ID   NAPA_AERHH              Reviewed;         829 AA.
AC   A0KIM1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=AHA_1586;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK35881.1; -; Genomic_DNA.
DR   RefSeq; YP_856122.1; -.
DR   SMR; A0KIM1; 40-828.
DR   GeneID; 4486851; -.
DR   GenomeReviews; CP000462_GR; AHA_1586.
DR   KEGG; aha:AHA_1586; -.
DR   TIGR; AHA_1586; -.
DR   OMA; A0KIM1; KAGLRTN.
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; 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; IPR019546; TAT_signal.
DR   InterPro; IPR017909; Twin_arg_translocation_Tat.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10518; TAT_signal; 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_1000069707.
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;  92843 MW;  CA3A2CB2674ED4BE CRC64;
     MKLSRRDFMK ANAVAAAAAV AGVSAPTLAA NLITSTDKTA ITWDKAPCRF CGTGCSVLVG
     SQDGRVVATQ GDPDAPVNRG LNCIKGYFLS KIMYGQDRLT QPMLRMTDGK FDKNGNFAPI
     SWDQAFDIMA EKFKTTLKEK GPTAVGMFGS GQWTVWEGYA AAKLMKAGLR TNNLDPNARH
     CMASAVVGFM RTFGMDEPMG CYDDIEQADA FVLWGSNMAE MHPILWSRIS DRRLSHQDVQ
     VHVLSTFEHR SFELADNGMV FTPQTDLAIL NYIANYIIQN DKVNWEFVNK HTQFRKGVTD
     IGYGLRPTNP LQQKAKNPDS GDSTPMSFDD FAKFVADYDL ESVSKLSGVP KDKLEKLAQL
     YADPSKKVVS YWTMGFNQHT RGVWANNLCY NIHLLTGKIS TPGSGPFSLT GQPSACGTAR
     EVGTFAHRLP ADMVVTEPKH RAIAEKIWKL PEGTIPEQVG YHAVLQNRML KDGKLNAYWV
     MCNNNMQAGP NMNEEGLPGY RNPANFIVVS DPYPTVTAQA ADLILPTAMW VEKEGAYGNA
     ERRTQFWHQQ VKPPEGAKSD LWQLMEFSKR FKVEEVWPAE LIAKMPEVKG KTLFDVLYAN
     GQVNQFPKEQ SKGALNDEAE HFGFYVQKGL FEEYATFGRG HGHDLAPFDQ YHEARGLRWP
     VVDGKETLWR YREGFDPYVK AGEGVRFYGK PDGKAVIFAL PYEPAAEAPD KEYDMWLSTG
     RVLEHWHTGT MTRRVPELYR AFPDAVLFMH PEDAKARGVR RGEEVIVSSR RGEVKTRVET
     RGRNRPPKGL VFMPFFDASQ LVNKLTLDAT DPLSKETDYK KCAVKVVKA
//