ID   NAPA_RALEJ              Reviewed;         831 AA.
AC   Q46RX3;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=Reut_B4763;
OS   Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000091; AAZ64111.1; -; Genomic_DNA.
DR   RefSeq; YP_298955.1; -.
DR   SMR; Q46RX3; 41-830.
DR   GeneID; 3613319; -.
DR   GenomeReviews; CP000091_GR; Reut_B4763.
DR   KEGG; reu:Reut_B4763; -.
DR   NMPDR; fig|264198.3.peg.5696; -.
DR   HOGENOM; Q46RX3; -.
DR   OMA; Q46RX3; NAYWVQV.
DR   BioCyc; REUT264198:REUT_B4763-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     29       Tat-type signal (Potential).
FT   CHAIN        30    831       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000045997.
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   831 AA;  93762 MW;  D0F5A7BEF139884A CRC64;
     MKVSRRDFIK QTAIAATASV AGIPLGTEAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA
     VRDNKVVATQ GDPQCEVNKG LNCVKGYFLS KIMYGQDRLT KPLLRMKNGK YDKNGEFAPV
     TWDQAFDEME RQFKRVLKEK GPTAVGMFGS GQWTVWEGYA ASKLYKAGFR SNNIDPNARH
     CMASAVQGFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRIT DRRLSHPKTR
     VAVLSTFTHR SFDLADIPII FTPQTDLAML NYIANYIIQN NKVNKDFVNK HTVFKEGVTE
     IGYGLRPDHP LQKAAKNAAN PGDSKPITFD DFAKFVSKYD ADYVSKLSGV PKDKLRQLAE
     LYADPNVKVM SLWTMGFNQH TRGSWVNNMV YNVHLLTGKI ATPGNSPFSL TGQPSACGTA
     REVGTFSHRL PADMVVTNPK HREEAERIWK LPPGTIVEKP GYHAVLQNRM LRDGKLNAYW
     VQVNNNMQAA ANIMEEALPG YRNPANFIVV SDAYPTVTAL SADLILPSAM WVEKEGAYGN
     AERRTQFWHQ LVDAPGDARS DLWQLMEFSK RFKVEEVWPA ELVAKKPEYK GKTLFDVLYR
     NGQVDKFPIK EVSTEYHNAE AQAFGFYVQK GLFEEYASFG RGHGHDLAPF DRYHEERGLR
     WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF ALPYEPPPES PDKEYPFWLA
     TGRVLEHWHS GSMTRRVPEL YRAFPNAVVF MHPEDAKAMG LRRGVEVEVV SRRGRMRSRV
     ETRGRDAPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD YKKCAVKIVK V
//