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Protein

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

Gene

dkgA

Organism
Corynebacterium sp. (strain ATCC 31090)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
    Active sitei50Proton donor1 Publication1
    Binding sitei108Substrate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi188 – 242NADP1 PublicationAdd BLAST55

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Ascorbate biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17833.
    BRENDAi1.1.1.274. 1664.
    1.1.1.346. 1664.
    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 lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium

    Subcellular locationi

    GO - Cellular componenti

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi22F → Y: Tighter binding of NADH. 1
    Mutagenesisi232K → G: Tighter binding of NADH. 1
    Mutagenesisi238R → H: Tighter binding of NADH. 1
    Mutagenesisi272A → G: Tighter binding of NADH. 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00001245972 – 2782,5-diketo-D-gluconic acid reductase AAdd BLAST277

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1278
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 7Combined sources3
    Beta strandi13 – 17Combined sources5
    Helixi26 – 28Combined sources3
    Helixi29 – 39Combined sources11
    Beta strandi43 – 45Combined sources3
    Helixi47 – 49Combined sources3
    Helixi54 – 63Combined sources10
    Helixi67 – 69Combined sources3
    Beta strandi71 – 76Combined sources6
    Helixi78 – 80Combined sources3
    Helixi86 – 97Combined sources12
    Beta strandi102 – 107Combined sources6
    Helixi112 – 114Combined sources3
    Helixi117 – 129Combined sources13
    Beta strandi132 – 140Combined sources9
    Helixi143 – 153Combined sources11
    Beta strandi158 – 163Combined sources6
    Helixi171 – 179Combined sources9
    Beta strandi183 – 188Combined sources6
    Helixi191 – 193Combined sources3
    Helixi201 – 210Combined sources10
    Helixi214 – 224Combined sources11
    Helixi236 – 243Combined sources8
    Helixi252 – 259Combined sources8
    Beta strandi264 – 266Combined sources3
    Turni274 – 276Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A80X-ray2.10A2-278[»]
    1HW6X-ray1.90A1-278[»]
    1M9HX-ray2.00A1-278[»]
    ProteinModelPortaliP06632.
    SMRiP06632.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06632.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    KOiK06221.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M12799 Genomic DNA. Translation: AAA83534.1.
    PIRiI40838.

    Genome annotation databases

    KEGGiag:AAA83534.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M12799 Genomic DNA. Translation: AAA83534.1.
    PIRiI40838.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A80X-ray2.10A2-278[»]
    1HW6X-ray1.90A1-278[»]
    1M9HX-ray2.00A1-278[»]
    ProteinModelPortaliP06632.
    SMRiP06632.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAA83534.

    Phylogenomic databases

    KOiK06221.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17833.
    BRENDAi1.1.1.274. 1664.
    1.1.1.346. 1664.
    SABIO-RKP06632.

    Miscellaneous databases

    EvolutionaryTraceiP06632.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    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]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 95 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.