ID G9IE59_9BURK Unreviewed; 423 AA.
AC G9IE59;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Salicylate-5-hydroxylase large oxygenase {ECO:0000313|EMBL:AEV91667.1};
GN Name=nagG {ECO:0000313|EMBL:AEV91667.1};
OS Comamonas sp. MQ.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=882490 {ECO:0000313|EMBL:AEV91667.1};
RN [1] {ECO:0000313|EMBL:AEV91667.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MQ {ECO:0000313|EMBL:AEV91667.1};
RX PubMed=24500796; DOI=10.1007/s12010-014-0743-3;
RA Zhang X., Qu Y., Ma Q., Kong C., Zhou H., Cao X., Shen W., Shen E.,
RA Zhou J.;
RT "Production of Indirubin from Tryptophan by Recombinant Escherichia coli
RT Containing Naphthalene Dioxygenase Genes from Comamonas sp. MQ.";
RL Appl. Biochem. Biotechnol. 172:3194-3206(2014).
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 ---------------------------------------------------------------------------
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; JN655512; AEV91667.1; -; Genomic_DNA.
DR AlphaFoldDB; G9IE59; -.
DR SMR; G9IE59; -.
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 CDD; cd03539; Rieske_RO_Alpha_S5H; 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}.
FT DOMAIN 49..168
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 48808 MW; FE55B0A02824CA68 CRC64;
MNEPQRLKPV FPQDPKWPGE GSSRVPFWAY TREDLYKREL ERLFYANHWC YVGLEAEIPN
PGDFKRTVIG ERSVIMVRDP DGGINVVENV CAHRGMRFCR ERHGNAKDFF CPYHQWNYSL
KGDLQGVPFR RGVKQDGKVN GGMPKDFKLE EHGLTKLKVA ARGGAVFASF DHDVEPFEDF
LGPTILHYFD RVFNGRKLKI LGYRRQRIPG NWKLMQENIK DPYHPGLLHT WFSTFGLWRA
DNKSELKMDA KFRHAAMIST RGQGGKNEEV VSGVDSFKEQ MKVNDPRLLD IVPEPWWGGP
TAVMTTIFPS VIIQQQVNSV STRHIQPNGH GSFDFVWTHF GFEDDNEEWT QRRLIQANLF
GPAGFVSADD GEVIEWSQEG FEQKPTHRTV IEMGGHEIGD TDHMVTETLI RGMYDYWRKV
MGE
//
