ID   NAPA_RALEH              Reviewed;         831 AA.
AC   P39185; Q7WXC3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   25-NOV-2008, entry version 75.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=PHG211;
OS   Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
OS   (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier
OS   337)).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-50.
RX   MEDLINE=93388517; PubMed=8376334;
RA   Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B.,
RA   Kostka S., Friedrich B.;
RT   "Structure and function of a periplasmic nitrate reductase in
RT   Alcaligenes eutrophus H16.";
RL   J. Bacteriol. 175:5867-5876(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22830147; PubMed=12948488; DOI=10.1016/S0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B.,
RA   Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16
RT   megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and
RT   anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
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.
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.
CC   -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups
CC       per subunit.
CC   -!- SUBUNIT: Interacts with napB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: Expressed independently of nitrate induction and
CC       anaerobiosis.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has 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; X71385; CAA50507.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP85963.1; -; Genomic_DNA.
DR   PIR; A48489; A48489.
DR   RefSeq; NP_942849.1; -.
DR   HSSP; P81186; 2NAP.
DR   SMR; P39185; 41-830.
DR   GeneID; 2656653; -.
DR   GenomeReviews; AY305378_GR; PHG211.
DR   KEGG; reh:PHG211; -.
DR   HOGENOM; P39185; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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:InterPro.
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   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   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW   Nitrate assimilation; Oxidoreductase; Periplasm; Plasmid; Signal;
KW   Transport.
FT   SIGNAL        1     29       Tat-type signal.
FT   CHAIN        30    831       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000019168.
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).
FT   CONFLICT    146    151       GMFGSG -> ACSAPA (in Ref. 1; CAA50507).
SQ   SEQUENCE   831 AA;  93346 MW;  34CE1CDE6677C42F CRC64;
     MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA
     VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT RPLMRMKNGK YDKNGDFAPV
     TWDQAFDEME RQFKRVLKEK GPTAVGMFGS GQWTVWEGYA AAKLYKAGFR SNNIDPNARH
     CMASAAAGFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR
     VVVLSTFTHR CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD
     IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV PKAKLDQLAE
     LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI ATPGNSPFSL TGQPSACGTA
     REVGTFSHRL PADMVVTNPK HREEAERIWK LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW
     VQVNNNMQAA ANLMEEGLPG YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN
     AERRTQFWHQ LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR
     NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF DAYHEARGLR
     WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF ALPYEPPAES PDKEYPYWLV
     TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF MHPEDAKALG LRRGVEVEVV SRRGRMRSRI
     ETRGRDAPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD FKKCAVKIVK V
//