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 01-MAY-2013, entry version 78.
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: Molybdenum (molybdopterin) (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.
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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 OMA; FENDGQR; -.
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:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:EC.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.40.40.20; -; 1.
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_Fe4S4_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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; Asp_decarb_fold; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
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 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
//
