ID NAPA_SHIB3 Reviewed; 828 AA.
AC B2TV30;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=Periplasmic nitrate reductase;
DE EC=1.7.99.4;
DE Flags: Precursor;
GN Name=napA; OrderedLocusNames=SbBS512_E0735;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC (NAP). Only expressed at high levels during aerobic growth. NapAB
CC complex receives electrons from the membrane-anchored tetraheme
CC protein NapC, thus allowing electron flow between membrane and
CC periplasm. Essential function for nitrate assimilation and may
CC have a role in anaerobic metabolism (By similarity).
CC -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC acceptor.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC -!- COFACTOR: Binds 1 molybdenum ion per subunit (By similarity).
CC -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups
CC per subunit (By similarity).
CC -!- SUBUNIT: Interacts with NapB (By similarity).
CC -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC -!- PTM: Predicted to be exported by the Tat system. The position of
CC the signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
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DR EMBL; CP001063; ACD08569.1; -; Genomic_DNA.
DR RefSeq; YP_001879449.1; NC_010658.1.
DR ProteinModelPortal; B2TV30; -.
DR STRING; 344609.SbBS512_E0735; -.
DR EnsemblBacteria; ACD08569; ACD08569; SbBS512_E0735.
DR GeneID; 6272060; -.
DR KEGG; sbc:SbBS512_E0735; -.
DR PATRIC; 18668045; VBIShiBoy129590_0823.
DR eggNOG; COG0243; -.
DR HOGENOM; HOG000031441; -.
DR KO; K02567; -.
DR OMA; HWIKAAR; -.
DR ProtClustDB; PRK13532; -.
DR BioCyc; SBOY344609:GI0O-2912-MONOMER; -.
DR GO; GO:0042597; C:periplasmic space; 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:HAMAP.
DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:HAMAP.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:HAMAP.
DR GO; GO:0042128; P:nitrate assimilation; IEA:HAMAP.
DR Gene3D; 2.40.40.20; -; 1.
DR HAMAP; MF_01630; Nitrate_reduct; 1; -.
DR InterPro; IPR009010; Asp_de-COase-like_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 InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
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 TIGRFAMs; TIGR01706; NAPA; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW Periplasm; Signal; Transport.
FT SIGNAL 1 31 Tat-type signal (Potential).
FT CHAIN 32 828 Periplasmic nitrate reductase.
FT /FTId=PRO_1000186376.
FT METAL 46 46 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 49 49 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 53 53 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 81 81 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 828 AA; 93058 MW; 93ADF88D083C8796 CRC64;
MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ
QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKNGKYD KEGEFTLITW
DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ WTIWEGYAAS KLFKAGFRSN NIDPNARHCM
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGANMAEMH PILWSRITNR RLSNQNVTVA
VLSTYQHRSF ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG
YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD QLEQLAQLYA
DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV
GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS GTIPAKIGLH AVAQDRALKD GKLNVYWTMC
TNNMQAGPNI NEERMPGWRD PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER
RTQFWRQQVQ APGEAKSDLW QLVQFSRRFK TEEVWPEDLL AKKPELRGKT LYEVLYATPE
VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HKARGLRWPV
VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAEAPDE EYDLWLSTGR
VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARDLRR GDKVKVVSRR GEVISIVETR
GRNRPPQGLV YMPFFDAAQL VNKLTLDATD PLSKETDFKK CAVKLEKV
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