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UniProtKB/Swiss-Prot entry P28304

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name QOR_ECOLI
Primary accession number P28304
Secondary accession number Q2M6Q3
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 76)
Name and origin of the protein
Protein name Quinone oxidoreductase
Synonyms EC 1.6.5.5
NADPH:quinone reductase
Zeta-crystallin homolog protein
Gene name
Name: qor
Synonyms: hcz
OrderedLocusNames: b4051, JW4011
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Dixon N.E., Lilley P.E.;
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1006/jmbi.1995.0337; PubMed=7602590 [NCBI, ExPASy, EBI, Israel, Japan]
Thorn J.M., Barton J.D., Dixon N.E., Ollis D.L., Edwards K.J.;
"Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.";
J. Mol. Biol. 249:785-799(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L02312; AAA23691.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00006; AAC43145.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77021.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78053.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S45529; S45529.
RefSeq AP_004552.1; -.
NP_418475.1; -.
3D structure databases
PDB
1QOR; X-ray; 2.20 A; A/B=1-327.[ExPASy / RCSB / EBI]
2FRO; Model; -; A=3-327.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1QOR; -.
2FRO; -.
ModBase P28304.
Protein-protein interaction databases
DIP DIP:10631N; -.
IntAct P28304; -.
Enzyme and pathway databases
BioCyc EcoCyc:QOR-MON; -.
MetaCyc:QOR-MON; -.
Organism-specific databases
EchoBASE EB1455; -.
EcoGene EG11492; qor.
Ontologies
GO
GO:0003960; Molecular function: NADPH:quinone reductase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR016040; NAD(P)-bd.
IPR002364; Quin_OxRdtase/zeta-crystal_CS.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PROSITE PS01162; QOR_ZETA_CRYSTAL; 1.
BLOCKS P28304.
ProtoNet P28304.
Genome annotation databases
GeneID 948556; -.
GenomeReviews U00096_GR; b4051.
AP009048_GR; JW4011.
KEGG ecj:JW4011; -.
eco:b4051; -.
Phylogenomic databases
HOGENOM P28304; -.
Other
LinkHub P28304; -.
Genome annotation databases
CMR P28304; b4051.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   327  327     Quinone oxidoreductase. PRO_0000160901
STRAND   3     9  7      
HELIX   13    15  3      
STRAND   17    20  4      
STRAND   30    39  10      
HELIX   42    48  7      
STRAND   55    59  5      
STRAND   65    72  8      
STRAND   84    88  5      
STRAND   95   102  8      
HELIX   103   105  3      
STRAND   106   108  3      
HELIX   115   133  19      
STRAND   143   148  6      
HELIX   152   164  13      
STRAND   167   174  8      
HELIX   175   184  10      
STRAND   187   191  5      
TURN   192   194  3      
HELIX   197   204  8      
TURN   205   207  3      
STRAND   210   215  6      
HELIX   219   221  3      
HELIX   222   227  6      
STRAND   229   237  9      
HELIX   251   255  5      
STRAND   260   262  3      
HELIX   266   269  4      
HELIX   273   288  16      
HELIX   298   300  3      
STRAND   301   303  3      
HELIX   304   306  3      
HELIX   307   315  9      
STRAND   324   326  3      
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 35172 Da [This is the MW of the unprocessed precursor] CRC64: A6355B12DBA513B2 [This is a checksum on the sequence] 
        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
P28304 in FASTA format

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