ID   NAPA_RHOPB              Reviewed;         837 AA.
AC   Q21AR4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=RPC_0952;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) 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.
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DR   EMBL; CP000301; ABD86522.1; -; Genomic_DNA.
DR   RefSeq; YP_530841.1; -.
DR   SMR; Q21AR4; 44-833.
DR   GeneID; 3969715; -.
DR   GenomeReviews; CP000301_GR; RPC_0952.
DR   KEGG; rpc:RPC_0952; -.
DR   HOGENOM; Q21AR4; -.
DR   OMA; Q21AR4; NAYWVQV.
DR   BioCyc; RPAL316056:RPC_0952-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     33       Tat-type signal (Potential).
FT   CHAIN        34    837       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000256075.
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   837 AA;  93633 MW;  CA1EB7B6C1D9B06F CRC64;
     MTTPKLDRRQ VLKLEAAAMA ALAGGIAMPA AAANLVTERA VSELKWDKAA CRFCGTGCSV
     MVATKENRVV ATHGDTKSEV NRGLNCVKGY FLSKIMYGHD RLTQPMLRKT DGKYDKNGEF
     MPVSWDEAFD IMAEKFKAAL KKRGPSGVGM FGSGQWTVWE GYAASKLFKA GFRSNNIDPN
     ARHCMASAVA GFMRTFGIDE PMGCYDDIEA ADVFVLWGSN MAEMHPLLWT RVTDRRLSAP
     HVKVAVLSTF EHRSFDLADL GLVFKPQTDL AILNAIANHI IKTGRVNKDF VAKHTTFKRG
     QTDIGYGLRP EHPLQKAATG AAKANDATDM SFEDYAAFVA DYTIEKASQI SGVPAAKIEA
     LAELYADPNT KVTSFWTMGF NQHTRGVWAN NLAYNLHLLT GKISEPGNSP FSLTGQPSAC
     GTAREVGTFS HRLPADMVVT NKKHRDIAEK IWKLPEGTIP DKPGYHAVLQ SRMLKDGLLN
     AYWVQVNNNL QAGANANEET YPGFRNPDNF IVVSDAYPSV TALAADLILP TAMWVEKEGA
     YGNAERRTQF WHQLVSAPGQ ARSDLWQLME FAKRFKIEEV WTEELLAKKP EVRGKTMYDV
     LYRNGQVDKY PSSDIEAGYL NDESKAFGYY VQKGLFEEYA SFGRGHGHDL APFDDYHRER
     GLRWPVVNGQ ETRWRFREGS DPYVQQGAGV QFYGFPDGRA RIFALPYEPA AEAPDAEFPF
     WLSTGRVLEH WHSGTMTRRV PELYKAFPEA VCFMHPDDAA ELKLRRGDEI KVESRRGFIR
     TRVETRGRNK PPRGLVFVPW FDEAQLINKV TLDATDPISL QTDYKKCAVR IERVTAS
//