ID   NAPA_VIBHB              Reviewed;         829 AA.
AC   A7N7J3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=VIBHAR_05377;
OS   Vibrio harveyi (strain ATCC BAA-1116 / BB120).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=338187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N.,
RA   Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C.,
RA   Irgon J., Wilson R.K.;
RL   Submitted (AUG-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; CP000790; ABU73282.1; -; Genomic_DNA.
DR   RefSeq; YP_001447509.1; -.
DR   GeneID; 5557405; -.
DR   GenomeReviews; CP000790_GR; VIBHAR_05377.
DR   KEGG; vha:VIBHAR_05377; -.
DR   NMPDR; fig|338187.4.peg.3153; -.
DR   OMA; A7N7J3; 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_1000069726.
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;  93061 MW;  EEA20FAF8A4AF69E CRC64;
     MKMTRRAFVK ANAAASAAAV AGITLPASAT NLIASSDQTK ITWDKAPCRF CGTGCSVLVG
     TQNGKVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGQDRLT KPLLRMKDGK YSKDGDFAPV
     SWDTAFDIMA EKWKASLEKK GPTSIGMFGS GQWTVMEGYA AAKMMKAGFR SNNIDPNARH
     CMASAVVGFM RAFGIDEPMG CYDDFENADA FVLWGSNMAE MHPVLWTRIT DRRLSHPHVK
     VNVLSTYYHR SFELADHGYI FNPQSDLAIA NFIANYIIEN DAVNWDFVNK HTNFTQADTD
     IGYGLRDDDP LQKAAKNPNS GKLTSISFEE YKKSVAPYTV EKASEISGVE KEKLIELAKQ
     YADPNTKVMS LWTMGMNQHT RGVWMNNLIY NIHLLTGKIA TPGNSPFSLT GQPSACGTAR
     EVGTFAHRLP ADMVVANPKH RKIAEDIWKL PEGTIPPKPG FHAVLQDRML HDGVLNCYWV
     QCNNNMQAGP NINTERLPGY RNPENFIVVS DPYPTATAQA ADLVLPTAMW IEKEGAYGNA
     ERRTQAWYQQ VETIGDAKSD LWQVMEFAKR FKMEEVWPEE LLAKAPEYRG KTMYDMLFKN
     GQVDKFPIEE AREMNDDAHH FGYYVQKGLF EEYATFGRGH GHDLAPYDVY HTVRGLRWPV
     VDGKETQWRF KEGSDPYAKA GSGWDFYGNA DGKAKIISAP YEAPPEVPNE EFDLWLCTGR
     VLEHWHTGTM TRRVPELYKA VPDAVVYMHP ADAKKRNVRR GEEVLIANKR GEVRVRVETR
     GRNRPPEGLV FVPFFDARIL INKLILDATD PLSKQTDFKK CPVKITKIA
//