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Reviewed, UniProtKB/Swiss-Prot P28304 (QOR_ECOLI)

Last modified November 3, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Quinone oxidoreductase
    EC=1.6.5.5
Alternative name(s):
    NADPH:quinone reductase
    Zeta-crystallin homolog protein
Gene names
Name: qor
Synonyms: hcz
Ordered Locus Names: b4051, JW4011
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

NADPH + 2 quinone = NADP+ + 2 semiquinone.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNADPH:quinone reductase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dnaKP0A6Y81EBI-556687,EBI-542092

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Quinone oxidoreductase
PRO_0000160901

Secondary structure

.......................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28304-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: A6355B12DBA513B2

FASTA32735,172
        10         20         30         40         50         60 
MATRIEFHKH GGPEVLQAVE FTPADPAENE IQVENKAIGI NFIDTYIRSG LYPPPSLPSG 

        70         80         90        100        110        120 
LGTEAAGIVS KVGSGVKHIK AGDRVVYAQS ALGAYSSVHN IIADKAAILP AAISFEQAAA 

       130        140        150        160        170        180 
SFLKGLTVYY LLRKTYEIKP DEQFLFHAAA GGVGLIACQW AKALGAKLIG TVGTAQKAQS 

       190        200        210        220        230        240 
ALKAGAWQVI NYREEDLVER LKEITGGKKV RVVYDSVGRD TWERSLDCLQ RRGLMVSFGN 

       250        260        270        280        290        300 
SSGAVTGVNL GILNQKGSLY VTRPSLQGYI TTREELTEAS NELFSLIASG VIKVDVAEQQ 

       310        320 
KYPLKDAQRA HEILESRATQ GSSLLIP 

« Hide

References

« Hide 'large scale' references
[1]Dixon N.E., Lilley P.E.
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH."
Thorn J.M., Barton J.D., Dixon N.E., Ollis D.L., Edwards K.J.
J. Mol. Biol. 249:785-799(1995) [PubMed: 7602590] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

L02312 Genomic DNA. Translation: AAA23691.1.
U00006 Genomic DNA. Translation: AAC43145.1.
U00096 Genomic DNA. Translation: AAC77021.1.
AP009048 Genomic DNA. Translation: BAE78053.1.
PIRS45529.
RefSeqAP_004552.1.
NP_418475.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QORX-ray2.20A/B1-327[»]
2FROmodel-A3-327[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:10631N.
IntActP28304. 4 interactions.
STRINGP28304.

Genome annotation databases

GeneID948556.
GenomeReviewsGene locus JW4011 in contig AP009048_GR.
Gene locus b4051 in contig U00096_GR.
KEGGecj:JW4011.
eco:b4051.

Organism-specific databases

EchoBASEEB1455.
EcoGeneEG11492. qor.
CMRSearch...

Phylogenomic databases

HOGENOMP28304.
OMAQTELSAR.

Enzyme and pathway databases

BioCycEcoCyc:QOR-MON.
MetaCyc:QOR-MON.

Gene expression databases

GenevestigatorP28304.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR016040. NAD(P)-bd_dom.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQOR_ECOLI
AccessionPrimary (citable) accession number: P28304
Secondary accession number(s): Q2M6Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 3, 2009
This is version 83 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

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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