Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06632

- DKGA_CORSC

UniProt

P06632 - DKGA_CORSC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

2,5-diketo-D-gluconic acid reductase A

Gene

dkgA

Organism
Corynebacterium sp. (strain ATCC 31090)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.

Catalytic activityi

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

Enzyme regulationi

Inhibited by Zn2+, Fe3+, Cu2+ and Ni2+.

Kineticsi

  1. KM=26 mM for 2,5-diketo-D-gluconate1 Publication
  2. KM=10 µM for NADPH1 Publication

pH dependencei

Optimum pH is 6.4. Active over a broad pH range.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Proton donor
Binding sitei108 – 1081Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 24255NADP1 PublicationAdd
BLAST

GO - Molecular functioni

  1. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. L-ascorbic acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17833.
SABIO-RKP06632.

Names & Taxonomyi

Protein namesi
Recommended name:
2,5-diketo-D-gluconic acid reductase A (EC:1.1.1.346)
Short name:
2,5-DKG reductase A
Short name:
2,5-DKGR A
Short name:
25DKGR-A
Alternative name(s):
AKR5C
Gene namesi
Name:dkgA
OrganismiCorynebacterium sp. (strain ATCC 31090)
Taxonomic identifieri268952 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Introduced by genetic manipulation and expressed in Erwinia herbicola by Anderson et al. The resultant organism is able to convert in a single fermentative step D-glucose into 2-keto-L-gulonic acid, a key precursor in the industrial production of L-ascorbic acid (vitamin C). However, the technology still needs some working on and is not used in commercial production at present.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221F → Y: Tighter binding of NADH.
Mutagenesisi232 – 2321K → G: Tighter binding of NADH.
Mutagenesisi238 – 2381R → H: Tighter binding of NADH.
Mutagenesisi272 – 2721A → G: Tighter binding of NADH.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 2782772,5-diketo-D-gluconic acid reductase APRO_0000124597Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73
Beta strandi13 – 175
Helixi26 – 283
Helixi29 – 3911
Beta strandi43 – 453
Helixi47 – 493
Helixi54 – 6310
Helixi67 – 693
Beta strandi71 – 766
Helixi78 – 803
Helixi86 – 9712
Beta strandi102 – 1076
Helixi112 – 1143
Helixi117 – 12913
Beta strandi132 – 1409
Helixi143 – 15311
Beta strandi158 – 1636
Helixi171 – 1799
Beta strandi183 – 1886
Helixi191 – 1933
Helixi201 – 21010
Helixi214 – 22411
Helixi236 – 2438
Helixi252 – 2598
Beta strandi264 – 2663
Turni274 – 2763

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A80X-ray2.10A2-278[»]
1HW6X-ray1.90A1-278[»]
1M9HX-ray2.00A1-278[»]
ProteinModelPortaliP06632.
SMRiP06632. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06632.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06632-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVPSIVLND GNSIPQLGYG VFKVPPADTQ RAVEEALEVG YRHIDTAAIY
60 70 80 90 100
GNEEGVGAAI AASGIARDDL FITTKLWNDR HDGDEPAAAI AESLAKLALD
110 120 130 140 150
QVDLYLVHWP TPAADNYVHA WEKMIELRAA GLTRSIGVSN HLVPHLERIV
160 170 180 190 200
AATGVVPAVN QIELHPAYQQ REITDWAAAH DVKIESWGPL GQGKYDLFGA
210 220 230 240 250
EPVTAAAAAH GKTPAQAVLR WHLQKGFVVF PKSVRRERLE ENLDVFDFDL
260 270
TDTEIAAIDA MDPGDGSGRV SAHPDEVD
Length:278
Mass (Da):30,119
Last modified:January 23, 2007 - v3
Checksum:i403A2E9AA4624A37
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12799 Genomic DNA. Translation: AAA83534.1.
PIRiI40838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12799 Genomic DNA. Translation: AAA83534.1 .
PIRi I40838.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A80 X-ray 2.10 A 2-278 [» ]
1HW6 X-ray 1.90 A 1-278 [» ]
1M9H X-ray 2.00 A 1-278 [» ]
ProteinModelPortali P06632.
SMRi P06632. Positions 2-278.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17833.
SABIO-RK P06632.

Miscellaneous databases

EvolutionaryTracei P06632.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Production of 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a genetically modified Erwinia herbicola."
    Anderson S., Marks C.B., Lazarus R.A., Miller J.V., Stafford K., Seymour J., Light D., Rastetter W., Estell D.A.
    Science 230:144-149(1985)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-41; 76-89; 97-123 AND 184-194, CHARACTERIZATION.
  2. "Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp."
    Miller J.V., Estell D.A., Lazarus R.A.
    J. Biol. Chem. 262:9016-9020(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-41, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
  3. "Molecular modeling of substrate binding in wild-type and mutant Corynebacteria 2,5-diketo-D-gluconate reductases."
    Khurana S., Sanli G., Powers D.B., Anderson S., Blaber M.
    Proteins 39:68-75(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF SUBSTRATE-BINDING SITE.
  4. "Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution."
    Khurana S., Powers D.B., Anderson S., Blaber M.
    Proc. Natl. Acad. Sci. U.S.A. 95:6768-6773(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  5. "Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor."
    Sanli G., Blaber M.
    J. Mol. Biol. 309:1209-1218(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  6. "Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase."
    Sanli G., Banta S., Anderson S., Blaber M.
    Protein Sci. 13:504-512(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT WITH TYR-22; GLY-232; HIS-238 AND GLY-272 IN COMPLEX WITH NADH.

Entry informationi

Entry nameiDKGA_CORSC
AccessioniPrimary (citable) accession number: P06632
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Modeling study indicates that the active site may not be optimized for 2,5-diketo-D-gluconic acid.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3