SWISSPROT: B2JS74_PARP8

ID   B2JS74_PARP8            Unreviewed;       385 AA.
AC   B2JS74;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   SubName: Full=Oxidoreductase FAD-binding domain protein {ECO:0000313|EMBL:ACC72451.1};
GN   OrderedLocusNames=Bphy_3295 {ECO:0000313|EMBL:ACC72451.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72451.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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DR   EMBL; CP001044; ACC72451.1; -; Genomic_DNA.
DR   RefSeq; WP_012402624.1; NC_010623.1.
DR   STRING; 391038.Bphy_3295; -.
DR   EnsemblBacteria; ACC72451; ACC72451; Bphy_3295.
DR   GeneID; 27742981; -.
DR   KEGG; bph:Bphy_3295; -.
DR   eggNOG; ENOG4105CJJ; Bacteria.
DR   eggNOG; COG1018; LUCA.
DR   HOGENOM; HOG000141051; -.
DR   KO; K21832; -.
DR   OMA; MQVHHIH; -.
DR   OrthoDB; 1885467at2; -.
DR   BioCyc; BPHY391038:G1GBS-3391-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; -; 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   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
DR   PRODOM; B2JS74.
DR   SWISS-2DPAGE; B2JS74.
KW   2Fe-2S {ECO:0000256|SAAS:SAAS00660781};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Iron {ECO:0000256|SAAS:SAAS00909025};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00908250};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00909276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   DOMAIN       31    134       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   DOMAIN      301    385       2Fe-2S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51085}.
SQ   SEQUENCE   385 AA;  42724 MW;  6DAE5636DBEFCFCF CRC64;
     MMRDGAPFEP VESRVTKPEF WSALPARWTS DVEETLVCCQ VRQETHDVKS FFFRSPEGRA
     FVFEPGQFIT LELDIEGETI NRCYTISSPP TRPHTISITV KRVPGGKVSN WLHDNLQAGA
     RVRVLGPAGE FTCARHPARK YLFLSAGSGI TPLMSMSRAH HELSEDRDIV FVHSARTPDD
     IIFPRELDLI ASNQANFRTS FVCERVGART SWPGITGFLT LPLLKLIAPD FMEREVFTCG
     PAPYMKAVRD LLDEAGFDRK QYHEESFSFE TLIEAEPQVA AEVLEAEQKS HADGANGAQT
     FSVSFARSNR SIECGSTQHV LDAARQAGVR LPASCTQGMC GTCKVKLVSG QVDMKHNGGI
     RQREIDQGMV LLCCSKPLSD LVVDK
//