ID   NAPA_VIBVU              Reviewed;         829 AA.
AC   Q8D623;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=VV2_0721;
OS   Vibrio vulnificus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H.,
RA   Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016796; AAO07656.1; -; Genomic_DNA.
DR   RefSeq; NP_762666.1; -.
DR   HSSP; Q53176; 1OGY.
DR   SMR; Q8D623; 41-827.
DR   GeneID; 1180709; -.
DR   GenomeReviews; AE016796_GR; VV2_0721.
DR   KEGG; vvu:VV2_0721; -.
DR   HOGENOM; Q8D623; -.
DR   OMA; Q8D623; ERRTQAW.
DR   BioCyc; VVUL216895:VV2_0721-MON; -.
DR   BRENDA; 1.7.99.4; 277169.
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     30       Tat-type signal (Potential).
FT   CHAIN        31    829       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000046012.
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;  92816 MW;  9AF0DD03181FA6E3 CRC64;
     MKMTRRAFVK ANAAASAAAV AGITLPASAA NLIASSDQTK ITWDKAPCRF CGTGCSVLVG
     TQNGKVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGQDRLT QPLLRMKDGK YDKEGDFTPV
     SWDVAFDTMA EKWKASLAKK GPTSIGMFGS GQWTVMEGYA AAKMMKAGFR SNNIDPNARH
     CMASAVVGFM RTFGIDEPMG CYDDFEHADS FVLWGSNMAE MHPVLWTRIT DRRLSHPHVK
     VNVLSTYYHR SFELADSGYI FKPQSDLAIA NFIANYIIQN DAVNWDFVNK HTNFKQATTD
     IGYGLRDDDP LQKQAKNPNS GNMTSISFEE YKKSVAPYTV EKASEMSGVA QDKLIELAKQ
     YADPNTKVMS LWTMGMNQHT RGVWMNSLVY NIHLLTGKIS TPGNSPFSLT GQPSACGTAR
     EVGTFAHRLP ADMVVANPKH RAIAEKIWKL PEGTIPPKPG FHAVLQDRML HDGVLNCYWV
     QCNNNMQAGP NINGERLPGY RNPENFIVVS DPYPTATAQA ADLILPTAMW IEKEGAYGNA
     ERRTQAWYQQ VGTVGEAKSD LWQVMEFSKR FKMEEVWPEE LLAKAPQYRG KTMYDMLFAN
     GQVDKFPLSE ARQLNDDSHH FGFYVQKGLF EEYAEFGRGH GHDLAPYDVY HTVRGLRWPV
     VDGKETLWRY KEGSDPYAKK GSGWDFYGKP DGKALIISAP YEAPPESPDA EYDMWLCTGR
     VLEHWHTGTM TRRVPELYKA VPDAVCYIHP EDAKARGLRR GDEVLISNKR GEVRVRVETR
     GRNRPPQGLV FVPFFDARIL INKLILDATD PLSKQTDFKK CPVKITKVA
//