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Database: UniProt
Entry: X7F4T8_9RHOB
LinkDB: X7F4T8_9RHOB
Original site: X7F4T8_9RHOB 
ID   X7F4T8_9RHOB            Unreviewed;       357 AA.
AC   X7F4T8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Dioxygenase {ECO:0000313|EMBL:ETX27932.1};
GN   ORFNames=RISW2_10710 {ECO:0000313|EMBL:ETX27932.1};
OS   Roseivivax isoporae LMG 25204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX27932.1, ECO:0000313|Proteomes:UP000023430};
RN   [1] {ECO:0000313|EMBL:ETX27932.1, ECO:0000313|Proteomes:UP000023430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX27932.1,
RC   ECO:0000313|Proteomes:UP000023430};
RA   Lai Q., Li G., Shao Z.;
RT   "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ETX27932.1}.
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DR   EMBL; JAME01000025; ETX27932.1; -; Genomic_DNA.
DR   AlphaFoldDB; X7F4T8; -.
DR   STRING; 1449351.RISW2_10710; -.
DR   PATRIC; fig|1449351.3.peg.3198; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000023430; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06215; FNR_iron_sulfur_binding_1; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Dioxygenase {ECO:0000313|EMBL:ETX27932.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:ETX27932.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023430}.
FT   DOMAIN          10..116
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          273..357
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   357 AA;  39079 MW;  2E30632DD8614920 CRC64;
     MIPMPKEDAP VWTDAEVLEC VLVVPEAPNV KTFVFRPPSG ARFWFRAGQF ITLDLPVPGG
     NVQRTYTISS SPTTSAFITV TVKAQKDSIG TRWMLDHLEP GMRIKAYGPA GLFHLPPQPD
     GSYLFISAGS GVTPMMSMAS FLWERGEDPD IAFVHCAQSP QNIIFRHKLE YMASRVSGLK
     LHFVVEQDDP YTVWTGYRGR FNSLMLGLMA PDYLDRDVYC CGPEGFMEAV REMLISLGYD
     MSRYHQESFS APAESKAELT EFDDLVPDDT AQSEVVFARA GVTASCFETD TVLGVAKAAG
     LNIPSGCTFG LCGTCKIRKT AGEVHMVHNG GISEDDIAAG YILACCSNPI GRVEVEV
//
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