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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//