ID   NAPA_SHEHH              Reviewed;         826 AA.
AC   B0TSW5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=Shal_0715;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ75290.1; -; Genomic_DNA.
DR   RefSeq; YP_001672949.1; -.
DR   GeneID; 5906601; -.
DR   GenomeReviews; CP000931_GR; Shal_0715.
DR   KEGG; shl:Shal_0715; -.
DR   OMA; B0TSW5; 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     32       Tat-type signal (Potential).
FT   CHAIN        33    826       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000088120.
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   826 AA;  92339 MW;  40B787D80A241A78 CRC64;
     MSISRREFLK ANAAVAAATA VGATLPVKIV EAAEQKDNIK WDKAPCRFCG VGCSVLVGTD
     NGKVVATKGD PESPVNKGLN CIKGYFLSKI MYGKDRLTTP LLRMKDGQYD KEGEFTPISW
     DSAFDIMADK WKDTLKTKGP TAVGMFGSGQ WTVWEGYAAS KLHKAGFLTN NIDPNARHCM
     ASAVGGFMRT FGIDEPMGCY DDLEAADQFV LWGANMAEMH PILWARLSDR RLSSPTSRVH
     VLSTYENRSF DLADNAMVFR PQSDLVILNY VANYIIQNDA VNKDFVNKHT KFALGTTDIG
     YGLRPDHPLE KKAKNPGNGK SKPISFDEYA KFVSSYTLEY AAEMSGVEPE KLELMAKAYA
     DPNVKMMSLW TMGINQHTRG VWANNMLYNI HLLTGKIATP GNSPFSLTGQ PSACGTAREV
     GTFAHRLPAD MVVANPKHRE ITEKLWQVPA GTIPPKPGFH AVLQSRMLKD GKLNCYWTMC
     TNNMQAGPNI NDEMYPGFRN PENFIVVSDP YPTVTAMAAD LILPTAMWVE KEGAYGNAER
     RTHMWHQQVK APEGAKSDLW QLMEFSKRFK VSEVWPAELI AKQPELADKT LFDVLYANGV
     VDKFPSSECK GQYNDEADAF GFYVQKGLFE EYAQFGRGHA HDLADFDTYH ETRGLRWPVV
     DGKETLRRFS KGDPYVKGDK EFDFYGKPDG KAVIFALPFE PAAEEPNEEY DIWLSTGRVL
     EHWHTGSMTA RVPELYRAYP DAQIFMHPED AKARGLKRGD EVIVASPRGE VKTRVETKGR
     NKPPRGVAFM PFFDARQLVN KLILDATDPL SKETDFKKCP VKVMKA
//