Reviewed, UniProtKB/Swiss-Prot Q8X7Z7 (DKGB_ECO57)

Names and origin

Protein names

Recommended 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
Ordered Locus Names:	Z0229, ECs0203

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Ascorbate biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2,5-didehydrogluconate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 267	267	2,5-diketo-D-gluconic acid reductase B		PRO_0000124605
Regions
	Nucleotide binding	179 – 231	53	NADP By similarity
Sites
	Active site	39	1	Proton donor By similarity
	Binding site	97	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X7Z7-1 [UniParc]. Last modified March 27, 2002. Version 1. Checksum: C03126A69D94CED4	FASTA	267	29,439
	10 20 30 40 50 60 MAIPAFGLGT FRLKDDVVIS SVKTALELGY RAIDTAQIYD NEAAVGLAIA ESGVPRHELY 70 80 90 100 110 120 ITTKIWIENL SKDKLIPSLK ESLQKLRTDY VDLTLIHWPS PNDEVSVEEF MQALLEAKKE 130 140 150 160 170 180 GLTREIGISN FTIPLMEKAI AAVGAENIAT NQIELSPYLQ NRKVVAWAKQ HGIHITSYMT 190 200 210 220 230 240 LAYGKALKDE VIARIAAKHN ATPAQVILAW AMGEGYSVIP SSTKRENLES NLKAQNLQLD 250 260 AEDKKAIAAL DCNDRLVSPE GLAPEWD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
[3]	"Comparative analysis of the whole set of rRNA operons between an enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an Escherichia coli K-12 strain MG1655." Ohnishi M., Murata T., Nakayama K., Kuhara S., Hattori M., Kurokawa K., Yasunaga T., Yokoyama K., Makino K., Shinagawa H., Hayashi T. Syst. Appl. Microbiol. 23:315-324(2000) [PubMed: 11108008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-206. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG54503.1. BA000007 Genomic DNA. Translation: BAB33626.1. AB035926 Genomic DNA. Translation: BAA93569.1.
PIR	C85505. C90654.
RefSeq	NP_285895.1. NP_308230.1.
3D structure databases
HSSP	HSSP built from PDB template 1HW6 based on UniProtKB P06632.
ModBase	Search...
Genome annotation databases
GeneID	914031. 956971.
GenomeReviews	Gene locus Z0229 in contig AE005174_GR. Gene locus ECs0203 in contig BA000007_GR.
KEGG	ece:Z0229. ecs:ECs0203.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8X7Z7.
OMA	Q8X7Z7. NRKVVDW.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS0203-MON.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
ProDom	PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DKGB_ECO57

Accession

Primary (citable) accession number: Q8X7Z7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	March 27, 2002
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)