Periplasmic nitrate reductase precursor - Desulfovibrio desulfuricans

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Reviewed, UniProtKB/Swiss-Prot P81186 (NAPA_DESDE)

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Periplasmic nitrate reductase
EC=1.7.99.4

Gene names

Name:	napA
Synonyms:	nap

Organism

Desulfovibrio desulfuricans

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length	755 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Periplasm
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP nitrate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

32

Tat-type signal

Chain

723

Periplasmic nitrate reductase

PRO_0000019169

Sites

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron-sulfur (4Fe-4S)

Secondary structure

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755

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P81186-1 [UniParc].

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

755

83,497

        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

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.