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P33937

- NAPA_ECOLI

UniProt

P33937 - NAPA_ECOLI

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Protein

Periplasmic nitrate reductase

Gene
napA, yojC, yojD, yojE, b2206, JW2194
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.UniRule annotation

Cofactori

Binds 1 4Fe-4S cluster By similarity.UniRule annotation
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461Iron-sulfur (4Fe-4S) By similarity
Metal bindingi49 – 491Iron-sulfur (4Fe-4S) By similarity
Metal bindingi53 – 531Iron-sulfur (4Fe-4S) By similarity
Metal bindingi81 – 811Iron-sulfur (4Fe-4S) By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  2. electron carrier activity Source: UniProtKB-HAMAP
  3. iron ion binding Source: UniProtKB-HAMAP
  4. molybdenum ion binding Source: EcoCyc
  5. nitrate reductase activity Source: CACAO
  6. oxidoreductase activity, acting on NAD(P)H Source: RefGenome
  7. protein binding Source: IntAct

GO - Biological processi

  1. anaerobic respiration Source: EcoliWiki
  2. cellular respiration Source: RefGenome
  3. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
  4. nitrate assimilation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Nitrate assimilation, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductase (EC:1.7.99.4)
Gene namesi
Name:napA
Synonyms:yojC, yojD, yojE
Ordered Locus Names:b2206, JW2194
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12067. napA.

Subcellular locationi

Periplasm 1 Publication

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: CACAO
  2. periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Tat-type signal1 PublicationAdd
BLAST
Chaini37 – 828792Periplasmic nitrate reductaseUniRule annotationPRO_0000019170Add
BLAST

Post-translational modificationi

Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.UniRule annotation

Proteomic databases

PaxDbiP33937.
PRIDEiP33937.

Expressioni

Gene expression databases

GenevestigatoriP33937.

Interactioni

Subunit structurei

Interacts with NapB By similarity.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
napDP0A9I58EBI-554952,EBI-554985

Protein-protein interaction databases

DIPiDIP-10304N.
IntActiP33937. 12 interactions.
MINTiMINT-1243254.
STRINGi511145.b2206.

Structurei

Secondary structure

1
828
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2116
Beta strandi26 – 294
Beta strandi40 – 456
Beta strandi47 – 493
Beta strandi54 – 607
Beta strandi63 – 697
Turni74 – 785
Helixi82 – 854
Helixi86 – 894
Beta strandi101 – 1099
Beta strandi114 – 1174
Helixi120 – 13718
Helixi140 – 1423
Beta strandi143 – 1475
Helixi153 – 16412
Turni165 – 1673
Beta strandi172 – 1743
Helixi175 – 1773
Turni178 – 1803
Helixi181 – 19010
Helixi200 – 2056
Beta strandi207 – 2137
Helixi216 – 2194
Helixi221 – 23212
Beta strandi238 – 2469
Helixi248 – 2525
Beta strandi254 – 2585
Turni261 – 2633
Helixi264 – 27714
Helixi283 – 2897
Beta strandi290 – 2956
Helixi308 – 3114
Beta strandi321 – 3233
Helixi326 – 3349
Helixi338 – 3458
Helixi349 – 36012
Beta strandi366 – 3716
Helixi372 – 3754
Helixi380 – 39415
Beta strandi402 – 4065
Turni411 – 4166
Helixi417 – 4204
Helixi436 – 44611
Helixi461 – 4699
Beta strandi475 – 4806
Helixi483 – 4864
Turni490 – 4934
Helixi494 – 4996
Beta strandi504 – 5118
Helixi514 – 5174
Beta strandi519 – 5257
Helixi528 – 5303
Beta strandi533 – 5364
Beta strandi540 – 5456
Helixi558 – 5658
Helixi566 – 5683
Helixi571 – 5744
Helixi577 – 5804
Helixi584 – 5863
Helixi591 – 5955
Turni599 – 6024
Helixi606 – 6083
Helixi616 – 6216
Helixi625 – 63713
Turni638 – 6414
Helixi647 – 6504
Beta strandi656 – 6583
Beta strandi667 – 6715
Turni672 – 6743
Beta strandi694 – 6985
Beta strandi710 – 7123
Beta strandi714 – 7196
Helixi731 – 7333
Helixi735 – 7384
Beta strandi745 – 7473
Helixi750 – 7545
Turni755 – 7573
Beta strandi763 – 7686
Beta strandi771 – 78212
Beta strandi789 – 7935
Helixi801 – 8033
Turni811 – 8133
Beta strandi821 – 8266

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NYAX-ray2.50A/F37-828[»]
2PQ4NMR-B1-35[»]
ProteinModelPortaliP33937.
SMRiP33937. Positions 1-35, 37-827.

Miscellaneous databases

EvolutionaryTraceiP33937.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 95574Fe-4S Mo/W bis-MGD-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0243.
HOGENOMiHOG000031441.
KOiK02567.
OMAiHPKTRVA.
OrthoDBiEOG6CVV7G.
PhylomeDBiP33937.

Family and domain databases

HAMAPiMF_01630. Nitrate_reduct.
InterProiIPR009010. 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]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33937-1 [UniParc]FASTAAdd to Basket

« Hide

MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG    50
TGCGVLVGTQ QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP 100
LLRMKNGKYD KEGEFTPITW DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ 150
WTIWEGYAAS KLFKAGFRSN NIDPNARHCM ASAVVGFMRT FGMDEPMGCY 200
DDIEQADAFV LWGANMAEMH PILWSRITNR RLSNQNVTVA VLSTYQHRSF 250
ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG 300
YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD 350
QLEQLAQLYA DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP 400
GCGPFSLTGQ PSACGTAREV GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS 450
GTIPAKIGLH AVAQDRALKD GKLNVYWTMC TNNMQAGPNI NEERMPGWRD 500
PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER RTQFWRQQVQ 550
APGEAKSDLW QLVQFSRRFK TEEVWPEDLL AKKPELRGKT LYEVLYATPE 600
VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY 650
HKARGLRWPV VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP 700
FEPAAEAPDE EYDLWLSTGR VLEHWHTGSM TRRVPELHRA FPEAVLFIHP 750
LDAKARDLRR GDKVKVVSRR GEVISIVETR GRNRPPQGLV YMPFFDAAQL 800
VNKLTLDATD PLSKETDFKK CAVKLEKV 828
Length:828
Mass (Da):93,042
Last modified:November 1, 1997 - v3
Checksum:iCE2D7AB000FEAFCA
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981T → R in AAA16399. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00008 Genomic DNA. Translation: AAA16399.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75266.1.
AP009048 Genomic DNA. Translation: BAA15989.2.
PIRiD64990.
RefSeqiNP_416710.1. NC_000913.3.
YP_490444.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75266; AAC75266; b2206.
BAA15989; BAA15989; BAA15989.
GeneIDi12933227.
947093.
KEGGiecj:Y75_p2167.
eco:b2206.
PATRICi32119771. VBIEscCol129921_2295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00008 Genomic DNA. Translation: AAA16399.1 . Frameshift.
U00096 Genomic DNA. Translation: AAC75266.1 .
AP009048 Genomic DNA. Translation: BAA15989.2 .
PIRi D64990.
RefSeqi NP_416710.1. NC_000913.3.
YP_490444.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NYA X-ray 2.50 A/F 37-828 [» ]
2PQ4 NMR - B 1-35 [» ]
ProteinModelPortali P33937.
SMRi P33937. Positions 1-35, 37-827.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10304N.
IntActi P33937. 12 interactions.
MINTi MINT-1243254.
STRINGi 511145.b2206.

Proteomic databases

PaxDbi P33937.
PRIDEi P33937.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75266 ; AAC75266 ; b2206 .
BAA15989 ; BAA15989 ; BAA15989 .
GeneIDi 12933227.
947093.
KEGGi ecj:Y75_p2167.
eco:b2206.
PATRICi 32119771. VBIEscCol129921_2295.

Organism-specific databases

EchoBASEi EB1994.
EcoGenei EG12067. napA.

Phylogenomic databases

eggNOGi COG0243.
HOGENOMi HOG000031441.
KOi K02567.
OMAi HPKTRVA.
OrthoDBi EOG6CVV7G.
PhylomeDBi P33937.

Enzyme and pathway databases

BioCyci EcoCyc:NAPA-MONOMER.
ECOL316407:JW2194-MONOMER.
MetaCyc:NAPA-MONOMER.

Miscellaneous databases

EvolutionaryTracei P33937.
PROi P33937.

Gene expression databases

Genevestigatori P33937.

Family and domain databases

HAMAPi MF_01630. Nitrate_reduct.
InterProi IPR009010. 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 ]
Pfami PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view ]
SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiNAPA_ECOLI
AccessioniPrimary (citable) accession number: P33937
Secondary accession number(s): P78087
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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