ID A0A366H2Q4_9BURK Unreviewed; 420 AA.
AC A0A366H2Q4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Salicylate 5-hydroxylase large subunit {ECO:0000313|EMBL:RBP36213.1};
GN ORFNames=DFR37_11344 {ECO:0000313|EMBL:RBP36213.1};
OS Eoetvoesiella caeni.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Eoetvoesiella.
OX NCBI_TaxID=645616 {ECO:0000313|EMBL:RBP36213.1, ECO:0000313|Proteomes:UP000253628};
RN [1] {ECO:0000313|EMBL:RBP36213.1, ECO:0000313|Proteomes:UP000253628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25520 {ECO:0000313|EMBL:RBP36213.1,
RC ECO:0000313|Proteomes:UP000253628};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
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:RBP36213.1}.
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DR EMBL; QNRQ01000013; RBP36213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366H2Q4; -.
DR OrthoDB; 9790995at2; -.
DR Proteomes; UP000253628; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08880; RHO_alpha_C_ahdA1c-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR043264; AhdA1c-like_alpha_C.
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; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43756:SF5; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000253628}.
FT DOMAIN 46..165
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 420 AA; 48247 MW; CD0250BDD716905B CRC64;
MSDIPVVFPK DPTWREEGTS RIPFWAYTDE DVYKKELERL FYHGHWCYVG LEAEIPNPGD
FKRTLIGERS VILTRDLEGG INVVENVCAH RGMQFCRERH GNKKELVCPY HQWNYSLKGD
LQGVPFLRGV KQNGKVLGGF PKDFKTSENG LNKLKVAVRG GVVFASFDHE VESFEDYIGP
EILGYFDRLF NGRKLTILGY NRQCIPGNWK LMQENIKDPY HPGLLHTWFI TYGLWRADNK
SALRMDDKFR HAAMISTRGN SGNKNEVTSG VTSFKEGMEI QDKRLLDIVH EDWWGEPTAV
MLTIFPSVIF QQQVNSVSTR HIQPNGNGSF DFVWTHFGFE DDTPEMTQRR LVQANLFGPA
GFVSADDGEV IEFSQDGFEQ KPYHRALAEL GGHTAENTEH MVTETLIRGM YDYWRKVMEG
//