Reviewed, UniProtKB/Swiss-Prot P30863 (DKGB_ECOLI)

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
Synonyms:	yafB
Ordered Locus Names:	b0207, JW0197

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [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	Evidence 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 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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
gsp	P0AES0	1	EBI-1114788,EBI-557080

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_0000124604
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
Experimental info
	Sequence conflict	194 – 195	2	RI → AY Ref.1
	Sequence conflict	194 – 195	2	RI → AY Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P30863-1 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: 265C7B1CC2D9C2E5	FASTA	267	29,437
	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

References

	« Hide 'large scale' referencesShow '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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	A64745.
RefSeq	AP_000862.1. NP_414743.1.
3D structure databases
HSSP	HSSP built from PDB template 1HW6 based on UniProtKB P06632.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30863. 1 interaction.
Genome annotation databases
GeneID	944901.
GenomeReviews	Gene locus JW0197 in contig AP009048_GR. Gene locus b0207 in contig U00096_GR.
KEGG	ecj:JW0197. eco:b0207.
Organism-specific databases
EchoBASE	EB1601.
EcoGene	EG11648. dkgB.
CMR	Search...
Phylogenomic databases
HOGENOM	P30863.
OMA	P30863. NRKVVDW.
Enzyme and pathway databases
BioCyc	EcoCyc:MON0-149. MetaCyc:MON0-149.
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_ECOLI

Accession

Primary (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:	June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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