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P39185 (NAPA_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. 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
Ordered Locus Names:PHG211
Encoded onPlasmid megaplasmid pHG1
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus ›

Protein attributes

Sequence length831 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 By similarity.

Binds 1 molybdenum ion per subunit.

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

Subunit structure

Interacts with NapB By similarity.

Subcellular location

Periplasm HAMAP-Rule MF_01630.

Induction

Expressed independently of nitrate induction and anaerobiosis. 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 – 2929Tat-type signal Ref.1
Chain30 – 831802Periplasmic nitrate reductase HAMAP-Rule MF_01630
PRO_0000019168

Sites

Metal binding481Iron-sulfur (4Fe-4S) By similarity
Metal binding511Iron-sulfur (4Fe-4S) By similarity
Metal binding551Iron-sulfur (4Fe-4S) By similarity
Metal binding831Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict146 – 1516GMFGSG → ACSAPA in CAA50507. Ref.1

Secondary structure

1 ................................................................................................................................................ 831
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39185 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: 34CE1CDE6677C42F

FASTA83193,346
        10         20         30         40         50         60 
MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA 

        70         80         90        100        110        120 
VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT RPLMRMKNGK YDKNGDFAPV 

       130        140        150        160        170        180 
TWDQAFDEME RQFKRVLKEK GPTAVGMFGS GQWTVWEGYA AAKLYKAGFR SNNIDPNARH 

       190        200        210        220        230        240 
CMASAAAGFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR 

       250        260        270        280        290        300 
VVVLSTFTHR CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD 

       310        320        330        340        350        360 
IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV PKAKLDQLAE 

       370        380        390        400        410        420 
LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI ATPGNSPFSL TGQPSACGTA 

       430        440        450        460        470        480 
REVGTFSHRL PADMVVTNPK HREEAERIWK LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW 

       490        500        510        520        530        540 
VQVNNNMQAA ANLMEEGLPG YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN 

       550        560        570        580        590        600 
AERRTQFWHQ LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR 

       610        620        630        640        650        660 
NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF DAYHEARGLR 

       670        680        690        700        710        720 
WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF ALPYEPPAES PDKEYPYWLV 

       730        740        750        760        770        780 
TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF MHPEDAKALG LRRGVEVEVV SRRGRMRSRI 

       790        800        810        820        830 
ETRGRDAPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD FKKCAVKIVK V

« Hide

References

« Hide 'large scale' references
[1]"Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16."
Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S., Friedrich B.
J. Bacteriol. 175:5867-5876(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-50.
[2]"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."
Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.
J. Mol. Biol. 332:369-383(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X71385 Genomic DNA. Translation: CAA50507.1.
AY305378 Genomic DNA. Translation: AAP85963.1.
PIRA48489.
RefSeqNP_942849.1. NC_005241.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML1X-ray1.60A30-831[»]
3O5AX-ray1.72A30-831[»]
ProteinModelPortalP39185.
SMRP39185. Positions 41-828.
ModBaseSearch...

Protein-protein interaction databases

STRING381666.PHG211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2656653.
KEGGreh:PHG211.
PATRIC35228976. VBIRalEut6770_0159.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0243.
HOGENOMHOG000031441.
KOK02567.
OMANAYWVQV.
ProtClustDBPRK13532.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-6487-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.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR010051. Periplasm_NO3_reductase_lsu.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[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.
TIGRFAMsTIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. False negative.
PS00932. MOLYBDOPTERIN_PROK_3. False negative.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNAPA_CUPNH
AccessionPrimary (citable) accession number: P39185
Secondary accession number(s): Q7WXC3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 27, 2004
Last modified: May 1, 2013
This is version 108 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

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