(data stored in SCRATCH zone)

SWISSPROT: C3MF54_SINFN

ID   C3MF54_SINFN            Unreviewed;       474 AA.
AC   C3MF54;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   SubName: Full=Predicted mercuric reductase {ECO:0000313|EMBL:ACP23891.1};
GN   OrderedLocusNames=NGR_c00870 {ECO:0000313|EMBL:ACP23891.1};
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:ACP23891.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23891.1, 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).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; CP001389; ACP23891.1; -; Genomic_DNA.
DR   RefSeq; WP_012706676.1; NC_012587.1.
DR   RefSeq; YP_002824644.1; NC_012587.1.
DR   STRING; 394.NGR_c00870; -.
DR   EnsemblBacteria; ACP23891; ACP23891; NGR_c00870.
DR   GeneID; 7790666; -.
DR   KEGG; rhi:NGR_c00870; -.
DR   PATRIC; fig|394.7.peg.2880; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276709; -.
DR   OMA; VIPWTTF; -.
DR   OrthoDB; 267896at2; -.
DR   BioCyc; SFRE394:GBYN-87-MONOMER; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MF54.
DR   SWISS-2DPAGE; C3MF54.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        8    321       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      342    449       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     141    143       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     178    185       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING      53     53       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     201    201       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     267    267       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     307    307       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     44     49       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   474 AA;  50495 MW;  A1B391FECC7B2389 CRC64;
     MGEIRNPDIC VIGGGAAGLS VAAGAAAFGV PVVLVERGRM GGDCLNYGCV PSKALIAAAR
     QAQAMRQAGA FGLVAAEPFI DGERLQARIR SVIEGIAAHD SVERFSGLGV EVIQETARFL
     DDRTVAAGTY LIRARRFVIA TGSSPAVPPI AGLAEVPYLT NESLFEFTPL PRHLVVVGAG
     PFGLEMAQAH CRLGARVTVV ERADALSKED TELKAIVLDA IRTEGTALHE RTTIRSIERD
     GDGVRLHCVD KKGGFDIEGS DLLLATGRTG NHAALDLGAA GIRHDAERIH VGADLRTSNR
     RVYAIGDAAG GLQFTHAANY HARLVLQQIL FRLPGRETRK IVPRVTFTDP EIAQVGATEE
     EARASFGTVE VVRSDLSGSD RARTDGLDRG MIKIVVGRGG RILGAGIAGA AAGEMINLWA
     FAIANRLTLK NFRDYVAPYP TLSEIGKQAA ISYYSPMVRN RFVRSAIGIL RRFG
//

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