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Reviewed, UniProtKB/Swiss-Prot P81186 (NAPA_DESDE)

Last modified November 4, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4
Gene names
Name: napA
Synonyms: nap
OrganismDesulfovibrio desulfuricans
Taxonomic identifier876 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length755 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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.

Binds 1 molybdenum ion per subunit.

Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Induction

Nitrate reductase activity is induced by potassium and sodium and inhibited by magnesium and calcium.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232Tat-type signal
Chain33 – 755723Periplasmic nitrate reductase
PRO_0000019169

Sites

Metal binding451Iron-sulfur (4Fe-4S)
Metal binding481Iron-sulfur (4Fe-4S)
Metal binding521Iron-sulfur (4Fe-4S)
Metal binding791Iron-sulfur (4Fe-4S)

Secondary structure

.......................................................................................................................... 755
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81186-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: D54BDB9D1FE21DC2

FASTA75583,497
        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 

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References

[1]"Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods."
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.
Structure 7:65-79(1999) [PubMed: 10368307] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Strain: ATCC 27774 / DSM 6949.
[2]"Nitrate reduction by Desulfovibrio desulfuricans: a periplasmic nitrate reductase system that lacks NapB, but includes a unique tetraheme c-type cytochrome, NapM."
Marietou A., Richardson D., Cole J., Mohan S.
FEMS Microbiol. Lett. 248:217-225(2005) [PubMed: 15972253] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27774 / DSM 6949.
[3]"Enzymatic properties and effect of ionic strength on periplasmic nitrate reductase (NAP) from Desulfovibrio desulfuricans ATCC 27774."
Bursakov S.A., Carneiro C., Almendra M.J., Duarte R.O., Caldeira J., Moura I., Moura J.J.G.
Biochem. Biophys. Res. Commun. 239:816-822(1997) [PubMed: 9367852] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-73.
Strain: ATCC 27774 / DSM 6949.
[4]"Isolation and preliminary characterization of a soluble nitrate reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans 27774."
Bursakov S., Liu M.-Y., Payne W.J., Legall J., Moura I., Moura J.J.G.
Anaerobe 1:55-60(1995) [PubMed: 16887508] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 27774 / DSM 6949.
+Additional computationally mapped references.