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P33937 (NAPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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:yojC, yojD, yojE
Ordered Locus Names:b2206, JW2194
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length828 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 By similarity. HAMAP-Rule MF_01630

Catalytic activity

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

Cofactor

Binds 1 4Fe-4S cluster By similarity. HAMAP-Rule MF_01630

Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit By similarity.

Subunit structure

Interacts with NapB By similarity. HAMAP-Rule MF_01630

Subcellular location

Periplasm Ref.6.

Post-translational modification

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.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Sequence caution

The sequence AAA16399.1 differs from that shown. Reason: Frameshift at positions 19 and 27.

Ontologies

Keywords
   Biological processElectron transport
Nitrate assimilation
Transport
   Cellular componentPeriplasm
   DomainSignal
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
Molybdenum
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMo-molybdopterin cofactor biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

anaerobic respiration

Inferred from genetic interaction PubMed 11844760. Source: EcoliWiki

cellular respiration

Inferred from Biological aspect of Ancestor. Source: RefGenome

nitrate assimilation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentouter membrane-bounded periplasmic space

Inferred from direct assay Ref.6. Source: CACAO

periplasmic space

Inferred from direct assay PubMed 8830238. Source: EcoCyc

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from direct assay PubMed 17130127. Source: EcoCyc

electron carrier activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

molybdenum ion binding

Inferred from direct assay PubMed 17130127. Source: EcoCyc

nitrate reductase activity

Inferred from direct assay Ref.6. Source: CACAO

oxidoreductase activity, acting on NAD(P)H

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 19151138PubMed 20974141PubMed 24314029PubMed 24561554. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

napDP0A9I58EBI-554952,EBI-554985

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636Tat-type signal Ref.6
Chain37 – 828792Periplasmic nitrate reductase HAMAP-Rule MF_01630
PRO_0000019170

Regions

Domain39 – 95574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding461Iron-sulfur (4Fe-4S) By similarity
Metal binding491Iron-sulfur (4Fe-4S) By similarity
Metal binding531Iron-sulfur (4Fe-4S) By similarity
Metal binding811Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict981T → R in AAA16399. Ref.1

Secondary structure

........................................................................................................................................................ 828
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33937 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: CE2D7AB000FEAFCA

FASTA82893,042
        10         20         30         40         50         60 
MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ 

        70         80         90        100        110        120 
QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKNGKYD KEGEFTPITW 

       130        140        150        160        170        180 
DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ WTIWEGYAAS KLFKAGFRSN NIDPNARHCM 

       190        200        210        220        230        240 
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGANMAEMH PILWSRITNR RLSNQNVTVA 

       250        260        270        280        290        300 
VLSTYQHRSF ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG 

       310        320        330        340        350        360 
YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD QLEQLAQLYA 

       370        380        390        400        410        420 
DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV 

       430        440        450        460        470        480 
GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS GTIPAKIGLH AVAQDRALKD GKLNVYWTMC 

       490        500        510        520        530        540 
TNNMQAGPNI NEERMPGWRD PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER 

       550        560        570        580        590        600 
RTQFWRQQVQ APGEAKSDLW QLVQFSRRFK TEEVWPEDLL AKKPELRGKT LYEVLYATPE 

       610        620        630        640        650        660 
VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HKARGLRWPV 

       670        680        690        700        710        720 
VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAEAPDE EYDLWLSTGR 

       730        740        750        760        770        780 
VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARDLRR GDKVKVVSRR GEVISIVETR 

       790        800        810        820 
GRNRPPQGLV YMPFFDAAQL VNKLTLDATD PLSKETDFKK CAVKLEKV 

« Hide

References

« Hide 'large scale' references
[1]"Automated multiplex sequencing of the E.coli genome."
Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / BHB2600.
[2]Robison K.
Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-757.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site."
Thomas G., Potter L., Cole J.A.
FEMS Microbiol. Lett. 174:167-171(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 37-43, SUBCELLULAR LOCATION.
[7]"Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides."
Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G.
J. Biol. Chem. 282:8309-8316(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: EXPORT VIA THE TAT-SYSTEM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00008 Genomic DNA. Translation: AAA16399.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75266.1.
AP009048 Genomic DNA. Translation: BAA15989.2.
PIRD64990.
RefSeqNP_416710.1. NC_000913.3.
YP_490444.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NYAX-ray2.50A/F37-828[»]
2PQ4NMR-B1-35[»]
ProteinModelPortalP33937.
SMRP33937. Positions 1-35, 37-827.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10304N.
IntActP33937. 12 interactions.
MINTMINT-1243254.
STRING511145.b2206.

Proteomic databases

PaxDbP33937.
PRIDEP33937.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75266; AAC75266; b2206.
BAA15989; BAA15989; BAA15989.
GeneID12933227.
947093.
KEGGecj:Y75_p2167.
eco:b2206.
PATRIC32119771. VBIEscCol129921_2295.

Organism-specific databases

EchoBASEEB1994.
EcoGeneEG12067. napA.

Phylogenomic databases

eggNOGCOG0243.
HOGENOMHOG000031441.
KOK02567.
OMAHPKTRVA.
OrthoDBEOG6CVV7G.
PhylomeDBP33937.

Enzyme and pathway databases

BioCycEcoCyc:NAPA-MONOMER.
ECOL316407:JW2194-MONOMER.
MetaCyc:NAPA-MONOMER.

Gene expression databases

GenevestigatorP33937.

Family and domain databases

HAMAPMF_01630. Nitrate_reduct.
InterProIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR027467. MopterinOxRdtase_cofactor_BS.
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. SSF50692. 1 hit.
TIGRFAMsTIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33937.
PROP33937.

Entry information

Entry nameNAPA_ECOLI
AccessionPrimary (citable) accession number: P33937
Secondary accession number(s): P78087
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene