ID   NAPA_BRASB              Reviewed;         834 AA.
AC   A5ED21;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=BBta_1862;
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=288000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S.,
RA   Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L.,
RA   Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P.,
RA   Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A.,
RA   Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic
RT   bradyrhizobia.";
RL   Science 316:1307-1312(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; CP000494; ABQ34065.1; -; Genomic_DNA.
DR   RefSeq; YP_001237971.1; -.
DR   GeneID; 5154592; -.
DR   GenomeReviews; CP000494_GR; BBta_1862.
DR   KEGG; bbt:BBta_1862; -.
DR   OMA; A5ED21; NAYWVQV.
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    834       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000069709.
FT   METAL        51     51       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        54     54       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        58     58       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        86     86       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   834 AA;  93602 MW;  2A73E0590EF976FB CRC64;
     MTDMKIDRRQ MLKLEAAAIA AAAAGMPSTS LAANLVTERE ASELKWDKAA CRFCGTGCSV
     MVATKDNRVV ATHGDIKAEV NRGLNCVKGY FLSKIMYGHD RLTHPMLRKT NGKYDKNGEF
     TPVSWDEAFD IMALKFKDAL KKRGPSGVGM FGSGQWTIWE GYAASKLFKA GFRTNNIDPN
     ARHCMASAVA GMMRTFGIDE PAGCYDDIEA ADAFVLWGSN MAEMHPILWT RVTDRRLSAP
     HVKVAVLSTF EHRSFDLADI GMVFKPQTDL YLLNAIANHI IKTGRVNKDF VQAHTVFKKG
     QTDIGYGLRP EHPLQKKATG AAKANDATDI SFDEYAKFVS DYTLEKAAEM SGVPLNRLEA
     LAELYADPKT KVVSFWTMGF NQHTRGVWCN NLVYNIHLLT GKIAEAGNSP FSLTGQPSAC
     GTAREVGTFS HRLPADMVVT NKEHRTKAEH IWQLPEGTIP DKPGYHAVLQ SRMLKDGLLN
     AYWVQVNNNL QAGPNANEET YPGFRNPDNF IVVSDAYPSV TALAADLILP TAMWVEKEGA
     YGNAERRTQF WHQLVSAPGE ARSDLWQLME FSKRFKIEEV WPEELIAKKP DVRGKTLFDV
     LYKNGQVDKF PLDQIEAGYA NDESKAFGFY VHKGLFEEYA AFGRGHGHDL APFEAYHKER
     GLRWPVVDGK ETRWRFREGS DPYVKAGTGV QFYGFPDGKA RIFALPYEPP AESPDKDYPF
     WLSTGRVVEH WHSGTMTRRV PELYKAFPEA VCFMHPDDAQ EANLRRGDEV KVASRRGFIR
     ARVETRGRDK PPRGLVFVPW FDESKLINKV TLDATDPISL QTDYKKCAVR IERV
//