ID   NAPA_PSEA7              Reviewed;         834 AA.
AC   A6V924;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=PSPA7_4205;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000744; ABR83935.1; -; Genomic_DNA.
DR   RefSeq; YP_001349559.1; -.
DR   GeneID; 5355582; -.
DR   GenomeReviews; CP000744_GR; PSPA7_4205.
DR   KEGG; pap:PSPA7_4205; -.
DR   OMA; A6V924; 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_1000069722.
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;  93510 MW;  0CAA2E0F04CE8707 CRC64;
     MNLTRREFAK ANAAAIAAAA AGLPILVRAS NLVTEADVTS LDWNKAPCRF CGTGCSVMVA
     TRDGQVVATH GDIKAEVNRG INCVKGYFLS KIMYGSDRLT RPLLRMKDGK FDKQGEFQPI
     SWEQAFDIMA EKFKAALKAK GPESVGMFGS GQWTVWEGYA ANKLFKAGLR SNNIDPNARH
     CMASAVMGFM RSFGMDEPMG CYDDIEATDS FVLWGSNMAE MHPVLWSRVT DRRLSAPQVK
     VAVLSTFEHR SFELADIPMV FKPQTDLIIL NYIANHIIES GAVNRDFVER HVRFAHGAED
     IGYGLRPDDP LEKKAKNADK ANTWSDIDFN AFAEFVKPYT LERAARESGV PAERLKALAE
     LYAAPRRKVV SFWTMGFNQH TRGVWANNLI YNIHLLTGKI SEPGNSPFSL TGQPSACGTA
     REVGTFSHRL PADLVVTNPK HRETAEKIWK VPAGTIQEKV GFHAVQQSRM LKDGVLNVYW
     TQVSNNMQAG PNVMQEVLPG WRNPDNFVIV SDVYPTVSAQ AADLILPSAM WVEKEGAFGN
     AERRTQFWHQ LVKAPGEAKS DLWQLVEFSK RFTTDEVWPA ELLAKAPELK GKTLYEVLFR
     NGQVDRFPAS DLAKGYANDE VDAFGFYIQK GLFEEYAAFG RGHGHDLAPF DAYHEARGLR
     WPVVDGKETR WRYREGYDPY VSKGSGVQFY GYPDKKAIVF ALPYEPPAEA PDRDYPFWLA
     TGRVLEHWHT GSMTARVPEL YKAVPDAVVY MHPDDARQLK LRRGSEVRVV SRRGEIRARV
     ETRGRNKPPQ GLVFVPFFDA NKLINKVTLD ATDPISKQTD YKKCAVRIEL LNLA
//