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Reviewed, UniProtKB/Swiss-Prot A7ZP28 (NAPA_ECO24)

Last modified November 25, 2008. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Ordered Locus Names: EcE24377A_2505
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length828 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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.

Catalytic activity

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactor

Binds 1 4Fe-4S cluster By similarity.

Binds 1 molybdenum ion per subunit By similarity.

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

Subunit structure

Interacts with napB By similarity.

Subcellular location

PeriplasmBy similarity.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not 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 – 3131Tat-type signal Potential
Chain32 – 828797Periplasmic nitrate reductase
PRO_1000069716

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

Sequences

Sequence LengthMass (Da)Tools
A7ZP28-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: ED9CB0D5FBDCD250

FASTA82893,130
        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 DTIPAKIGLH AVAQDRALKD GKLNVYWTMC 

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

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

       610        620        630        640        650        660 
VSKYPVSELA 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 

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References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000800 Genomic DNA. Translation: ABV17335.1.
RefSeqYP_001463557.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5586430.
GenomeReviewsGene locus EcE24377A_2505 in contig CP000800_GR.
KEGGecw:EcE24377A_2505.
NMPDRfig|331111.3.peg.246.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01630.
[Tree]
InterProIPR009010. Asp_de-COase-like_fold.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_Fe4S4.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006657. MPT_dinuc_bd.
IPR010051. NO3_reductase_lsu_periplasm.
IPR006311. Tat.
[Graphical view]
Gene3DG3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
PfamPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
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_ECO24
AccessionPrimary (citable) accession number: A7ZP28
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 25, 2008
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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