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Reviewed, UniProtKB/Swiss-Prot Q8ZI40 (DKGA_YERPE)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2,5-diketo-D-gluconic acid reductase A
      Short name=2,5-DKG reductase A
      Short name=2,5-DKGR A
      Short name=25DKGR-A
    EC=1.1.1.274
Alternative name(s):
    AKR5C
Gene names
Name: dkgA
Synonyms: ara14
Ordered Locus Names: YPO0676, y3501, YP_2991
OrganismYersinia pestis [Complete proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Monomer By similarity.

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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

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 – 2772772,5-diketo-D-gluconic acid reductase A
PRO_0000124603

Regions

Nucleotide binding187 – 24155NADP By similarity

Sites

Active site511Proton donor By similarity
Binding site1071Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZI40-1 [UniParc].

Last modified March 27, 2002. Version 1.
Checksum: ED9C2945F0EBD140

FASTA27731,520
        10         20         30         40         50         60 
MTMQPLIKLY DGRLMPQLGL GVWQASIQET ELAVSKALEV GYRSIDTAAI YKNEEGVGKA 

        70         80         90        100        110        120 
LKAAAVARDE LFITTKLWND DQHNPQQALE TSLQKLQLDY VDLYLIHWPD PKQDHYVSAW 

       130        140        150        160        170        180 
RELVTLKEQG LIRSIGVCNF HIPHLQRLID ETGIAPTVNQ IELHPLLQQR QLHAWNATHH 

       190        200        210        220        230        240 
IATESWSPLA QGGKGVFDQE IIRKLAQQYN KTPAQIVIRW HLDSGLIVIP KSVTPARIRE 

       250        260        270 
NFEVFDFKLQ KEELLAITKL DCGKRLGPDP EVFGSDR 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed: 11586360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed: 12142430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM5 / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed: 15368893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

AL590842 Genomic DNA. Translation: CAL19352.1.
AE009952 Genomic DNA. Translation: AAM87049.1.
AE017042 Genomic DNA. Translation: AAS63169.1.
PIRAF0083.
RefSeqNP_670798.1.
NP_994292.1.
YP_002345742.1.

3D structure databases

HSSPHSSP built from PDB template 1HW6 based on UniProtKB P06632.
SMRQ8ZI40. Positions 6-274.
ModBaseSearch...

Genome annotation databases

GeneID1148448.
1173519.
2766792.
GenomeReviewsGene locus y3501 in contig AE009952_GR.
Gene locus YP_2991 in contig AE017042_GR.
Gene locus YPO0676 in contig AL590842_GR.
KEGGype:YPO0676.
ypk:y3501.
ypm:YP_2991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8ZI40.
OMAQ8ZI40. GIAVEAY.

Enzyme and pathway databases

BioCycYPES187410:Y3501-MON.
YPES214092:YPO0676-MON.
YPES229193:YP2991-MON.
BRENDA1.1.1.274. 142588.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDKGA_YERPE
AccessionPrimary (citable) accession number: Q8ZI40
Secondary accession number(s): Q0WIZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: June 16, 2009
This is version 58 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

SIMILARITY comments

Index of protein domains and families

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