ID   NAPA_YERE8              Reviewed;         831 AA.
AC   A1JL26;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=YE1156;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the
RT   high pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL11250.1; -; Genomic_DNA.
DR   RefSeq; YP_001005483.1; -.
DR   SMR; A1JL26; 39-828.
DR   GeneID; 4712672; -.
DR   GenomeReviews; AM286415_GR; YE1156.
DR   KEGG; yen:YE1156; -.
DR   NMPDR; fig|630.2.peg.1132; -.
DR   OMA; A1JL26; NMLYNIH.
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; 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    831       Periplasmic nitrate reductase.
FT                                /FTId=PRO_5000201017.
FT   METAL        47     47       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        50     50       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        54     54       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        82     82       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   831 AA;  93407 MW;  C7CFFE972D7248D0 CRC64;
     MKLSRRDFMK ANAAVAAAAA AGLTIPTVAK AVVGETTNAI KWDKAPCRFC GTGCGVLVGT
     QNGRIVASQG DPDSPVNRGL NCVKGYFLPK IMYGKDRLTQ PLLRMKDGQY DKEGDFTPIS
     WEKAFDIMEL KFKNALKEKG PTAVGMFGSG QWTVWEGYAA SKLLKAGFRS NNLDPNARHC
     MASSVVGFMR TFGMDEPMGC YDDIEEADAF VLWGSNMAEM HPILWSRMTS RRLTNEHVRI
     AVLSTFEHRS FELADNPIVF TPQTDLVIMN YIANYIIQNN AVDQGFLDRH VNFRRGATDI
     GYGLRPTHPL EKAAKNPGSD ASEPMSFDDF KAFVAEYTLE KTAKMSGVPE DQLESLAQLY
     ADPKVKLVSY WTMGFNQHTR GVWANNMCYN LHLLTGKISK PGSGPFSLTG QPSACGTARE
     VGTFSHRLPA DMVVTNEKHR QIAETKWQLP AGTIPEKVGL HAVAQDRALK DGTLNAYWVM
     CNNNMQAGPN INEERMPGWR DPRNFIVVSD PYPTISALAA DLILPTAMWV EKEGAYGNAE
     RRTQFWRQQV PAPGEAKSDL WQMVEFAKRF KVEEVWPDEL INKKPEYRGK TLYDVLFANN
     VVNKYPLSEI PADQLNDEAR DFGFYIQKGL FEEYADFGRG HGHDLAPFDR YHQERGLRWP
     VVNGKETLWR YREGFDPFVP KGEDVRFYGK PDGKAVIFAL PYEPAAESPD QEYDLWLSTG
     RVLEHWHTGS MTRRVPELHR AFPEAVLFIH PLDAKARGLR RGDKVKVISR RGEVISLVET
     RGRNRPPQGL VYMPFFDAAQ LVNNLTLDAT DPLSKETDFK KCAVKLARVV A
//