Skip Header

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

Glyceraldehyde-3-phosphate dehydrogenase 2

Gene

gap2

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.1 Publication

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.1 Publication

Enzyme regulationi

Inhibited by pentalenolactone.1 Publication

Kineticsi

kcat is 165 sec(-1) with D-glyceraldehyde 3-phosphate.1 Publication

  1. KM=0.33 mM for D-glyceraldehyde 3-phosphate1 Publication

    Pathwayi: glycolysis

    This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Curated
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Glyceraldehyde-3-phosphate dehydrogenase 1 (gap1), Glyceraldehyde-3-phosphate dehydrogenase 2 (gap2)
    2. Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
    4. Enolase (eno)
    5. Pyruvate kinase (pykA2), Pyruvate kinase (pykA1)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351NADBy similarity
    Binding sitei79 – 791NAD; via carbonyl oxygenBy similarity
    Binding sitei121 – 1211NADBy similarity
    Active sitei153 – 1531NucleophileBy similarity
    Sitei180 – 1801Activates thiol group during catalysisBy similarity
    Binding sitei183 – 1831Glyceraldehyde 3-phosphateBy similarity
    Binding sitei184 – 1841NADBy similarity
    Binding sitei198 – 1981Glyceraldehyde 3-phosphateBy similarity
    Binding sitei234 – 2341Glyceraldehyde 3-phosphateBy similarity
    Binding sitei316 – 3161NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 132NADBy similarity

    GO - Molecular functioni

    • glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
    • NAD binding Source: UniProtKB
    • NADP binding Source: InterPro

    GO - Biological processi

    • glucose metabolic process Source: InterPro
    • glycolytic process Source: UniProtKB-UniPathway
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSAVE227882:GJU1-6377-MONOMER.
    UniPathwayiUPA00109; UER00184.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 21 Publication (EC:1.2.1.121 Publication)
    Short name:
    GAPDH 21 Publication
    Alternative name(s):
    NAD-dependent glyceraldehyde-3-phosphate dehydrogenase1 Publication
    PL-sensitive glyceraldehyde-3-phosphate dehydrogenase1 Publication
    Gene namesi
    Name:gap2
    Ordered Locus Names:SAV_6296
    OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
    Taxonomic identifieri227882 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
    Proteomesi
    • UP000000428 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335Glyceraldehyde-3-phosphate dehydrogenase 2PRO_0000422015Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi227882.SAV_6296.

    Structurei

    3D structure databases

    ProteinModelPortaliQ829W3.
    SMRiQ829W3. Positions 3-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 1543Glyceraldehyde 3-phosphate bindingBy similarity
    Regioni211 – 2122Glyceraldehyde 3-phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C17. Bacteria.
    COG0057. LUCA.
    HOGENOMiHOG000071679.
    KOiK00134.
    OMAiFVRVLSW.
    OrthoDBiEOG66TG3S.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10836. PTHR10836. 1 hit.
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    PRINTSiPR00078. G3PDHDRGNASE.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q829W3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTIRVGINGF GRIGRNYFRA LLEQGADIEI VAVNDLGDTA TTAHLLKYDT
    60 70 80 90 100
    ILGRLKAEVT HTADTITVDG KTIKVFSERN PADIPWGELN VDIVIESTGI
    110 120 130 140 150
    FTKKADAEKH IAGGAKKVLI SAPASDEDIT IVLGVNEDKY DPAKHNVISN
    160 170 180 190 200
    ASCTTNCVAP MAKVLDENFG IVKGLMTTIH AYTNDQRILD FPHKDLRRAR
    210 220 230 240 250
    AAAENIIPTT TGAAKATALV LPQLKGKMDG ISMRVPVPTG SATDLVVEVS
    260 270 280 290 300
    REVTKDEVNA AFKKAAEGEL QGYLSYTEDP IVSSDIVGDP SSCTFDSAMT
    310 320 330
    MVMEGTSVKI LGWYDNEWGY SNRLVDLTVF VGNQL
    Length:335
    Mass (Da):36,162
    Last modified:June 1, 2003 - v1
    Checksum:i8A006B5A173776B7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000030 Genomic DNA. Translation: BAC74007.1.
    RefSeqiWP_010987697.1. NZ_JZJK01000089.1.

    Genome annotation databases

    EnsemblBacteriaiBAC74007; BAC74007; SAV_6296.
    KEGGisma:SAV_6296.
    PATRICi23726648. VBIStrAve112782_6676.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000030 Genomic DNA. Translation: BAC74007.1.
    RefSeqiWP_010987697.1. NZ_JZJK01000089.1.

    3D structure databases

    ProteinModelPortaliQ829W3.
    SMRiQ829W3. Positions 3-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi227882.SAV_6296.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAC74007; BAC74007; SAV_6296.
    KEGGisma:SAV_6296.
    PATRICi23726648. VBIStrAve112782_6676.

    Phylogenomic databases

    eggNOGiENOG4105C17. Bacteria.
    COG0057. LUCA.
    HOGENOMiHOG000071679.
    KOiK00134.
    OMAiFVRVLSW.
    OrthoDBiEOG66TG3S.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00184.
    BioCyciSAVE227882:GJU1-6377-MONOMER.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10836. PTHR10836. 1 hit.
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    PRINTSiPR00078. G3PDHDRGNASE.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
      Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
      Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680.
    2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
      Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
      Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680.
    3. "A gene cluster for biosynthesis of the sesquiterpenoid antibiotic pentalenolactone in Streptomyces avermitilis."
      Tetzlaff C.N., You Z., Cane D.E., Takamatsu S., Omura S., Ikeda H.
      Biochemistry 45:6179-6186(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680.

    Entry informationi

    Entry nameiG3P2_STRAW
    AccessioniPrimary (citable) accession number: Q829W3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2013
    Last sequence update: June 1, 2003
    Last modified: March 16, 2016
    This is version 95 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

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.