(data stored in SCRATCH zone)

SWISSPROT: C3MHF0_SINFN

ID   C3MHF0_SINFN            Unreviewed;       476 AA.
AC   C3MHF0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ACP24278.1};
GN   OrderedLocusNames=NGR_c04820 {ECO:0000313|EMBL:ACP24278.1};
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:ACP24278.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24278.1, 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; ACP24278.1; -; Genomic_DNA.
DR   RefSeq; WP_012707063.1; NC_012587.1.
DR   RefSeq; YP_002825031.1; NC_012587.1.
DR   STRING; 394.NGR_c04820; -.
DR   EnsemblBacteria; ACP24278; ACP24278; NGR_c04820.
DR   GeneID; 7791708; -.
DR   KEGG; rhi:NGR_c04820; -.
DR   PATRIC; fig|394.7.peg.3290; -.
DR   eggNOG; ENOG4105CQB; Bacteria.
DR   eggNOG; COG0277; LUCA.
DR   HOGENOM; HOG000230997; -.
DR   OMA; VYEWTAR; -.
DR   OrthoDB; POG091H02HQ; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; C3MHF0.
DR   SWISS-2DPAGE; C3MHF0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN       40    221       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   476 AA;  50559 MW;  13BA1933ACEB02BD CRC64;
     MTAIPSPELI ASFADIVGPG HALTAPAETA PYLVESRGLY HGTTPLVLKP GSVDEVSRIL
     QLASRTQTAI VPQGGNTGHV AGQIPREGKA DVALSLERLN RIRDIDPVGN VIVADAGCIL
     ADIQKAADDV DRLFPLSLGS EGSARIGGNL STNAGGTAVL AYGNTRQLCL GLEVVLPTGE
     VWDGLRRLKK DNTGYDLRDL FIGAEGTLGV ITGAVLKLFP KPRGHQVAFA GLASVDAALS
     LFDRASSLCG PALTGFELMP RLGIEFTTRH IPGVRDPMET SHPWYALIDI SSSDSAESAE
     RMVQGLLEAG IDDGLVENAV IAQSEAQRKA LWHLRESMSP AQKPEGGSIK HDVSVPVSSI
     PAFMADADAA VMTAIPDARI CAFGHMGDGN IHYNISQPIG ADSQAFLARW REVNAIVHAI
     VLKYNGSISA EHGIGQLKRD ELAAIRSPIE IELMRRIKHA FDPAGIMNPD KVLRQD
//

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