ID   NAPA_PSEMY              Reviewed;         834 AA.
AC   A4XWM0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=Pmen_2981;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C.,
RA   Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP85736.1; -; Genomic_DNA.
DR   RefSeq; YP_001188468.1; -.
DR   GeneID; 5107699; -.
DR   GenomeReviews; CP000680_GR; Pmen_2981.
DR   KEGG; pmy:Pmen_2981; -.
DR   OMA; A4XWM0; NAYWVQV.
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; 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   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     29       Tat-type signal (Potential).
FT   CHAIN        30    834       Periplasmic nitrate reductase.
FT                                /FTId=PRO_5000240716.
FT   METAL        48     48       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        51     51       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        55     55       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        83     83       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   834 AA;  93453 MW;  7C8384E88B6363B1 CRC64;
     MKLSRREFAK ANAAAIAAAA AGLPLASTAS NLITEADMTR LDWNKAPCRF CGTGCSVMVA
     TRDNRVVATH GDVKAEVNRG LNCVKGYFLS KIMYGVDRLT QPLLRMKNGV YDKQGEFQPV
     SWDQAFDIMA QKIKQAIAEQ GPEAVGMFGS GQWTVWEGYA ANKLMKAGFR SNNIDPNARH
     CMASAVMGFM RTFGMDEPMG CYDDIEAADA FVLWGSNMAE MHPILWSRVT DRRLSHPNTR
     VAVLSTFEHR SFDLADIPLV FKPQTDLLIL NYIANHIIES GAVNKDFVGK HTKFARGADD
     IGYGLRADNP LEMQAKNAAK ANTWEDMSFE QFAAFVKPYT LERTAKESGV AAERLKALAK
     LYADPKRKVM SFWTMGFNQH TRGVWANNLI YNLHLLTGKI SEPGNSPFSL TGQPSACGTA
     REVGTFSHRL PADMLVANPK HRETAEKIWK LPPGTIQEKP GFHAVEQSRK LKDGVLKVYW
     TQVSNNMQAG PNVMQEILPG WRNPQAFVIV SDVYPTVSAQ AADLILPSAM WVEKEGAYGN
     AERRTQFWHQ LVKAPGEAKS DLWQLVEFSK RFTTDEVWPA ELLAKAPDYK GKTLYQVLFA
     NGQVDQFPSE QIEAGYANDE AEAFGFYLQK GLFEEYARFG RGHAHDLAPF DSYHAERGLR
     WPVVDGKETR WRYREGHDPY VEKGSGVQFY GYPDKRALIF ALPYEPPAEA PDDEFPFWLS
     TGRVLEHWHT GSMTQRVEEL HGAVPDALVY MHPDDAKALK ARRGSEVKVI SRRGEIRARI
     ETRGRNKPPR GLVFVPFFDA NKLINKVTLD ATDPISKQTD YKKCAVKIEL VSLA
//