ID   NAPA_SHEON              Reviewed;         826 AA.
AC   Q8EIJ1;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=SO_0848;
OS   Shewanella oneidensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=70863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   MEDLINE=22297686; PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
RA   Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA   Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA   White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA   Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA   Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN53924.1; -; Genomic_DNA.
DR   RefSeq; NP_716479.1; -.
DR   HSSP; Q53176; 1OGY.
DR   SMR; Q8EIJ1; 38-825.
DR   GeneID; 1168695; -.
DR   GenomeReviews; AE014299_GR; SO_0848.
DR   KEGG; son:SO_0848; -.
DR   NMPDR; fig|211586.1.peg.788; -.
DR   TIGR; SO_0848; -.
DR   HOGENOM; Q8EIJ1; -.
DR   OMA; Q8EIJ1; NMLYNIH.
DR   BioCyc; SONE211586:SO_0848-MON; -.
DR   BRENDA; 1.7.99.4; 257422.
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:UniProtKB-KW.
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   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01630; -; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006657; MPT_dinuc_bd.
DR   InterPro; IPR010051; NO3_reductase_lsu_periplasm.
DR   InterPro; IPR006311; Tat.
DR   InterPro; IPR019546; TAT_signal.
DR   InterPro; IPR017909; Twin_arg_translocation_Tat.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   TIGRFAMs; TIGR01706; NAPA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; FALSE_NEG.
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     32       Tat-type signal (Potential).
FT   CHAIN        33    826       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000046003.
FT   METAL        45     45       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        48     48       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        52     52       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        80     80       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   826 AA;  92475 MW;  33474D23868F6316 CRC64;
     MSISRREFLK ANAAVAAATA VGVTLPVKMV EAAESDNIKW DKAPCRFCGV GCSVLVGTKA
     GKVVATKGDP ESPVNRGLNC IKGYFLSKIM YGKDRLTTPL LRMKDGKYHK EGEFTPVSWD
     VAFDTMAAKW KHSIATKGPT SVGMFGSGQW TIWEGYAASK LHKAGFLTNN IDPNARHCMA
     SAVVGFMRTF GIDEPMGCYD DLEAADHFVL WGANMAEMHP ILWARLSDRR LSSKDCRVHV
     LSTFENRSFD LADNPMVFHP QSDLVILNYI ANYIIQNKAV NTDFVTKHTK FALGVDDIGY
     GLRPDHPLEK KAKNPGNGKS TPISFDEYAK FVSTYTLEYA AKMSGVEPEK LETLAKAYAD
     PKAKVMSLWT MGINQHVRGV WANNMLYNIH LLTGKIATPG NSPFSLTGQP SACGTAREVG
     TFAHRLPADM VVDNDKHRAI TEKMWQVPEG TIPPKPGYHA VLQSRMLKDG KLNCYWTMCT
     NNMQAGPNIN EEMYPGFRNP ENFIVVSDPY PTVTAMAADL ILPTAMWVEK EGAYGNAERR
     THMWHQQVKA PEGAKSDLWQ LVEFSKRFKV AEVWPAELIA KKPEYADKTL YEVLFANGVI
     NKFPTTDCKG DLNDESEHFS FYVQKGIFEE YAAFGRGHGH DLAEFDRYHE TRGLRWPVVN
     DKETLRRFVE GSDPYVKAGE GYNFYGKPDG KAVIFALPYE PAAEEPNSEY DLWMSTGRVL
     EHWHTGSMTA RVPELYRAYP DAQIFMHPED AKARGLQRGD EVLVASPRGE IKTRVETKGR
     NKPPRGVVFM PFFDARQLVN KLILDATDPL SKETDFKKCP VKVMKA
//