GenomeNet

Database: UniProt
Entry: O33732
LinkDB: O33732
Original site: O33732 
ID   NARB_SHEFN              Reviewed;         938 AA.
AC   O33732; Q084F9;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   19-FEB-2014, entry version 83.
DE   RecName: Full=Nitrate reductase;
DE            EC=1.7.99.4;
GN   OrderedLocusNames=Sfri_1505;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA   Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA   Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-397.
RX   PubMed=10861223; DOI=10.1042/0264-6021:3490153;
RA   Gordon E.H.J., Pike A.D., Hill A.E., Cuthbertson P.M., Chapman S.K.,
RA   Reid G.A.;
RT   "Identification and characterization of a novel cytochrome c3 from
RT   Shewanella frigidimarina that is involved in Fe(III) respiration.";
RL   Biochem. J. 349:153-158(2000).
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first
CC       step of nitrate assimilation in plants, fungi and bacteria.
CC   -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC       acceptor.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
CC   -!- COFACTOR: Binds 1 molybdenum-bis(molybdopterin guanine
CC       dinucleotide) (Mo-bis-MGD) cofactor per subunit (By similarity).
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000447; ABI71356.1; -; Genomic_DNA.
DR   EMBL; AJ000006; CAA03851.1; -; Genomic_DNA.
DR   RefSeq; YP_750194.1; NC_008345.1.
DR   ProteinModelPortal; O33732; -.
DR   STRING; 318167.Sfri_1505; -.
DR   EnsemblBacteria; ABI71356; ABI71356; Sfri_1505.
DR   GeneID; 4277460; -.
DR   KEGG; sfr:Sfri_1505; -.
DR   PATRIC; 23496939; VBISheFri14343_1562.
DR   eggNOG; COG0243; -.
DR   HOGENOM; HOG000031440; -.
DR   KO; K00372; -.
DR   OMA; SMPRADR; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   ProtClustDB; CLSK958261; -.
DR   BioCyc; SFRI318167:GIXS-1564-MONOMER; -.
DR   UniPathway; UPA00653; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR009010; Asp_de-COase-like_dom.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    938       Nitrate reductase.
FT                                /FTId=PRO_0000063236.
FT   DOMAIN        1     64       4Fe-4S Mo/W bis-MGD-type.
FT   METAL         8      8       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        11     11       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        15     15       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        50     50       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   938 AA;  101087 MW;  C8951CAC0306A663 CRC64;
     MSVVQSSCAY CGVGCGVSVS SNKPNWTDVD AADLILVGDN KHPANYGHLC AKGERLLDSL
     AQPNVLRYPK LRSGMPLDWD KASTLIADTF AKTIAEHGPD SVALYLSGQL LTEDYYVANK
     FAKGFLKTAN VDTNSRLCMS SAVSAMQRAF GEDVVPGCYD DLEQADVIVL VGANTAWTHP
     VLFQRILAAI KANNAQLVVI DPLSTATAKQ ADLHLAIKPG ADLTLFHGLL GYLADQNRVD
     HAYIAAHTEG FDTVVLQAQQ LSANLADLAT QVGVSVTQLT QFYQLVANNK KVLTASCQGV
     NQSTIGTDAT NAMINCHLAL GHIGQAGCGF FSLTGQPNAM GGREVGGLAT QLACHMGFSQ
     PEQQLLADFW KVDSIADQKG LVAVEMFDAL AEGKIKAIWI MGTNPVVSLP NSEKIAQALA
     DCPFVVVSEI SPDSDTAKLA DVLLPAQGWS EKCGTVTNSE RTITRQRGFI TAKGQAKPDW
     WAVSQVAKKM GFDGFEFDDN ASIFSEFAAL SAKVKQVFPT KVFDLTGLTE LSKAQYDALA
     PTQWPIASAT QIGQQNVRVF GLGEFATATG KAQFVTPAVV SVPQQSLPSN TLLLNTGRSR
     DQWHTMTRTG HIASLRASIP EPVVHLHSSQ LSALSLTEGG LVRIEAIQNQ IEQYSTETAN
     PDLFTHASFT MARAVVDDDI PTNMALMSMH WSAQFSLTKG VNQALDARVD PISKQPGFKC
     QPVTLTPVEL ALQGVVFGQH YSSAHGLCWQ VAQTLENGVC HHIGFTDTDD GFAYQATVHS
     LKWTLTVVGQ PLYIQCNMDK GLLKALKVLS HTQVNVALYQ MNDFIGKPVD KQLIKQLHQQ
     IKAGNSPLIC ACTGVTEANI NDEINQQFND QVMSDGLANI SFEQALDSTQ LLLGCGRQCG
     SCHSEVKQCA KQSWKDALSY CESYSDIDHQ PSVAEDVA
//
DBGET integrated database retrieval system