ID   NAPA_DINSH              Reviewed;         831 AA.
AC   A8LLY9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-NOV-2008, entry version 12.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=Dshi_3165;
OS   Dinoroseobacter shibae (strain DFL 12).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
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., Thompson L.S., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Dinoroseobacter shibae DFL 12.";
RL   Submitted (SEP-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; CP000830; ABV94898.1; -; Genomic_DNA.
DR   RefSeq; YP_001534499.1; -.
DR   GeneID; 5712221; -.
DR   GenomeReviews; CP000830_GR; Dshi_3165.
DR   KEGG; dsh:Dshi_3165; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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:InterPro.
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   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     35       Tat-type signal (Potential).
FT   CHAIN        36    831       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000335805.
FT   METAL        49     49       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        52     52       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        56     56       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        84     84       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   831 AA;  92890 MW;  0D8369C67278F4D9 CRC64;
     MTISDSRRTF LKASAAAATA SAAGIPLANG TAAEAQAIST GIRWDKAACR FCGTGCSVLV
     GTKEGRVVAT QGDPDAPVNR GLNCIKGYFL SKIMYGEDRL TMPLLRKTNG VYDKNGTFEP
     VSWDEAFDVM AQKWKEALAK KGPTSVGMFG SGQWTVWEGY AAAKLMKAGF RSNNIDPNAR
     HCMASAVVGF MRTFGIDEPM GCYDDFEHAD TFVLWGSNMA EMHPILWSRL TDTRLTKPGS
     EVHVLSTYEH RSFELADNGM VFAPQTDLAI LNYIANYIIS TGRVNEDFMS KHVNITKTAT
     DIGYGLRDEH ALQQEAENPN SGKLEPISFD EYAASVAEYT VDKVSELSGV PAAQLEKLAE
     QYADPNRKVM SLWTMGFNQH TRGSWVNSLM YNVHLLVGKI SEPGNSPFSL TGQPSACGTA
     REVGTFAHRL PADMVVMNDA HRALTEKKWN LPEGTIPAKP GFHAVLQHRK LKDGDLNAYW
     VQCNNNMQAA PNMNEEGYPG YRNPENFITV SDPYPTVTTM SADLILPTAM WVEKEGAYGN
     AERRTQFWRQ QVKAPGEAKS DLWQLMEFSK RFTIEEVWGE ELLAKMPEHR GKTMYDVLFA
     NGKVDKYPLS ETAEGFDNDE SEHFGYYVQK GLFEEYAGFG RGKAHDLASF ETYHQSRGLR
     WPVVDGQETL YRFREGYDPY VPEGEGVRFY GHSDGKAKII YAPYEPAPEV PDAEFDLWLC
     TGRVLEHWHS GSMTRRVPEL HRAYPAAVVY MHPEDAKARG LRRGQEINIS TRRGDMLSRV
     ETRGRNKVPQ GLVFVPWFDE GQLINQLTLD ATCPLSKETD FKKCACKVER A
//