ID   NAPA_HAES1              Reviewed;         827 AA.
AC   Q0I5G9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=HS_1508;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17172329; DOI=10.1128/JB.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni)
RT   strain 129Pt and comparison to Haemophilus ducreyi 35000HP and
RT   Haemophilus influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI25781.1; -; Genomic_DNA.
DR   RefSeq; YP_719718.1; -.
DR   SMR; Q0I5G9; 36-826.
DR   GeneID; 4241028; -.
DR   GenomeReviews; CP000436_GR; HS_1508.
DR   KEGG; hso:HS_1508; -.
DR   NMPDR; fig|205914.1.peg.689; -.
DR   HOGENOM; Q0I5G9; -.
DR   OMA; Q0I5G9; ERRTQAW.
DR   BioCyc; HSOM205914:HS_1508-MON; -.
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; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW   Periplasm; Signal; Transport.
FT   SIGNAL        1     32       Tat-type signal (Potential).
FT   CHAIN        33    827       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000069720.
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   827 AA;  93016 MW;  19DCB138A81CCC7E CRC64;
     MNLSRRDFMK ANAALAAASV AGLIIPVKNV NAADTSITWD KAVCRFCGTG CAVLVGTKDG
     RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTHPML RMKNGQYDKE GEFTPVTWDF
     AFKTMAEKFK SALKAKGPNG VGMFTSGQST IFEGVAKSKL FKAGLLSNNI DPNARHCMAS
     AAVAFVRTFG IDEPMGCYDD IEHADAFVLW GSNMAEMHPI LWSRISDRRL ANPDTVSVNV
     LSTFEHRSFE LADLGILLKP QSDLAILNYI ANYLIENNAI NREFIEKHTK FKRGETDIGY
     GLRPQDPREQ IAKNVKTAGK MYDSSFEEFK KLVAPYTLEK AHEISGVPKE QLEKLAKLYA
     DPNKKVVSYW TMGINQHTRG VWANHLIYNI HLLTGKISLP GCGPFSLTGQ PSACGTAREV
     GTFIHRLPAD LVVTKPEHRK IAEKIWKLPE GLISDKLGFH AVAQSRALKD GKMQVLWQMC
     NNNMQAGPNI NEETYPGWRN PDNFIVVSDP YPTVSALSAD LILPTAMWVE KEGAYGNAER
     RTQFWRQQVK APGEAKSDLW QLVEFSKYFT TDEVWPAEIL AKNPAYQGKT LYEVLYLNGQ
     VNQYSNDELK GRLNDEAYHF GFYIQKGLFE EYASFGRGHG HDLADFDTYH KARGLRWPVV
     DGKETLWRYR EGYDPYVKAG EGVSFYGQAD KRAVILAVPY EPPAEVPDRE YDLWLTTGRI
     LEHWHTGSMT RRVPELHRSF PNNLVWMNPN DAKKRGLKHG DKIKVISRRG EITSYIDTRG
     RNKCPEGLIY TTFFDAGQLA NKLILDATDP ISKETDFKKC AVKVVKA
//