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P10618

- G3P_METFE

UniProt

P10618 - G3P_METFE

Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

gap

Organism
Methanothermus fervidus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Exhibits a dual-cofactor specificity, with a marked preference for NADP+ over NAD+.

    Catalytic activityi

    D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei110 – 1101NADP; via amide nitrogen1 Publication
    Active sitei140 – 1401NucleophileBy similarity
    Binding sitei171 – 1711NADP1 Publication
    Binding sitei300 – 3001NADP; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 122NADP1 Publication
    Nucleotide bindingi34 – 352NADP1 Publication

    GO - Molecular functioni

    1. glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity Source: UniProtKB-EC
    2. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB-HAMAP
    3. glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity Source: CACAO
    4. NAD binding Source: InterPro
    5. NADP binding Source: InterPro

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    SABIO-RKP10618.
    UniPathwayiUPA00109; UER00184.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.59)
    Short name:
    GAPDH
    Alternative name(s):
    NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
    Gene namesi
    Name:gap
    OrganismiMethanothermus fervidus
    Taxonomic identifieri2180 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 337337Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145722Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Helixi13 – 219
    Beta strandi23 – 3513
    Helixi38 – 458
    Beta strandi50 – 545
    Helixi55 – 573
    Helixi58 – 636
    Helixi72 – 776
    Beta strandi80 – 845
    Helixi90 – 10112
    Beta strandi105 – 1073
    Helixi113 – 1164
    Helixi122 – 1254
    Helixi126 – 1294
    Beta strandi133 – 1375
    Helixi140 – 15617
    Beta strandi158 – 17013
    Beta strandi184 – 1918
    Helixi194 – 1996
    Beta strandi206 – 2149
    Beta strandi219 – 22911
    Helixi233 – 24210
    Beta strandi246 – 2494
    Turni251 – 2544
    Helixi258 – 26811
    Helixi271 – 2733
    Beta strandi277 – 2815
    Helixi282 – 2843
    Beta strandi286 – 2883
    Beta strandi291 – 2988
    Turni300 – 3034
    Helixi304 – 31512
    Helixi322 – 33312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CF2X-ray2.10O/P/Q/R1-337[»]
    ProteinModelPortaliP10618.
    SMRiP10618. Positions 1-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10618.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni139 – 1413Glyceraldehyde 3-phosphate bindingBy similarity
    Regioni194 – 1952Glyceraldehyde 3-phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    KOiK00150.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00559. G3P_dehdrog_arch.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006436. Glyceraldehyde-3-P_DH_2_arc.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01546. GAPDH-II_archae. 1 hit.
    PROSITEiPS00071. GAPDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10618-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAVAINGYG TVGKRVADAI AQQDDMKVIG VSKTRPDFEA RMALKKGYDL    50
    YVAIPERVKL FEKAGIEVAG TVDDMLDEAD IVIDCTPEGI GAKNLKMYKE 100
    KGIKAIFQGG EKHEDIGLSF NSLSNYEESY GKDYTRVVSC NTTGLCRTLK 150
    PLHDSFGIKK VRAVIVRRGA DPAQVSKGPI NAIIPNPPKL PSHHGPDVKT 200
    VLDINIDTMA VIVPTTLMHQ HNVMVEVEET PTVDDIIDVF EDTPRVILIS 250
    AEDGLTSTAE IMEYAKELGR SRNDLFEIPV WRESITVVDN EIYYMQAVHQ 300
    ESDIVPENVD AVRAILEMEE DKYKSINKTN KAMNILQ 337
    Length:337
    Mass (Da):37,408
    Last modified:July 1, 1989 - v1
    Checksum:iD83CBA88AAE5B0B8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19980 Genomic DNA. Translation: AAA88227.1.
    PIRiJT0286.
    RefSeqiYP_004003841.1. NC_014658.1.

    Genome annotation databases

    GeneIDi9961991.
    KEGGimfv:Mfer_0276.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19980 Genomic DNA. Translation: AAA88227.1 .
    PIRi JT0286.
    RefSeqi YP_004003841.1. NC_014658.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CF2 X-ray 2.10 O/P/Q/R 1-337 [» ]
    ProteinModelPortali P10618.
    SMRi P10618. Positions 1-336.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 9961991.
    KEGGi mfv:Mfer_0276.

    Phylogenomic databases

    KOi K00150.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00184 .
    SABIO-RK P10618.

    Miscellaneous databases

    EvolutionaryTracei P10618.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00559. G3P_dehdrog_arch.
    InterProi IPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006436. Glyceraldehyde-3-P_DH_2_arc.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000149. GAP_DH. 1 hit.
    SMARTi SM00846. Gp_dh_N. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01546. GAPDH-II_archae. 1 hit.
    PROSITEi PS00071. GAPDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from the nucleotide sequence of the thermophilic archaebacterium Methanothermus fervidus."
      Fabry S., Hensel R.
      Gene 64:189-197(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution."
      Charron C., Talfournier F., Isupov M.N., Littlechild J.A., Branlant G., Vitoux B., Aubry A.
      J. Mol. Biol. 297:481-500(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

    Entry informationi

    Entry nameiG3P_METFE
    AccessioniPrimary (citable) accession number: P10618
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

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

    External Data

    Dasty 3