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UniProtKB/Swiss-Prot entry P81186


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NAPA_DESDE
Primary accession number P81186
Secondary accession number Q599G8
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 66)
Name and origin of the protein
Protein name Periplasmic nitrate reductase [Precursor]
Synonym EC 1.7.99.4
Gene name
Name: napA
Synonyms: nap
From
Desulfovibrio desulfuricans [TaxID: 876] 
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; Desulfovibrionaceae; Desulfovibrio.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
STRAIN=ATCC 27774 / DSM 6949;
DOI=10.1016/S0969-2126(99)80010-0; PubMed=10368307 [NCBI, ExPASy, EBI, Israel, Japan]
Dias J.M., Than M.E., Humm A., Huber R., Bourenkov G.P., Bartunik H.D., Bursakov S., Calvete J.J., Caldeira J., Carneiro C., Moura J.J.G., Moura I., Romao M.J.;
"Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods.";
Structure 7:65-79(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 27774 / DSM 6949;
DOI=10.1016/j.femsle.2005.05.042; PubMed=15972253 [NCBI, ExPASy, EBI, Israel, Japan]
Marietou A., Richardson D., Cole J., Mohan S.;
"Nitrate reduction by Desulfovibrio desulfuricans: a periplasmic nitrate reductase system that lacks NapB, but includes a unique tetraheme c-type cytochrome, NapM.";
FEMS Microbiol. Lett. 248:217-225(2005).
[3]
PROTEIN SEQUENCE OF 33-73.
STRAIN=ATCC 27774 / DSM 6949;
DOI=10.1006/bbrc.1997.7560; PubMed=9367852 [NCBI, ExPASy, EBI, Israel, Japan]
Bursakov S.A., Carneiro C., Almendra M.J., Duarte R.O., Caldeira J., Moura I., Moura J.J.G.;
"Enzymatic properties and effect of ionic strength on periplasmic nitrate reductase (NAP) from Desulfovibrio desulfuricans ATCC 27774.";
Biochem. Biophys. Res. Commun. 239:816-822(1997).
[4]
CHARACTERIZATION.
STRAIN=ATCC 27774 / DSM 6949;
DOI=10.1016/S1075-9964(95)80444-7; PubMed=16887508 [NCBI, ExPASy, EBI, Israel, Japan]
Bursakov S., Liu M.-Y., Payne W.J., Legall J., Moura I., Moura J.J.G.;
"Isolation and preliminary characterization of a soluble nitrate reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans 27774.";
Anaerobe 1:55-60(1995).
Comments
  • FUNCTION: Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism.
  • CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced acceptor.
  • COFACTOR: Binds 1 4Fe-4S cluster.
  • COFACTOR: Binds 1 molybdenum ion per subunit.
  • COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit.
  • SUBUNIT: Monomer.
  • SUBCELLULAR LOCATION: Periplasm.
  • INDUCTION: Nitrate reductase activity is induced by potassium and sodium and inhibited by magnesium and calcium.
  • PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
  • SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y18045; CAA77019.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ920046; CAI72603.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR PC4422; PC4422.
3D structure databases
PDB
2JIM; X-ray; 2.45 A; A=33-755.[ExPASy / RCSB / EBI]
2JIO; X-ray; 2.20 A; A=33-755.[ExPASy / RCSB / EBI]
2JIP; X-ray; 2.30 A; A=33-755.[ExPASy / RCSB / EBI]
2JIQ; X-ray; 2.44 A; A=33-755.[ExPASy / RCSB / EBI]
2JIR; X-ray; 2.35 A; A=33-755.[ExPASy / RCSB / EBI]
2NAP; X-ray; 1.90 A; A=33-755.[ExPASy / RCSB / EBI]
2V3V; X-ray; 1.99 A; A=33-755.[ExPASy / RCSB / EBI]
2V45; X-ray; 2.40 A; A=33-755.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2JIM; -.
2JIO; -.
2JIP; -.
2JIQ; -.
2JIR; -.
2NAP; -.
2V3V; -.
2V45; -.
ModBase P81186.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from HAMAP).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0008940; Molecular function: nitrate reductase activity (inferred from electronic annotation from HAMAP).
GO:0006777; Biological process: Mo-molybdopterin cofactor biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0042128; Biological process: nitrate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01630; -; 1.
PBIL [Tree]
InterPro IPR009010; Asp_de-COase-like_fold.
IPR006656; Mopterin_OxRdtase.
IPR006963; Mopterin_OxRdtase_Fe4S4.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
IPR006311; Tat.
Graphical view of domain structure.
Gene3D G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
Pfam PF04879; Molybdop_Fe4S4; 1.
PF00384; Molybdopterin; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01409; TAT_signal_seq; 1.
PROSITE PS00551; MOLYBDOPTERIN_PROK_1; FALSE_NEG.
PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P81186.
Other
ProtoNet P81186.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Periplasm; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    32  32     Tat-type signal. 
CHAIN   33   755  723     Periplasmic nitrate reductase. PRO_0000019169
METAL   45    45        Iron-sulfur (4Fe-4S). 
METAL   48    48        Iron-sulfur (4Fe-4S). 
METAL   52    52        Iron-sulfur (4Fe-4S). 
METAL   79    79        Iron-sulfur (4Fe-4S). 
STRAND   38    44  7      
STRAND   53    59  7      
STRAND   62    68  7      
TURN   73    76  4      
HELIX   80    83  4      
HELIX   86    89  4      
HELIX   113   131  19      
HELIX   133   135  3      
STRAND   136   140  5      
HELIX   146   158  13      
STRAND   165   167  3      
HELIX   168   170  3      
TURN   171   173  3      
HELIX   174   184  11      
HELIX   193   197  5      
STRAND   200   206  7      
HELIX   209   212  4      
HELIX   214   226  13      
STRAND   231   235  5      
HELIX   241   245  5      
STRAND   247   250  4      
TURN   254   256  3      
HELIX   257   270  14      
HELIX   276   282  7      
STRAND   283   286  4      
HELIX   295   302  8      
HELIX   303   305  3      
HELIX   307   314  8      
HELIX   318   330  13      
STRAND   331   338  8      
TURN   340   342  3      
STRAND   343   345  3      
HELIX   348   362  15      
STRAND   370   374  5      
HELIX   381   384  4      
TURN   385   389  5      
TURN   396   398  3      
HELIX   404   414  11      
HELIX   429   438  10      
STRAND   443   448  6      
HELIX   451   454  4      
STRAND   455   457  3      
HELIX   458   465  8      
STRAND   471   475  5      
HELIX   482   485  4      
STRAND   488   491  4      
HELIX   496   498  3      
STRAND   501   504  4      
STRAND   508   513  6      
HELIX   526   537  12      
TURN   541   544  4      
HELIX   549   560  12      
HELIX   572   577  6      
STRAND   581   583  3      
TURN   599   601  3      
STRAND   610   613  4      
STRAND   623   626  4      
STRAND   639   641  3      
STRAND   643   648  6      
HELIX   660   662  3      
HELIX   664   667  4      
STRAND   675   678  4      
HELIX   679   685  7      
STRAND   692   697  6      
STRAND   700   712  13      
STRAND   716   720  5      
HELIX   728   730  3      
TURN   738   740  3      
STRAND   748   754  7      
Sequence information
Length: 755 AA [This is the length of the unprocessed precursor] Molecular weight: 83497 Da [This is the MW of the unprocessed precursor] CRC64: D54BDB9D1FE21DC2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTSRRDFLK YFAMSAAVAA ASGAGFGSLA LAADNRPEKW VKGVCRYCGT GCGVLVGVKD 

        70         80         90        100        110        120 
GKAVAIQGDP NNHNAGLLCL KGSLLIPVLN SKERVTQPLV RRHKGGKLEP VSWDEALDLM 

       130        140        150        160        170        180 
ASRFRSSIDM YGPNSVAWYG SGQCLTEESY VANKIFKGGF GTNNVDGNPR LCMASAVGGY 

       190        200        210        220        230        240 
VTSFGKDEPM GTYADIDQAT CFFIIGSNTS EAHPVLFRRI ARRKQVEPGV KIIVADPRRT 

       250        260        270        280        290        300 
NTSRIADMHV AFRPGTDLAF MHSMAWVIIN EELDNPRFWQ RYVNFMDAEG KPSDFEGYKA 

       310        320        330        340        350        360 
FLENYRPEKV AEICRVPVEQ IYGAARAFAE SAATMSLWCM GINQRVQGVF ANNLIHNLHL 

       370        380        390        400        410        420 
ITGQICRPGA TSFSLTGQPN ACGGVRDGGA LSHLLPAGRA IPNAKHRAEM EKLWGLPEGR 

       430        440        450        460        470        480 
IAPEPGYHTV ALFEALGRGD VKCMIICETN PAHTLPNLNK VHKAMSHPES FIVCIEAFPD 

       490        500        510        520        530        540 
AVTLEYADLV LPPAFWCERD GVYGCGERRY SLTEKAVDPP GQCRPTVNTL VEFARRAGVD 

       550        560        570        580        590        600 
PQLVNFRNAE DVWNEWRMVS KGTTYDFWGM TRERLRKESG LIWPCPSEDH PGTSLRYVRG 

       610        620        630        640        650        660 
QDPCVPADHP DRFFFYGKPD GRAVIWMRPA KGAAEEPDAE YPLYLTSMRV IDHWHTATMT 

       670        680        690        700        710        720 
GKVPELQKAN PIAFVEINEE DAARTGIKHG DSVIVETRRD AMELPARVSD VCRPGLIAVP 

       730        740        750 
FFDPKKLVNK LFLDATDPVS REPEYKICAA RVRKA 

P81186 in FASTA format

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