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

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: Annotation score: 3 out of 5-Protein inferred from homologyi

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiQ759G5.
KOiK00006.
OMAiEVANDNF.

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

        10         20         30         40         50
MVNTTALIRS PTFVAQFRVL KQVNRGLFSQ TSYARTHART SYTHTMAGTD
60 70 80 90 100
RLQQTSQILS RSTSSEIRLE RPFKVTVIGS GNWGTTIAKV VAENTQEYPQ
110 120 130 140 150
LFERRVDMWV FEEQIEGRKL TEIINEQHEN VKYLPGITLP ENLVANPSVA
160 170 180 190 200
AAAADADVLV FNIPHQFLGR IVEQLKGHVK PGARAISCLK GFSVGKDGVQ
210 220 230 240 250
LLSTYIEEHL HIPCGALSGA NLAPEVAKGN WSETTVAYTL PQDFRGTGKD
260 270 280 290 300
VDHAVLKKLF HRPYFHVNVV DDVAGISVAG ALKNVVALAC GFVLGLGWGN
310 320 330 340 350
NAAAAVQRVG LSEMIKFARM FFPESKVETF YQESAGVADL ITTCAGGRNV
360 370 380 390 400
RIGRAMAETG KSAQELEKEL LNGQSSQGIY TTQEVHEWLQ QCGKKDEFPL
410 420
FEAVYKIVYE GVPMSKLPDM LEDA
Length:424
Mass (Da):46,646
Last modified:July 5, 2004 - v1
Checksum:i014C3D1A7F251630
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE016817 Genomic DNA. Translation: AAS52231.1.
RefSeqiNP_984407.1. NM_209760.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi33169.AGOS_ADR311C.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0240.
HOGENOMiHOG000246855.
InParanoidiQ759G5.
KOiK00006.
OMAiEVANDNF.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 84 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

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 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.