(data stored in SCRATCH zone)

SWISSPROT: C3MHF5_SINFN

ID   C3MHF5_SINFN            Unreviewed;       450 AA.
AC   C3MHF5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   SubName: Full=Putative dioxygenase reductase subunit {ECO:0000313|EMBL:ACP24283.1};
GN   OrderedLocusNames=NGR_c04870 {ECO:0000313|EMBL:ACP24283.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24283.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24283.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR   EMBL; CP001389; ACP24283.1; -; Genomic_DNA.
DR   RefSeq; WP_012707068.1; NC_012587.1.
DR   RefSeq; YP_002825036.1; NC_012587.1.
DR   STRING; 394.NGR_c04870; -.
DR   EnsemblBacteria; ACP24283; ACP24283; NGR_c04870.
DR   GeneID; 7791713; -.
DR   KEGG; rhi:NGR_c04870; -.
DR   PATRIC; fig|394.7.peg.3294; -.
DR   eggNOG; ENOG4105CJJ; Bacteria.
DR   eggNOG; COG1018; LUCA.
DR   HOGENOM; HOG000141051; -.
DR   OMA; MQVHHIH; -.
DR   OrthoDB; POG091H03GC; -.
DR   Proteomes; UP000001054; Chromosome.
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:0009055; F:electron carrier 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   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR008333; OxRdtase_FAD-bd_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR001221; Phe_hydroxylase.
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   PRINTS; PR00410; PHEHYDRXLASE.
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; C3MHF5.
DR   SWISS-2DPAGE; C3MHF5.
KW   2Fe-2S {ECO:0000256|SAAS:SAAS00436776};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Dioxygenase {ECO:0000313|EMBL:ACP24283.1};
KW   Iron {ECO:0000256|SAAS:SAAS00437297};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00437807};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00438843};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00706734};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN      104    207       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   DOMAIN      366    450       2Fe-2S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51085}.
SQ   SEQUENCE   450 AA;  48743 MW;  A0C8F1D201889C0A CRC64;
     MACQQGCGRG CRLYARGSDA CLDRDQRPGP PDRRGKRIRH PFAGLSAGAL FGGTRGGRHA
     VRRLVFALHA GSPAGQRRSS VAGGMTMEMA RSFHHFDELH PWIDRQHLLE CTSVVAETAD
     VMTFTFRSDR PAWFRYLPGQ FVTLELPTGE EPVMRTYTLS STPSRPLSVA VTVKAQSNSI
     GTRWMFDNLK PGMVLKALGP LGDFSFVRHP GEKYLFISAG SGITPMMSMT RWMADCAPAT
     DVTFVSCARQ PEDLLFKSEL EILARQMPHL NLGFLVEGHE ARHGWHGLRG RIDATKLPLL
     APDVLERTVF CCGPEPFMRG VRDMLKGAGF DMARYHQESF QPAAAPAAEE LAIRAGPATG
     AGAEAARVTF TMSGKDVSAV PGQTILQTAR ANGVRIGAAC EGGICGTCRV LKIAGDVAMN
     HNGGILDDEI DEGYILACCS RPLGDVQIEA
//

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