GenomeNet

Database: UniProt
Entry: Q6LTV9
LinkDB: Q6LTV9
Original site: Q6LTV9 
ID   NAPA1_PHOPR             Reviewed;         828 AA.
AC   Q6LTV9;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   01-OCT-2014, entry version 71.
DE   RecName: Full=Periplasmic nitrate reductase 1 {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.7.99.4 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA1 {ECO:0000255|HAMAP-Rule:MF_01630};
GN   OrderedLocusNames=PBPRA0853;
OS   Photobacterium profundum (Photobacterium sp. (strain SS9)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=74109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N.,
RA   Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N.,
RA   Romualdi C., Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and
RT   expression analysis.";
RL   Science 307:1459-1461(2005).
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; CR378665; CAG19266.1; -; Genomic_DNA.
DR   RefSeq; YP_129068.1; NC_006370.1.
DR   ProteinModelPortal; Q6LTV9; -.
DR   SMR; Q6LTV9; 41-827.
DR   STRING; 298386.PBPRA0853; -.
DR   EnsemblBacteria; CAG19266; CAG19266; PBPRA0853.
DR   GeneID; 3123080; -.
DR   KEGG; ppr:PBPRA0853; -.
DR   PATRIC; 22932429; VBIPhoPro109272_0936.
DR   eggNOG; COG0243; -.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; EYRGKTM; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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     30       Tat-type signal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   CHAIN        31    828       Periplasmic nitrate reductase 1.
FT                                /FTId=PRO_0000045993.
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   828 AA;  93366 MW;  58C80D6AE7BC8A63 CRC64;
     MKMTRRAFVK ANAAASAAAV AGITLPASAA NLIVSSDETK IKWDKAPCRF CGTGCSVLVG
     TQNGRVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGKDRLQ TPMLRMKNGE YNKEGDFAPV
     SWDQAFDVMA EKFKKALKEK GPTSVGMFGS GQWTVMEGYA ASKMMKAGFR SNNIDPNARH
     CMASAVGGFM RTFGIDEPMG CYDDFEHADS FVLWGSNMAE MHPVLWTRIT DRRLSHPHVK
     VNVLSTYYHR SFELADNGMI FEPQTDLAIA NFIANYIIQN DAVNWDFVTK HTHFKRAETD
     IGYGLRDDNP LQMKAKHPNS GALHPMDFEQ YKASVAEYTV EKASQMSGVS EEKLIEMAKQ
     YADPKVKVMS LWTMGMNQHT RGVWMNSLVY NIHLLTGKIS QPGNSPFSLT GQPSACGTAR
     EVGTFSHRLP ADMVVANPKH RAIAEKIWKL PDGTIPAKPG YHAVQQDRML KDGKLNAYWV
     MCNNNMQAGP NINEERLPGY RNPENFIVCS DPYPTVTAQA SDLILPTAMW VEKEGAYGNA
     ERRTQAWYQQ VKSQGDSKSD LWQLMEFSKR FKIEEVWGED LLAQMPEYRG KTMYEVLFRN
     GQVDKFPLSE AQELNDDAKA QGFYLQKGLF EEYAAFGRGH GHDLAPYDVY HQVRGLRWPV
     VDGKETLWRF VEGSDPYVPE GEGFRFYGKP DGKANIIFAP FEPAPEEPDQ EYDMWLCTGR
     VLEHWHTGTM TRRVPELYKA VPDALCFIHP DDAQKRGLRR GDEVLLESRR GEVRCRVETR
     GRNRPPVGLV FVPFFDARVL VNKLILDATD PLSKQTDYKK CPIKITKV
//
DBGET integrated database retrieval system