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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   28-MAR-2018, entry version 94.
DE   RecName: Full=Periplasmic nitrate reductase 1 {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA1 {ECO:0000255|HAMAP-Rule:MF_01630};
GN   OrderedLocusNames=PBPRA0853;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / 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       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; CR378665; CAG19266.1; -; Genomic_DNA.
DR   RefSeq; WP_011217603.1; NC_006370.1.
DR   ProteinModelPortal; Q6LTV9; -.
DR   SMR; Q6LTV9; -.
DR   STRING; 298386.PBPRA0853; -.
DR   PRIDE; Q6LTV9; -.
DR   EnsemblBacteria; CAG19266; CAG19266; PBPRA0853.
DR   KEGG; ppr:PBPRA0853; -.
DR   eggNOG; ENOG4107QIW; Bacteria.
DR   eggNOG; COG0243; LUCA.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; EPRYDFP; -.
DR   OrthoDB; POG091H060P; -.
DR   Proteomes; UP000000593; Chromosome 1.
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:0043546; F:molybdopterin cofactor 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     30       Tat-type signal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   CHAIN        31    828       Periplasmic nitrate reductase 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT                                /FTId=PRO_0000045993.
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      510    511       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      718    727       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     374    374       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     378    378       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     484    484       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     533    533       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     560    560       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     794    794       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     802    802       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     819    819       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {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
//
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