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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   31-JAN-2018, entry version 76.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.9.6.1 {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;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H.,
RA   Zhan Y., Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the
RT   genome of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
CC   -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC       complex NapAB. Receives electrons from NapB and catalyzes the
CC       reduction of nitrate to nitrite. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY: 2 ferrocytochrome + nitrate + 2 H(+) = 2
CC       ferricytochrome + nitrite. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
CC       (Mo-bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01630};
CC   -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB
CC       complex composed of NapA and NapB. {ECO:0000255|HAMAP-
CC       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       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
DR   EMBL; CP000304; ABP78962.1; -; Genomic_DNA.
DR   RefSeq; WP_011912447.1; NC_009434.1.
DR   ProteinModelPortal; A4VJ11; -.
DR   SMR; A4VJ11; -.
DR   STRING; 379731.PST_1268; -.
DR   EnsemblBacteria; ABP78962; ABP78962; PST_1268.
DR   KEGG; psa:PST_1268; -.
DR   eggNOG; ENOG4107QIW; Bacteria.
DR   eggNOG; COG0243; LUCA.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; TTDEVWP; -.
DR   OrthoDB; POG091H060P; -.
DR   Proteomes; UP000000233; Chromosome.
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:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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   PANTHER; PTHR11615:SF123; PTHR11615:SF123; 1.
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                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT                                /FTId=PRO_1000069724.
FT   DOMAIN       41     97       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      214    221       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      245    249       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      264    266       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      511    512       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      721    730       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
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}.
FT   BINDING      85     85       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     152    152       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     177    177       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     181    181       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     375    375       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     379    379       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     485    485       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     534    534       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     561    561       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     797    797       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     805    805       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     822    822       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {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
//
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