLEERLGKER TEFIVSQSRN
LALYPNVFLM DQFSTQIRVV RPISASQTEV TIYCFAPKGE SAENRATRIR QYEDFFNVSG
MGTPDDLEEF RACQSAYEGA GALWNDLSRG ALRWIAGPDE NARAMGMNPL LSSERSEDEG
LFVRQHEYWA KAMLAGLDRD ARAALPEAAE
//
