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P81186 (NAPA_DESDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Periplasmic nitrate reductase
EC=1.7.99.4
Gene names
Name:napA
Synonyms:nap
Ordered Locus Names:Ddes_0616
OrganismDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) [Complete proteome] [HAMAP]
Taxonomic identifier525146 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio ›

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. HAMAP-Rule MF_01630

Catalytic activity

Nitrite + acceptor = nitrate + reduced acceptor. HAMAP-Rule MF_01630

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 HAMAP-Rule MF_01630.

Induction

Nitrate reductase activity is induced by potassium and sodium and inhibited by magnesium and calcium. HAMAP-Rule MF_01630

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. HAMAP-Rule MF_01630

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 Ref.4
Chain33 – 755723Periplasmic nitrate reductase HAMAP-Rule MF_01630
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

1 .................................................................................................................................... 755
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81186 [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

« Hide

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Hazen T.C.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27774 / DSM 6949.
[4]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-73.
[5]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y18045 Genomic DNA. Translation: CAA77019.1.
AJ920046 Genomic DNA. Translation: CAI72603.1.
CP001358 Genomic DNA. Translation: ACL48525.1.
PIRPC4422.
RefSeqYP_002479203.1. NC_011883.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JIMX-ray2.45A33-755[»]
2JIOX-ray2.20A33-755[»]
2JIPX-ray2.30A33-755[»]
2JIQX-ray2.44A33-755[»]
2JIRX-ray2.35A33-755[»]
2NAPX-ray1.90A33-755[»]
2V3VX-ray1.99A33-755[»]
2V45X-ray2.40A33-755[»]
ProteinModelPortalP81186.
SMRP81186. Positions 35-755.
ModBaseSearch...

Protein-protein interaction databases

STRING525146.Ddes_0616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL48525; ACL48525; Ddes_0616.
GeneID7284288.
KEGGdds:Ddes_0616.
PATRIC21734702. VBIDesDes50650_0720.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0243.
HOGENOMHOG000031441.
KOK02567.
ProtClustDBCLSK2311774.

Enzyme and pathway databases

BioCycDDES525146:GIWF-637-MONOMER.

Family and domain databases

Gene3D2.40.40.20. 1 hit.
HAMAPMF_01630. Nitrate_reduct.
InterProIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_Fe4S4_dom.
IPR010051. Periplasm_NO3_reductase_lsu.
IPR006311. TAT_signal.
[Graphical view]
PfamPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
PROSITEPS00551. MOLYBDOPTERIN_PROK_1. False negative.
PS00490. MOLYBDOPTERIN_PROK_2. False negative.
PS00932. MOLYBDOPTERIN_PROK_3. False negative.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP81186.

Entry information

Entry nameNAPA_DESDA
AccessionPrimary (citable) accession number: P81186
Secondary accession number(s): B8IYC9, Q599G8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents