ID   NAPA_SHEDO              Reviewed;         829 AA.
AC   Q12P44;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=Sden_1497;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) 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; CP000302; ABE54782.1; -; Genomic_DNA.
DR   RefSeq; YP_562505.1; -.
DR   SMR; Q12P44; 39-828.
DR   GeneID; 4017266; -.
DR   GenomeReviews; CP000302_GR; Sden_1497.
DR   KEGG; sdn:Sden_1497; -.
DR   NMPDR; fig|318161.14.peg.1462; -.
DR   HOGENOM; Q12P44; -.
DR   OMA; Q12P44; NAYWVQV.
DR   BioCyc; SDEN318161:SDEN_1497-MON; -.
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     27       Tat-type signal (Potential).
FT   CHAIN        28    829       Periplasmic nitrate reductase.
FT                                /FTId=PRO_5000114527.
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   829 AA;  93039 MW;  F452E7CAE302C02F CRC64;
     MNRRDFMKAN AVIAAASAAG LALPAGASNL ITSSEQTKLE WNKAPCRFCG TGCSVMVATR
     EGKVVATHGD ANSEVNRGLS CIKGYFLSKI MYGRDRLTSP MLRMTDGKYD KHGEFTPVSW
     EKAFDTMAER WKATIKEKGP TAVGMFGSGQ WTVWEGYAAV KLMKAGFGTN NIDPNARHCM
     ASAVAGFMRT FGIDEPMGCY DDMEAADAFV LWGSNMAEMH PILWTRVTDR RLSAPHVKVA
     VLSTFEHRSF DLADLPMVFH PQTDLAILNF IANYIIQNNK VNWDFVNKHV NFRKGTTDIG
     YGLRPAHPTQ MKSKNAATAN DSTPIDFEQF KKFVADYDVE SVSKLSGVPE HKLLELAELY
     ADPKVKVTSF WTMGFNQHTR GVWCNNLMYN IHLLVGKIST PGNSPFSLTG QPSACGTARE
     VGTFSHRLPA DMVVTDPKHR KIAENIWKIP SGIIPEKPGY HAVEQSRRLK DGDLNCYWVQ
     VNNNMQAGPN INEEGLPGYR NPANFIVVSD AYPTVTTQAA DLILPTAMWV EKEGAYGNAE
     RRTQFWHQMV KAPGESKSDL WQLMEFSKRF TTDEVWSKAV LDANPKYKGK TLFEVLFKNG
     QVDKFPLADA DPKYMNDEND AFGFYVQKGL FEEYATFGRG HGHDLADFDT YHKEHGLRWP
     VVDGKETKWR FREGSDPYVK AGTGFEFYGK PDGRAVIFAL PYEPAAEAPD EEFDMWLSTG
     RVLEHWHSGS MTQRVPELYK AFPDAVCFMH PDDAKKRGLR RGDEVKVMSR RGEIKTRIET
     RGRNKPPVGL VFVPWFDASQ LINKVTLDAT DPISKQTDFK KCAVKVIKA
//