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-MAY-2013, entry version 63.
DE RecName: Full=Periplasmic nitrate reductase 1;
DE EC=1.7.99.4;
DE Flags: Precursor;
GN Name=napA1; 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 (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; 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; IISAPYE; -.
DR ProtClustDB; PRK13532; -.
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 30 Tat-type signal (Potential).
FT CHAIN 31 828 Periplasmic nitrate reductase 1.
FT /FTId=PRO_0000045993.
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 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
//
