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P30863 (DKGB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,5-diketo-D-gluconic acid reductase B

Short name=2,5-DKG reductase B
Short name=2,5-DKGR B
Short name=25DKGR-B
EC=1.1.1.274
Alternative name(s):
AKR5D
Gene names
Name:dkgB
Synonyms:yafB
Ordered Locus Names:b0207, JW0197
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).

Catalytic activity

2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH.

Subunit structure

Monomer.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

2-keto-L-gulonic acid is a key intermediate in the production of L-ascorbic acid (vitamin C).

Sequence similarities

Belongs to the aldo/keto reductase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0.

Ontologies

Keywords
   Biological processAscorbate biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processL-ascorbic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function2,5-didehydrogluconate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2672672,5-diketo-D-gluconic acid reductase B
PRO_0000124604

Regions

Nucleotide binding179 – 23153NADP By similarity

Sites

Active site391Proton donor By similarity
Binding site971Substrate By similarity

Experimental info

Sequence conflict194 – 1952RI → AY in BAA02170. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P30863 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 265C7B1CC2D9C2E5

FASTA26729,437
        10         20         30         40         50         60 
MAIPAFGLGT FRLKDDVVIS SVITALELGY RAIDTAQIYD NEAAVGQAIA ESGVPRHELY 

        70         80         90        100        110        120 
ITTKIWIENL SKDKLIPSLK ESLQKLRTDY VDLTLIHWPS PNDEVSVEEF MQALLEAKKQ 

       130        140        150        160        170        180 
GLTREIGISN FTIPLMEKAI AAVGAENIAT NQIELSPYLQ NRKVVAWAKQ HGIHITSYMT 

       190        200        210        220        230        240 
LAYGKALKDE VIARIAAKHN ATPAQVILAW AMGEGYSVIP SSTKRKNLES NLKAQNLQLD 

       250        260 
AEDKKAIAAL DCNDRLVSPE GLAPEWD 

« Hide

References

« Hide 'large scale' references
[1]Nishimura K., Komine Y., Miyamoto K., Kitabatake M., Mathunaga F., Hisano T., Miki T., Inokuchi H.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"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], SEQUENCE REVISION TO 194-195.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Sequence of the distal tRNA1Asp gene and the transcription termination signal in the Escherichia coli ribosomal RNA operon rrnF(or G)."
Sekiya T., Mori M., Takahashi N., Nishimura S.
Nucleic Acids Res. 8:3809-3827(1980) [PubMed: 6255418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[7]"Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli."
Yum D.-Y., Lee B.-Y., Pan J.-G.
Appl. Environ. Microbiol. 65:3341-3346(1999) [PubMed: 10427017] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D12650 Genomic DNA. Translation: BAA02170.1.
U70214 Genomic DNA. Translation: AAB08629.1.
U00096 Genomic DNA. Translation: AAC73312.1.
AP009048 Genomic DNA. Translation: BAA77878.2.
V00336 Genomic DNA. Translation: CAA23619.1.
PIRA64745.
RefSeqNP_414743.1. NC_000913.2.

3D structure databases

ProteinModelPortalP30863.
SMRP30863. Positions 1-256.
ModBaseSearch...

Protein-protein interaction databases

IntActP30863. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003306; EBESCP00000003306; EBESCG00000002710.
EBESCT00000014801; EBESCP00000014092; EBESCG00000013861.
GeneID944901.
GenomeReviewsGene locus JW0197 in contig AP009048_GR.
Gene locus b0207 in contig U00096_GR.
KEGGecj:JW0197.
eco:b0207.
PATRIC32115527. VBIEscCol129921_0209.

Organism-specific databases

EchoBASEEB1601.
EcoGeneEG11648. dkgB.

Phylogenomic databases

eggNOGCOG0656.
GeneTreeEBGT00050000009262.
HOGENOMHBG605727.
OMALAWAMQL.
PhylomeDBP30863.
ProtClustDBPRK11172.

Enzyme and pathway databases

BioCycEcoCyc:MONOMER0-149.
MetaCyc:MONOMER0-149.

Gene expression databases

GenevestigatorP30863.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
KOK06222.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. Aldo/ket_red. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDKGB_ECOLI
AccessionPrimary (citable) accession number: P30863
Secondary accession number(s): P77777
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: April 27, 2001
Last modified: January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families