ID   NAPA_ACTAC              Reviewed;         828 AA.
AC   Q8VL02;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA;
OS   Actinobacillus actinomycetemcomitans (Haemophilus
OS   actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29523 / Serotype a;
RA   Hu W., Teng Y.-T.A.;
RL   Submitted (NOV-2000) 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; AF321232; AAL55891.1; -; Genomic_DNA.
DR   HSSP; Q53176; 1OGY.
DR   SMR; Q8VL02; 37-826.
DR   BRENDA; 1.7.99.4; 164755.
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; IPR019546; TAT_signal.
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   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; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Molybdenum; Nitrate assimilation; Oxidoreductase; Periplasm; Signal;
KW   Transport.
FT   SIGNAL        1     32       Tat-type signal (Potential).
FT   CHAIN        33    828       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000045975.
FT   METAL        44     44       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        47     47       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        51     51       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        79     79       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   828 AA;  93492 MW;  581F9299D595C87B CRC64;
     MNLSRRDFMK ANAAMAAATA AGLSIPVKNV EAAESEIKWD KAVCRFCGTG CAVLVGTKDG
     RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTQPML RMKDGKYDKN GDFTPVSWDV
     AFKTMAEKFK AAVKELGPNG VGMFSSGQTT IFEGYAKSKL WKAGFRSNNI DPNARHCMAS
     AAVAFMRTFG MDEPMGCYND IEQAEAFVLW GSNMAEMHPI LWSRITDRRL SNQDVKVAVL
     STFEHRSFEL ADYSLIFKPH TDLVILNYII NYLIQNDAIN RDFVNKHTKF KRGETDIGYG
     LRPENPLEQK AKNVKTAGKM YDSNFDELKA LVAEYTLDKA HEMSGVPKDV LENLAKLYAD
     PKKKVVSYWT MGFNQHTRGV WANHLIYNIH LLTGKISIPG CGPFSLTGQP SACGTAREVG
     TFIHRLPADL VVTNPKHREK AEQIWKLPAG VITDVLGFHA VAQSRALKDG KMRVLWQMCT
     NNMQGGPNIN RETFPGWRNP DNFIVVSDPY PTVSCLAADL MLPTAMWVEK EGAYGNAERR
     TQFWRQQVKA PGEAKSDVWQ LVEFSKYFTT DEMWPAEILD KNPEYKGKTL YDVLYRNGQV
     DKFPLSELAE GQLNDESYHF GFYLQKGLFE EYASFGRGHG HDLASFDTYH KARGLRWPVV
     DGKETLWRYR EGYDPYVKEG EGVAFYGYPD KKAIILAVPY EPPAESPDEE YDLWLCTGRV
     LEHWHTGTMT RRVPELHRSF PNNLVWMHPT DAQKRGLRHG DKVKVASRRG EIISFLDTRG
     RNKVPEGLIY TTFFDAGQLA NKLTLDATDP ISKETDFKKC AVKVEKAA
//