UniProtKB - Q00055 (GPD1_YEAST)
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Protein
Glycerol-3-phosphate dehydrogenase [NAD(+)] 1
Gene
GPD1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells.1 Publication
Miscellaneous
Present with 807 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 129 | NADBy similarity | 1 | |
Binding sitei | 152 | NAD; via amide nitrogenBy similarity | 1 | |
Binding sitei | 152 | SubstrateBy similarity | 1 | |
Binding sitei | 185 | NAD; via amide nitrogenBy similarity | 1 | |
Active sitei | 245 | Proton acceptorBy similarity | 1 | |
Binding sitei | 310 | NADBy similarity | 1 | |
Binding sitei | 339 | NADBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 41 – 46 | NADBy similarity | 6 |
GO - Molecular functioni
- glycerol-3-phosphate dehydrogenase [NAD+] activity Source: SGD
- NAD binding Source: InterPro
- protein homodimerization activity Source: InterPro
GO - Biological processi
- carbohydrate metabolic process Source: InterPro
- glycerol-3-phosphate catabolic process Source: InterPro
- intracellular accumulation of glycerol Source: SGD
- NADH oxidation Source: SGD
- protein import into peroxisome matrix Source: SGD
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Stress response |
Ligand | NAD |
Enzyme and pathway databases
BioCyci | MetaCyc:YDL022W-MONOMER. YEAST:YDL022W-MONOMER. |
BRENDAi | 1.1.1.8. 984. |
Reactomei | R-SCE-1483166. Synthesis of PA. |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:GPD1 Synonyms:DAR1, HOR1, OSG1 Ordered Locus Names:YDL022W ORF Names:D2830 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
EuPathDBi | FungiDB:YDL022W. |
SGDi | S000002180. GPD1. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000138100 | 2 – 391 | Glycerol-3-phosphate dehydrogenase [NAD(+)] 1Add BLAST | 390 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserine1 Publication | 1 | |
Modified residuei | 24 | PhosphoserineCombined sources | 1 | |
Modified residuei | 27 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
MaxQBi | Q00055. |
PaxDbi | Q00055. |
PRIDEi | Q00055. |
TopDownProteomicsi | Q00055. |
PTM databases
iPTMneti | Q00055. |
Expressioni
Inductioni
By osmotic stress and by methylglyoxal in a HOG pathway-dependent manner.2 Publications
Interactioni
GO - Molecular functioni
- protein homodimerization activity Source: InterPro
Protein-protein interaction databases
BioGridi | 32033. 88 interactors. |
DIPi | DIP-6393N. |
IntActi | Q00055. 5 interactors. |
MINTi | Q00055. |
STRINGi | 4932.YDL022W. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 35 – 40 | Combined sources | 6 | |
Helixi | 44 – 59 | Combined sources | 16 | |
Turni | 61 – 63 | Combined sources | 3 | |
Beta strandi | 64 – 71 | Combined sources | 8 | |
Beta strandi | 76 – 79 | Combined sources | 4 | |
Helixi | 82 – 86 | Combined sources | 5 | |
Turni | 87 – 89 | Combined sources | 3 | |
Turni | 93 – 95 | Combined sources | 3 | |
Beta strandi | 103 – 109 | Combined sources | 7 | |
Helixi | 111 – 115 | Combined sources | 5 | |
Beta strandi | 119 – 123 | Combined sources | 5 | |
Helixi | 127 – 129 | Combined sources | 3 | |
Helixi | 130 – 137 | Combined sources | 8 | |
Turni | 138 – 140 | Combined sources | 3 | |
Beta strandi | 146 – 149 | Combined sources | 4 | |
Beta strandi | 155 – 157 | Combined sources | 3 | |
Beta strandi | 160 – 162 | Combined sources | 3 | |
Helixi | 164 – 172 | Combined sources | 9 | |
Beta strandi | 175 – 180 | Combined sources | 6 | |
Helixi | 185 – 189 | Combined sources | 5 | |
Beta strandi | 194 – 199 | Combined sources | 6 | |
Beta strandi | 209 – 212 | Combined sources | 4 | |
Helixi | 215 – 222 | Combined sources | 8 | |
Beta strandi | 227 – 233 | Combined sources | 7 | |
Helixi | 235 – 257 | Combined sources | 23 | |
Helixi | 261 – 283 | Combined sources | 23 | |
Helixi | 289 – 294 | Combined sources | 6 | |
Turni | 296 – 298 | Combined sources | 3 | |
Helixi | 299 – 307 | Combined sources | 9 | |
Helixi | 310 – 320 | Combined sources | 11 | |
Helixi | 325 – 333 | Combined sources | 9 | |
Helixi | 340 – 354 | Combined sources | 15 | |
Helixi | 361 – 371 | Combined sources | 11 | |
Helixi | 379 – 383 | Combined sources | 5 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4FGW | X-ray | 2.45 | A/B | 1-391 | [»] | |
ProteinModelPortali | Q00055. | |||||
SMRi | Q00055. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 310 – 311 | Substrate bindingBy similarity | 2 |
Sequence similaritiesi
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.Curated
Phylogenomic databases
GeneTreei | ENSGT00390000003114. |
HOGENOMi | HOG000246855. |
InParanoidi | Q00055. |
KOi | K00006. |
OMAi | WLCKGFE. |
OrthoDBi | EOG092C3ZQP. |
Family and domain databases
Gene3Di | 1.10.1040.10. 1 hit. |
InterProi | View protein in InterPro IPR008927. 6-PGluconate_DH-like_C_sf. IPR013328. 6PGD_dom2. IPR006168. G3P_DH_NAD-dep. IPR006109. G3P_DH_NAD-dep_C. IPR017751. G3P_DH_NAD-dep_euk. IPR011128. G3P_DH_NAD-dep_N. IPR036291. NAD(P)-bd_dom_sf. |
Pfami | View protein in Pfam PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. |
PIRSFi | PIRSF000114. Glycerol-3-P_dh. 1 hit. |
PRINTSi | PR00077. GPDHDRGNASE. |
SUPFAMi | SSF48179. SSF48179. 1 hit. SSF51735. SSF51735. 1 hit. |
TIGRFAMsi | TIGR03376. glycerol3P_DH. 1 hit. |
PROSITEi | View protein in PROSITE PS00957. NAD_G3PDH. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q00055-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA
60 70 80 90 100
KVVAENCKGY PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT
110 120 130 140 150
LPDNLVANPD LIDSVKDVDI IVFNIPHQFL PRICSQLKGH VDSHVRAISC
160 170 180 190 200
LKGFEVGAKG VQLLSSYITE ELGIQCGALS GANIATEVAQ EHWSETTVAY
210 220 230 240 250
HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI CGALKNVVAL
260 270 280 290 300
GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA
310 320 330 340 350
DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW
360 370 380 390
LETCGSVEDF PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 103 – 107 | DNLVA → TIWLL in AAA18631 (PubMed:1676389).Curated | 5 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 16 | N → D in strain: WFB. 1 Publication | 1 | |
Natural varianti | 143 | S → A in strain: WFB. 1 Publication | 1 | |
Natural varianti | 164 | L → P in strain: WFB. 1 Publication | 1 | |
Natural varianti | 183 | N → S in strain: WFB. 1 Publication | 1 | |
Natural varianti | 225 | P → S in strain: WFB. 1 Publication | 1 | |
Natural varianti | 256 | E → V in strain: WFB. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z24454 Genomic DNA. Translation: CAA80827.1. X76859 Genomic DNA. Translation: CAA54189.1. U04621 Genomic DNA. Translation: AAA64936.1. AY598965 Genomic DNA. Translation: AAT27375.1. AY598968 Genomic DNA. Translation: AAT27378.1. Z48432 Genomic DNA. Translation: CAA88337.1. Z74071 Genomic DNA. Translation: CAA98582.1. EF596737 Genomic DNA. Translation: ABQ58864.1. M38740 Genomic DNA. Translation: AAA18631.1. BK006938 Genomic DNA. Translation: DAA11828.1. |
PIRi | S40059. |
RefSeqi | NP_010262.1. NM_001180081.1. |
Genome annotation databases
EnsemblFungii | YDL022W; YDL022W; YDL022W. |
GeneIDi | 851539. |
KEGGi | sce:YDL022W. |
Similar proteinsi
Entry informationi
Entry namei | GPD1_YEAST | |
Accessioni | Q00055Primary (citable) accession number: Q00055 Secondary accession number(s): A5YWB0 Q6J5J5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | January 23, 2007 | |
Last modified: | March 28, 2018 | |
This is version 183 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Caution
Was originally thought to be GUT2, the FAD-dependent glycerol-3-phosphate dehydrogenase.1 Publication