GenomeNet

Database: UniProt
Entry: A4VJ11
LinkDB: A4VJ11
Original site: A4VJ11 
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   29-OCT-2014, entry version 55.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.7.99.4 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA {ECO:0000255|HAMAP-Rule:MF_01630};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC       acceptor. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- COFACTOR: Binds 1 molybdenum-bis(molybdopterin guanine
CC       dinucleotide) (Mo-bis-MGD) cofactor per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SUBUNIT: Interacts with NapB. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630}.
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       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
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; CP000304; ABP78962.1; -; Genomic_DNA.
DR   RefSeq; WP_011912447.1; NC_009434.1.
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; LVYMHPE; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   BioCyc; PSTU379731:GJER-1268-MONOMER; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-HAMAP.
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_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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; SSF50692; 1.
DR   TIGRFAMs; TIGR01706; NAPA; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
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; Reference proteome; Signal; Transport.
FT   SIGNAL        1     29       Tat-type signal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   CHAIN        30    834       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000069724.
FT   DOMAIN       41     97       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   METAL        48     48       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        51     51       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        55     55       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        83     83       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
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
//
DBGET integrated database retrieval system