Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q759G5

- GPD_ASHGO

UniProt

Q759G5 - GPD_ASHGO

Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)]

Gene

GPD

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671NADBy similarity
    Binding sitei190 – 1901NAD; via amide nitrogenBy similarity
    Binding sitei190 – 1901SubstrateBy similarity
    Binding sitei223 – 2231NAD; via amide nitrogenBy similarity
    Active sitei283 – 2831Proton acceptorBy similarity
    Binding sitei348 – 3481NADBy similarity
    Binding sitei377 – 3771NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi79 – 846NADBy similarity

    GO - Molecular functioni

    1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: UniProtKB-EC
    2. NAD binding Source: InterPro

    GO - Biological processi

    1. glycerol-3-phosphate catabolic process Source: InterPro
    2. glycerol metabolic process Source: EnsemblFungi
    3. intracellular accumulation of glycerol Source: EnsemblFungi
    4. NADH oxidation Source: EnsemblFungi

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD(+)] (EC:1.1.1.8)
    Gene namesi
    Name:GPD
    Ordered Locus Names:ADR311C
    OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
    Taxonomic identifieri284811 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
    ProteomesiUP000000591: Chromosome IV

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EnsemblFungi
    2. glycerol-3-phosphate dehydrogenase complex Source: InterPro
    3. mitochondrion Source: EnsemblFungi
    4. nucleus Source: EnsemblFungi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Glycerol-3-phosphate dehydrogenase [NAD(+)]PRO_0000138085Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi33169.AGOS_ADR311C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ759G5.
    SMRiQ759G5. Positions 73-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni348 – 3492Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0240.
    HOGENOMiHOG000246855.
    KOiK00006.
    OMAiPVGEFIH.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR006168. G3P_DH_NAD-dep.
    IPR006109. G3P_DH_NAD-dep_C.
    IPR017751. G3P_DH_NAD-dep_euk.
    IPR011128. G3P_DH_NAD-dep_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11728. PTHR11728. 1 hit.
    PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
    PF01210. NAD_Gly3P_dh_N. 1 hit.
    [Graphical view]
    PRINTSiPR00077. GPDHDRGNASE.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
    PROSITEiPS00957. NAD_G3PDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q759G5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVNTTALIRS PTFVAQFRVL KQVNRGLFSQ TSYARTHART SYTHTMAGTD    50
    RLQQTSQILS RSTSSEIRLE RPFKVTVIGS GNWGTTIAKV VAENTQEYPQ 100
    LFERRVDMWV FEEQIEGRKL TEIINEQHEN VKYLPGITLP ENLVANPSVA 150
    AAAADADVLV FNIPHQFLGR IVEQLKGHVK PGARAISCLK GFSVGKDGVQ 200
    LLSTYIEEHL HIPCGALSGA NLAPEVAKGN WSETTVAYTL PQDFRGTGKD 250
    VDHAVLKKLF HRPYFHVNVV DDVAGISVAG ALKNVVALAC GFVLGLGWGN 300
    NAAAAVQRVG LSEMIKFARM FFPESKVETF YQESAGVADL ITTCAGGRNV 350
    RIGRAMAETG KSAQELEKEL LNGQSSQGIY TTQEVHEWLQ QCGKKDEFPL 400
    FEAVYKIVYE GVPMSKLPDM LEDA 424
    Length:424
    Mass (Da):46,646
    Last modified:July 5, 2004 - v1
    Checksum:i014C3D1A7F251630
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016817 Genomic DNA. Translation: AAS52231.1.
    RefSeqiNP_984407.1. NM_209760.1.

    Genome annotation databases

    EnsemblFungiiAAS52231; AAS52231; AGOS_ADR311C.
    GeneIDi4620680.
    KEGGiago:AGOS_ADR311C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016817 Genomic DNA. Translation: AAS52231.1 .
    RefSeqi NP_984407.1. NM_209760.1.

    3D structure databases

    ProteinModelPortali Q759G5.
    SMRi Q759G5. Positions 73-422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33169.AGOS_ADR311C.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii AAS52231 ; AAS52231 ; AGOS_ADR311C .
    GeneIDi 4620680.
    KEGGi ago:AGOS_ADR311C.

    Phylogenomic databases

    eggNOGi COG0240.
    HOGENOMi HOG000246855.
    KOi K00006.
    OMAi PVGEFIH.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR006168. G3P_DH_NAD-dep.
    IPR006109. G3P_DH_NAD-dep_C.
    IPR017751. G3P_DH_NAD-dep_euk.
    IPR011128. G3P_DH_NAD-dep_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11728. PTHR11728. 1 hit.
    Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
    PF01210. NAD_Gly3P_dh_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00077. GPDHDRGNASE.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR03376. glycerol3P_DH. 1 hit.
    PROSITEi PS00957. NAD_G3PDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
      Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
      Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
    2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
      Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
      G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

    Entry informationi

    Entry nameiGPD_ASHGO
    AccessioniPrimary (citable) accession number: Q759G5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3