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Database: UniProt
Entry: A0A1H4HWI4_9BURK
LinkDB: A0A1H4HWI4_9BURK
Original site: A0A1H4HWI4_9BURK 
ID   A0A1H4HWI4_9BURK        Unreviewed;       454 AA.
AC   A0A1H4HWI4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Benzoate/toluate 1,2-dioxygenase alpha subunit {ECO:0000313|EMBL:SEB25890.1};
GN   ORFNames=SAMN05444680_12812 {ECO:0000313|EMBL:SEB25890.1};
OS   Variovorax sp. YR216.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882828 {ECO:0000313|EMBL:SEB25890.1, ECO:0000313|Proteomes:UP000199122};
RN   [1] {ECO:0000313|Proteomes:UP000199122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR216 {ECO:0000313|Proteomes:UP000199122};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNRO01000028; SEB25890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4HWI4; -.
DR   STRING; 1882828.SAMN05444680_12812; -.
DR   OrthoDB; 9790995at2; -.
DR   Proteomes; UP000199122; 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; 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:SEB25890.1};
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          56..152
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   454 AA;  51194 MW;  2B95792C649EBCC6 CRC64;
     MNTTATTDKY GDVEQLLDSA LQDDKDAGVF RCRRDIFTDP ALFELEMKHI FESNWVYLAH
     ESQIPEINDY FTTTIGRQPI VITRSKDGKL NAVINACAHR GAMLCRKKHG NKGSFTCPFH
     GWTFNNGGKL LKVKDEKTSE YPVQFNKEGS HDLKKVARFE SYKGFLFGSL NADVQSLDDY
     LGETKVIIDQ IVDQAPDGLE VLRGNSSYTY DGNWKLQMEN GSDGYHVSSV HWNYAATMGR
     RADGGTKAVD AAGWSKSVGG VYGFENGHIL LWTKTMNPEV RPVYSRRDEL KERLGETKAE
     FIVSQTRNLC LYPNVYLMDQ FSTQIRVTRP ISVDKTEITI YCFAPKGESA EDRAVRIRQY
     EDFFNVSGMG TADDLEEFRS CQTGYAGKAA PWNDLSRGAP LWVEGPDENA KKMGMKPLIS
     GERSEDEGLF VCQHDYWAKA MRKGVKQERE GAQA
//
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