ID A0A0H1AJ00_9GAMM Unreviewed; 452 AA.
AC A0A0H1AJ00;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Benzene 1,2-dioxygenase {ECO:0000313|EMBL:KLI99263.1};
GN ORFNames=WQ56_12725 {ECO:0000313|EMBL:KLI99263.1};
OS Luteimonas sp. FCS-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLI99263.1, ECO:0000313|Proteomes:UP000035397};
RN [1] {ECO:0000313|EMBL:KLI99263.1, ECO:0000313|Proteomes:UP000035397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLI99263.1,
RC ECO:0000313|Proteomes:UP000035397};
RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Luteimonas oceanisediminis
RT sp. nov., a novel gammaproteobacteria isolated from a marine sediment.";
RL Submitted (APR-2015) 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:KLI99263.1}.
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DR EMBL; LASZ01000015; KLI99263.1; -; Genomic_DNA.
DR RefSeq; WP_047137505.1; NZ_LASZ01000015.1.
DR AlphaFoldDB; A0A0H1AJ00; -.
DR STRING; 1547516.WQ56_12725; -.
DR PATRIC; fig|1547516.3.peg.2667; -.
DR OrthoDB; 9769355at2; -.
DR Proteomes; UP000035397; 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 CDD; cd03542; Rieske_RO_Alpha_HBDO; 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; 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.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:KLI99263.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035397}.
FT DOMAIN 54..135
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 452 AA; 51194 MW; 9050A8CCAF892604 CRC64;
MSAIVDKATE LDLLLANAVQ DDKEAGVFRC RRDIFTNADL FELEMKHIFE RNWVYLAHES
QLPENNDYYT TYIGRQPVVV TRDKAGELHA VINACAHKGA MLCRRKHGNK GSFTCPFHGW
TFSNAGKLLK VKDEKTTQYP EQFNTNGSHD LKRVARFQNY RGFLFGSLNP DVVPLEDFLG
ETRVIIDQIV DQAPNGLEVL RGNSSYIYEG NWKLQMENGC DGYHVSSVHW NYLATMGRRK
EEGTKAVDAN SWSKSVAGVY GFDNGHILLW TNTRNPEVRP VYGQREEIAA RVGEERAGFI
VNQTRNLCLY PNVFLMDQFS TQIRVTRPIS VDQTEISIFC FAPKGESAAD RTLRLRQYED
FFNVSGMGTA DDLEEFRACQ NGYAASAAPW NDMSRGAPLW IDGPDENARR MGIAPLLSGE
RSEDEGLFVR QHAYWVQTMR DALARERAAV AA
//