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Database: UniProt
Entry: Q57M92
LinkDB: Q57M92
Original site: Q57M92 
ID   NAPA_SALCH              Reviewed;         828 AA.
AC   Q57M92;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   14-MAY-2014, entry version 65.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=SCH_2264;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y.,
RA   Wang H.-S., Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a
RT   highly invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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-bis(molybdopterin guanine
CC       dinucleotide) (Mo-bis-MGD) cofactor 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.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
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DR   EMBL; AE017220; AAX66170.1; -; Genomic_DNA.
DR   RefSeq; YP_217251.1; NC_006905.1.
DR   ProteinModelPortal; Q57M92; -.
DR   SMR; Q57M92; 1-35, 37-827.
DR   STRING; 321314.SC2264; -.
DR   PRIDE; Q57M92; -.
DR   EnsemblBacteria; AAX66170; AAX66170; SCH_2264.
DR   PATRIC; 32325491; VBISalEnt136302_2723.
DR   eggNOG; COG0243; -.
DR   OMA; AGKMHDS; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   BioCyc; SENT321314:GJCS-2366-MONOMER; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-HAMAP.
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_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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; SSF50692; 1.
DR   TIGRFAMs; TIGR01706; NAPA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
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_0000045999.
FT   DOMAIN       39     95       4Fe-4S Mo/W bis-MGD-type.
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;  92874 MW;  0CF99BC8B2509A85 CRC64;
     MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ
     QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP MLRMKDGSYH KDGEFTPVSW
     EQAFDVMEEK FKTSLKEKGP EAIGMFGSGQ WTIWEGYAAA KLFKAGFRSN NIDPNARHCM
     ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGSNMAEMH PILWSRITNR RLSDPNVKVA
     VLSTFQHRSF ELADNGIVFT PQSDLVILNY IANYIIQNNA VNQDFFTKHV NLRKGATDIG
     YGLRPTHPLE KAAKNPGSDA SEPMSFDEYK AFVAEYTLDK TAEMTGVPKD QLEQLAQLYA
     DPNKRVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV
     GTFSHRLPAD MVVTNEKHRD ICEKHWQIPA GTIPAKVGLH AVAQDRALKD GKLNVYWVMC
     NNNMQAGPNI NEDRMPGWRD PRNFIIVSDP YPTVSALSAD LILPTAMWVE KEGAYGNAER
     RTQFWRQQIK APGEAKSDLW QLVQFSRRFK TEEVWPEALL AQKPELRGKT LYDVLFATPA
     VSKFPLSELK EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HNARGLRWPV
     VEGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAESPDN EYDLWLSTGR
     VLEHWHTGSM TRRVPELHRA FPEAVVFIHP LDAKARDLRR GDKVKVSSRR GEVISIVETR
     GRNRPPQGLV YMPFFDAAQL VNNLTLDATD PLSKETDFKK CAVKLAKV
//
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