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P37754

- 6PGD9_ECOLX

UniProt

P37754 - 6PGD9_ECOLX

Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

gnd

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.By similarity

    Catalytic activityi

    6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021NADPBy similarity
    Binding sitei102 – 1021SubstrateBy similarity
    Active sitei183 – 1831Proton acceptorBy similarity
    Active sitei190 – 1901Proton donorBy similarity
    Binding sitei191 – 1911SubstrateBy similarity
    Binding sitei260 – 2601Substrate; via amide nitrogenBy similarity
    Binding sitei287 – 2871SubstrateBy similarity
    Binding sitei445 – 4451Substrate; shared with dimeric partnerBy similarity
    Binding sitei451 – 4511Substrate; shared with dimeric partnerBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156NADPBy similarity
    Nucleotide bindingi33 – 353NADPBy similarity
    Nucleotide bindingi74 – 763NADPBy similarity

    GO - Molecular functioni

    1. NADP binding Source: InterPro
    2. phosphogluconate dehydrogenase (decarboxylating) activity Source: UniProtKB

    GO - Biological processi

    1. D-gluconate metabolic process Source: UniProtKB-KW
    2. pentose-phosphate shunt Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Gluconate utilization, Pentose shunt

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00115; UER00410.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphogluconate dehydrogenase, decarboxylating (EC:1.1.1.44)
    Gene namesi
    Name:gnd
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4684686-phosphogluconate dehydrogenase, decarboxylatingPRO_0000090038Add
    BLAST

    Proteomic databases

    PaxDbiP37754.
    PRIDEiP37754.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP37754.
    SMRiP37754. Positions 1-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni128 – 1303Substrate bindingBy similarity
    Regioni186 – 1872Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0362.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR006114. 6PGDH_C.
    IPR006113. 6PGDH_decarbox.
    IPR006115. 6PGDH_NADP-bd.
    IPR006184. 6PGdom_BS.
    IPR013328. DH_multihelical.
    IPR012284. Fibritin/6PGD_C-extension.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000109. 6PGD. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR00873. gnd. 1 hit.
    PROSITEiPS00461. 6PGD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P37754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK    50
    LVPYYTVQEF VESLETPRRI LLMVKAGSGT DSAIDSLKPY LDKGDIIIDG 100
    GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE 150
    LVAPILKQIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA 200
    YALLKGGLTL SNEELAQTFT EWNEGELSSY LYDITKDIFT KKDEEGKYLV 250
    DVILDEAANK GTGKWTSQSS LDLGEPLSLI TESVFPRYIS SLKDQRVAAS 300
    KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYNWE 350
    LNYAEIAKIF RAGCIIRAQF LQKITDAYAQ NAGIANLLLA PYFKQIADDY 400
    QQALRDVVAY AVQNGIRVPT FSAAIAYYDS YRSAVLPANL IQAQRDYFGA 450
    HTYKRTDKEG VFHTEWLE 468
    Length:468
    Mass (Da):51,625
    Last modified:October 1, 1994 - v1
    Checksum:iC13D94CFD78BFF3A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27646 Genomic DNA. Translation: AAA21136.1.
    PIRiI41250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27646 Genomic DNA. Translation: AAA21136.1 .
    PIRi I41250.

    3D structure databases

    ProteinModelPortali P37754.
    SMRi P37754. Positions 1-466.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P37754.
    PRIDEi P37754.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0362.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00410 .

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR006114. 6PGDH_C.
    IPR006113. 6PGDH_decarbox.
    IPR006115. 6PGDH_NADP-bd.
    IPR006184. 6PGdom_BS.
    IPR013328. DH_multihelical.
    IPR012284. Fibritin/6PGD_C-extension.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000109. 6PGD. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00873. gnd. 1 hit.
    PROSITEi PS00461. 6PGD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide."
      Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C.
      J. Bacteriol. 176:3126-3139(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: O9:K30:H12 / E69.

    Entry informationi

    Entry namei6PGD9_ECOLX
    AccessioniPrimary (citable) accession number: P37754
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3