ID   NAPA_VIBC3              Reviewed;         829 AA.
AC   A5EZX9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=VC0395_0617;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Heidelberg J.;
RL   Submitted (MAR-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; CP000626; ABQ18717.1; -; Genomic_DNA.
DR   RefSeq; YP_001215456.1; -.
DR   RefSeq; YP_002821704.1; -.
DR   GeneID; 5134168; -.
DR   GeneID; 7777698; -.
DR   GenomeReviews; CP000626_GR; VC0395_0617.
DR   KEGG; vco:VC0395_0617; -.
DR   OMA; A5EZX9; ERRTQAW.
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    829       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000073642.
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   829 AA;  93106 MW;  6B9BEE7A10D99975 CRC64;
     MKMTRRAFVK ANAAASAAAV AGITLPASAT NLIASSDQTA IHWDKAPCRF CGTGCSVLVG
     TQDGRVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGQDRLK TPLLRMKDGQ YHKDGEFTPV
     SWDTAFDVMA EKWKASLKTK GPTSVGMFGS GQWTVMEGYA AVKLMKAGFR SNNIDPNARH
     CMASAVVGFM RTFGIDEPMG CYDDFEHADA FVLWGSNMAE MHPVLWTRIT DRRLSHPHVK
     VNVLSTYYHR SFELADHGYI FHPQSDLAIA NFIANYIIQN DAVNWDFVNK HTHFKQAVTD
     IGYGLRDDHP LQKKAKNANS GDVSDISFEE YKKSVAPYTV EKASEISGVS PDKLITLAKQ
     YADPNTKVMS LWTMGMNQHT RGVWMQSLVY NLHLLTGKIA TPGNSPFSLT GQPSACGTAR
     EVGTFAHRLP ADMVVANPKH RAIAEKVWKL PEGTIPEKPG FHAVQQDRML KDGVLNCYWV
     QCNNNMQAGP NINEERLPGY RNPENFIVVS DAYPTVTAQA ADLVLPTAMW VEKEGAYGNA
     ERRTQVWYQQ VKTVGESHSD SWQVIEFSKR FKVEDVWPEE LLAKAPQYRG KTLYDVLFKN
     GQVDKFPLSE ARELNDDAHH FGFYIQKGLF EEYAEFGRGH GHDLAPYDVY HQVRGLRWPV
     VDGKETKWRF KEGSDPYAKA GSGWDFYGKP DGKAWIISSP YEAPPEMPNE EYDLWLCTGR
     VLEHWHTGTM TRRVPELYKA VPDALCFMHH EDAQARGLRR GDEVLISNSR GEVRVRVETR
     GRNKPPKGLV FVPFFDARIL VNKLILDATD PLSKQTDFKK CPVKITKVA
//