P28304 (QOR1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Quinone oxidoreductase 1
EC=1.6.5.5

Alternative name(s):
NADPH:quinone reductase 1
Zeta-crystallin homolog protein

Gene names

Name:	qorA
Synonyms:	hcz, qor, qor1
Ordered Locus Names:	b4051, JW4011

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	NADPH + 2 quinone = NADP+ + 2 semiquinone.
Subunit structure	Homodimer. Ref.5
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: EcoliWiki
Molecular function	NADPH:quinone reductase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 327

327

Quinone oxidoreductase 1

PRO_0000160901

Regions

Nucleotide binding

42 – 46

5

NADP

Nucleotide binding

152 – 153

2

NADP

Nucleotide binding

173 – 177

5

NADP

Nucleotide binding

238 – 241

4

NADP

Nucleotide binding

264 – 266

3

NADP

Sites

Binding site

130

1

NADP

Binding site

192

1

NADP

Binding site

216

1

NADP; via carbonyl oxygen

Binding site

317

1

NADP

Secondary structure

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327

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

13 – 15

3

Beta strand

17 – 20

4

Beta strand

30 – 39

10

Helix

42 – 48

7

Beta strand

55 – 59

5

Beta strand

65 – 72

8

Beta strand

84 – 88

5

Beta strand

95 – 102

8

Helix

103 – 105

3

Beta strand

106 – 108

3

Helix

115 – 133

19

Beta strand

143 – 148

6

Helix

152 – 164

13

Beta strand

167 – 174

8

Helix

175 – 184

10

Beta strand

187 – 191

5

Turn

192 – 194

3

Helix

197 – 204

8

Turn

205 – 207

3

Beta strand

210 – 215

6

Helix

219 – 221

3

Helix

222 – 227

6

Beta strand

229 – 237

9

Helix

251 – 255

5

Beta strand

260 – 262

3

Helix

266 – 269

4

Helix

273 – 288

16

Helix

298 – 300

3

Beta strand

301 – 303

3

Helix

304 – 306

3

Helix

307 – 315

9

Beta strand

324 – 326

3

Sequences

	Sequence		Length	Mass (Da)
	P28304 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: A6355B12DBA513B2	FASTA	327	35,172
	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

References

	« Hide 'large scale' referencesShow '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) IN COMPLEX WITH NADP, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

S45529.

RefSeq

NP_418475.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QOR	X-ray	2.20	A/B	1-327	[»]

ProteinModelPortal

P28304.

SMR

P28304. Positions 2-327.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10631N.

IntAct

P28304. 4 interactions.

MINT

MINT-1267314.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004313; EBESCP00000004313; EBESCG00000003513.
EBESCT00000017952; EBESCP00000017243; EBESCG00000017008.

GeneID

948556.

GenomeReviews

Gene locus JW4011 in contig AP009048_GR.
Gene locus b4051 in contig U00096_GR.

KEGG

ecj:JW4011.
eco:b4051.

PATRIC

32123641. VBIEscCol129921_4169.

Organism-specific databases

EchoBASE

EB1455.

EcoGene

EG11492. qorA.

Phylogenomic databases

eggNOG

COG0604.

GeneTree

EBGT00050000008798.

HOGENOM

HBG753318.

OMA

ENTQAMA.

PhylomeDB

P28304.

ProtClustDB

PRK10754.

Enzyme and pathway databases

BioCyc

EcoCyc:QOR-MONOMER.
MetaCyc:QOR-MONOMER.

Gene expression databases

Genevestigator

P28304.

Family and domain databases

InterPro

IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K00344.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

SUPFAM

SSF50129. GroES_like. 1 hit.

PROSITE

PS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

QOR1_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program