ID   NAPA_BURXL              Reviewed;         827 AA.
AC   Q13I15;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-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=Bxeno_C0346; ORFNames=Bxe_C0367;
OS   Burkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000272; ABE36274.1; -; Genomic_DNA.
DR   RefSeq; YP_555624.1; -.
DR   SMR; Q13I15; 35-826.
DR   GeneID; 4009881; -.
DR   GenomeReviews; CP000272_GR; Bxeno_C0346.
DR   KEGG; bxe:Bxe_C0367; -.
DR   HOGENOM; Q13I15; -.
DR   OMA; Q13I15; NAYWVQV.
DR   BioCyc; BXEN266265:BXE_C0367-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; 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     32       Tat-type signal (Potential).
FT   CHAIN        33    827       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000256070.
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;  92597 MW;  3B9D6FE05EE4C769 CRC64;
     MTLSRRAFIK QTAAATAASA AGVVLPGVDA LAASDSLTWS KAPCRFCGTG CGVSVGVKNG
     KVVATQGDPQ AEVNRGLNCV KGYFLSKIMY GQDRLTTPLL RMKDGKYAKD GEFAPVSWDQ
     AFDVMADHFK RTLKEKGPTA VGMFGSGQWT VWEGYAAVKL MKAGFRSNNL DPNARHCMAS
     AVTGFMRTFG MDEPMGCYDD IEQADTFVLW GSNMSEMHPI LWTRITDRRL STPTTRVVVL
     STFEHRSFDL ADQTIIFTPQ SDLAILNYIA NYIIRNGNVN RDFVNRHTVF KQGNADIGYG
     LRPDNPLQKT ARNAGDPNGS QPITFDEFAK FVSKYDAAYV TKLSGVPQNK LDQLARLYAD
     PKVKVMSFWT MGFNQHTRGT WANNMVYNLH LLTGKIATPG NSPFSLTGQP SACGTAREVG
     TFSHRLPADM VVTNPKHREE AEHIWKLPAG TIPDKPGYHA VLQNRMLRDG KLNAYWVQVN
     NNVQAAANIN GEALPGYRNP QAFVVVSDVY PTVTAVAADL ILPSAMWVEK EGAYGNAERR
     TQFWHQLVDA PAGARSDLWQ LVEFSKRFKV EEVWPADLLA KKPEYRGKTL YDVLYRNGQV
     DRFALTETDS HYRNDEAKAF GFYIQKGLFE EYASFGRGHG HDLAPFDAYH KARGLRWPVV
     NGKETRWRYK EGSDPYVKTG TGWQFYGNPD GRAVIYALPY EPPPEVPDKE YPFWLATGRV
     LEHWHSGSMT RRVPELYRAF PNAVCFMHPD DAKAMGVRRG VEVKVMSRRG YILTRVETRG
     RDKPPRGLVF VPWFDSSQLI NKVTLDATDP ISLQTDYKKC AVKIVKV
//