ID NAPA_PSEU5 Reviewed; 834 AA.
AC A4VJ11;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 46.
DE RecName: Full=Periplasmic nitrate reductase;
DE EC=1.7.99.4;
DE Flags: Precursor;
GN Name=napA; OrderedLocusNames=PST_1268;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RA Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W.,
RA Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D.,
RA Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Complete genome sequence of the metabolically versatile and root-
RT associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501.";
RL Submitted (APR-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; CP000304; ABP78962.1; -; Genomic_DNA.
DR RefSeq; YP_001171804.1; NC_009434.1.
DR ProteinModelPortal; A4VJ11; -.
DR SMR; A4VJ11; 41-829.
DR STRING; 379731.PST_1268; -.
DR EnsemblBacteria; ABP78962; ABP78962; PST_1268.
DR GeneID; 5097354; -.
DR KEGG; psa:PST_1268; -.
DR PATRIC; 19962969; VBIPseStu31643_1270.
DR eggNOG; COG0243; -.
DR HOGENOM; HOG000031441; -.
DR KO; K02567; -.
DR OMA; NAYWVQV; -.
DR ProtClustDB; PRK13532; -.
DR BioCyc; PSTU379731:GJER-1268-MONOMER; -.
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: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 Gene3D; 2.40.40.20; -; 1.
DR HAMAP; MF_01630; Nitrate_reduct; 1; -.
DR InterPro; IPR009010; Asp_de-COase-like_dom.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR TIGRFAMs; TIGR01706; NAPA; 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 30 834 Periplasmic nitrate reductase.
FT /FTId=PRO_1000069724.
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 834 AA; 93752 MW; 7621B1EF0FDE3B4D CRC64;
MSLTRRQFAK ANAAAIAATV AGMPIASTAS NLVTEADATN LKWDKAPCRF CGTGCGVMVA
TRENRVVATH GDVKADVNRG INCVKGYFLS KIMYGTDRLT QPLLRMKDGK FDKQGEFQPV
TWDQAFDIME EKYKAALKAG GPEAIGMFGS GQWTIWEGYA ANKLMKAGFR SNNIDPNARH
CMASAAFGFM RTFGMDEPMG CYEDIEAADA FVLWGSNMAE MHPVLWTRLT DRRLSAPHVK
VAVMSTFEHR SFELADIPMI FNPQTDLVIL NYIANHIIQS GAVNKEFIDK HTRFAKGATN
IGYGLRPTDP LELKAENAAV ANTWTDIGYE DYVEFLKPYT LEHAAKESGV PAERLKALAE
LYADPKVKVM SFWTMGFNQH TRGVWANNMI YNIHLLTGKI SEPGNSPFSL TGQPSACGTA
REVGTFSHRL PADMAVTNPK HRAITEKIWK LPEGTIQEKP GFHAVDQSRK LKDGVLKVYW
TQVTNNMQAG PNVMQEILPG WRNPETFVIV SDVYPTVSAQ AADLILPSAM WVEKEGAYGN
AERRTQFWHQ LVTAPGEARS DLWQLVEFSK RFRVDEVWPA ELLSKAPEFK DKTLFDVLFK
NGQVDRFSND EIAEGYANYE AEAFGFYLQK GLFEEYAEFG RGHAHDLAAF DVYHRERGLR
WPVVDEKETQ WRYREGYDPY VEAGSGVQFY GNADKKAIIF ALPYEVPAEV PDEEYPFWLS
TGRVLEHWHT GSMTQRVDEL HKAVPDALVY MHPEDARKLN VRRGSVVKIV SRRGEMQGRV
ETRGRNKPPM GLVYVPFFDA NKLINKVTLD ATDPISKQTD FKKCAVKIEV VSIA
//
