Reviewed, UniProtKB/Swiss-Prot P15339 (DKGB_CORSS)

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

Organism

Corynebacterium sp. (strain SHS752001)

Taxonomic identifier

268953 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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). 25DKGR-B has higher catalytic efficiency than 25DKGR-A. Ref.1
Catalytic activity	2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH.
Subcellular location	Cytoplasm Probable.
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	Direct protein sequencing
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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 277	276	2,5-diketo-D-gluconic acid reductase B		PRO_0000124598
Regions
	Nucleotide binding	189 – 242	54	NADP By similarity
Sites
	Active site	51	1	Proton donor By similarity
	Binding site	109	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15339-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7E72D1C24FFD30AA	FASTA	277	30,548
	10 20 30 40 50 60 MPNIPTISLN DGRPFAEPGL GTYNLRGDEG VAAMVAAIDS GYRLLDTAVN YENESEVGRA 70 80 90 100 110 120 VRASSVDRDE LIVASKIPGR QHGRAEAVDS IRGSLDRLGL DVIDLQLIHW PNPSVGRWLD 130 140 150 160 170 180 TWRGMIDARE AGLVRSIGVS NFTEPMLKTL IDETGVTPAV NQVELHPYFP QAALRAFHDE 190 200 210 220 230 240 HGIRTESWSP LARRSELLTE QLLQELAVVY GVTPTQVVLR WHVQLGSTPI PKSADPDRQR 250 260 270 ENADVFGFAL TADQVDAISG LERGRLWDGD PDTHEEM

References

[1]

"Conversion of glucose to 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a recombinant strain of Erwinia citreus." Grindley J.F., Payton M.A., van de Pol H., Hardy K.G. Appl. Environ. Microbiol. 54:1770-1775(1988) [PubMed: 16347687] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-61 AND 147-176, FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M21193 Genomic DNA. Translation: AAA23291.1.
PIR	A45961.
3D structure databases
HSSP	HSSP built from PDB template 1HW6 based on UniProtKB P06632.
ModBase	Search...
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DKGB_CORSS

Accession

Primary (citable) accession number: P15339

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 58 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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