ID   NAPA_DECAR              Reviewed;         837 AA.
AC   Q47A87;
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=Daro_3515;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
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., Di Bartolo G., Trong S., Kellar K.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
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.
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DR   EMBL; CP000089; AAZ48244.1; -; Genomic_DNA.
DR   RefSeq; YP_286714.1; -.
DR   SMR; Q47A87; 35-836.
DR   GeneID; 3567380; -.
DR   GenomeReviews; CP000089_GR; Daro_3515.
DR   KEGG; dar:Daro_3515; -.
DR   NMPDR; fig|159087.4.peg.2719; -.
DR   HOGENOM; Q47A87; -.
DR   OMA; Q47A87; ERRTQAW.
DR   BioCyc; DARO159087:DARO_3515-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     31       Tat-type signal (Potential).
FT   CHAIN        32    837       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000045983.
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   837 AA;  93395 MW;  E16F8200D0517622 CRC64;
     MKLNRRDFIK ANAAAAAISA AGLSVPGAAV AQGKDEIRWD KAACRFCGTG CGVLVGTQDG
     RVVATQGDPD APVNRGLNCI KGYFLSKIMY GADRLKTPML RMKDGKYDKN GEFTPISWTK
     AFDIMEEKAK ATMKAKGPNG LAMFGSGQWT IWEGYAASKL MKAGFRTNNL DPNARHCMAS
     AVAGFMRTFG IDEPMGCYDD IEHADAFVLW GSNMAEMHPI LWTRITDRKL SNKGVKVAVL
     STFEHRSYEL ADIPMIFTPQ TDLAILNYIA NYIIQNGKVN QAFVDKNVNF KKSATDIGYG
     LRPTHALEKN ATSNGYPDAD GKPKGDTGKS DPITFDEFKK FVSEYTVEKV SKLSGVAEKD
     LKALAELYAD PKVKVISFWT MGFNQHTRGT WANNLCYNIH LLTGKISEPG NSPFSLTGQP
     SACGTAREVG TFSHRLPADM VVTNPEHRKH TEELWGLPEG TIPDKVGYHA VAMARALKDG
     KVNFYWQQCN NNMQAGPNIN EELYPGWRKP ENFIVVSDPY PTVSAMAADL ILPTAMWVEK
     EGAYGNAERR TQFWRQQVKA PGEARSDLWQ LMEFSKRFKV EEVWPAELVA KAPKLKGKTL
     FDVLYANGVV NKYKLNETAA GFDNDDSKLI GFYIQKGLFE EYASFGRGHG HDLAPFDSYH
     QARGLRWPVV GGKETLWRFR EGYDPYVKKG EGVKFYGHKD GKAVIFALPY QPPAESPDKE
     FDMWLSTGRV LEHWHTGTMT RRVPELYKAF PDAVVFMHPD DAKARGLQRG MEVKVASRRG
     EIQLRVETRG RNKPPRGLVF IPFFDAGRLV NKLTLDATCP ISKETDYKKC AVKVTKV
//