P30863 (DKGB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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=1.1.1.346

Alternative name(s):
AKR5D

Gene names

Name:	dkgB
Synonyms:	yafB
Ordered Locus Names:	b0207, JW0197

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
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-L-gulonate + 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 Reference proteome
Gene Ontology (GO)
Biological_process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methylglyoxal catabolic process Inferred from mutant phenotype PubMed 16077126. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2,5-didehydrogluconate reductase activity Inferred from electronic annotation. Source: EC aldo-keto reductase (NADP) activity Inferred from direct assay Ref.7. Source: EcoCyc aryl-alcohol dehydrogenase (NADP+) activity Inferred from direct assay PubMed 16813561. Source: EcoCyc methylglyoxal reductase (NADPH-dependent, acetol producing) Inferred from direct assay PubMed 16077126. Source: EcoCyc
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_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 in BAA02170. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P30863 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

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.
PIR	A64745.
RefSeq	NP_414743.1. NC_000913.2. YP_488504.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P30863.
SMR	P30863. Positions 3-267.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30863. 1 interaction.
STRING	511145.b0207.
Proteomic databases
PaxDb	P30863.
PRIDE	P30863.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73312; AAC73312; b0207. BAA77878; BAA77878; BAA77878.
GeneID	12932790. 944901.
KEGG	ecj:Y75_p0198. eco:b0207.
PATRIC	32115527. VBIEscCol129921_0209.
Organism-specific databases
EchoBASE	EB1601.
EcoGene	EG11648. dkgB.
Phylogenomic databases
eggNOG	COG0656.
HOGENOM	HOG000250272.
KO	K06222.
OMA	CEAMATY.
ProtClustDB	PRK11172.
Enzyme and pathway databases
BioCyc	EcoCyc:MONOMER0-149. ECOL316407:JW0197-MONOMER. MetaCyc:MONOMER0-149.
SABIO-RK	P30863.
Gene expression databases
Genevestigator	P30863.
Family and domain databases
Gene3D	3.20.20.100. 1 hit.
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. IPR020471. Aldo/keto_reductase_subgr. IPR023210. NADP_OxRdtase_dom. [Graphical view]
PANTHER	PTHR11732. PTHR11732. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
PIRSF	PIRSF000097. AKR. 1 hit.
PRINTS	PR00069. ALDKETRDTASE.
SUPFAM	SSF51430. Aldo/ket_red. 1 hit.
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:	May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program