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Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 1

Gene

gpd1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei121NADBy similarity1
Binding sitei144NAD; via amide nitrogenBy similarity1
Binding sitei144SubstrateBy similarity1
Binding sitei177NAD; via amide nitrogenBy similarity1
Active sitei232Proton acceptorBy similarity1
Binding sitei296NADBy similarity1
Binding sitei325NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 34NADBy similarity6

GO - Molecular functioni

  • glycerol-3-phosphate dehydrogenase [NAD+] activity Source: PomBase
  • NAD binding Source: InterPro

GO - Biological processi

  • cellular response to osmotic stress Source: PomBase
  • cellular water homeostasis Source: PomBase
  • glycerol-3-phosphate catabolic process Source: InterPro
  • glycerol biosynthetic process Source: PomBase
  • NADH oxidation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-SPO-1483166. Synthesis of PA.
R-SPO-75109. Triglyceride Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)] 1 (EC:1.1.1.8)
Alternative name(s):
GPDH-C
Short name:
GPD-C
Gene namesi
Name:gpd1
ORF Names:SPBC215.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC215.05.
PomBaseiSPBC215.05. gpd1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • glycerol-3-phosphate dehydrogenase complex Source: InterPro
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001380951 – 385Glycerol-3-phosphate dehydrogenase [NAD(+)] 1Add BLAST385

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei376Phosphoserine1 Publication1
Modified residuei382Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP21696.
PRIDEiP21696.

PTM databases

iPTMnetiP21696.
SwissPalmiP21696.

Interactioni

Protein-protein interaction databases

BioGridi276983. 43 interactors.
MINTiMINT-4687624.

Structurei

3D structure databases

ProteinModelPortaliP21696.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni296 – 297Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000246855.
InParanoidiP21696.
KOiK00006.
OMAiCDTIKDH.
OrthoDBiEOG092C3ZQP.
PhylomeDBiP21696.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
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]
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGYGQQGVS AANIDSIRPK KRLSIGVVGS GNWGTAIAKI CGENARAHGH
60 70 80 90 100
HFRSKVRMWV FEEEIEYKGE KRKLTEVFNE AHENVKYLPG IECPPNVIAV
110 120 130 140 150
PDVREVARRA DILVFVVPHQ FIERVCDQMV GLIRPGAVGI SCIKGVAVSK
160 170 180 190 200
EGVRLYSEVI SEKLGIYCGV LSGANVANEV AREQFCETTI GFNPPNEVDI
210 220 230 240 250
PREQIAAVFD RPYFSVVSVD DVAGVALGGA LKNVVAMAVG FADGLEWGGN
260 270 280 290 300
TKAAIMRRGL LEMQKFATTF FDSDPRTMVE QSCGIADLVT SCLGGRNNRC
310 320 330 340 350
AEAFVKTGKS LETLEKELLG GQLLQGAATS KDVHEFLLTK DMVKDFPLFT
360 370 380
AVYNISYEDM DPKDLIIVLQ PLKEDSENEG GTETE
Length:385
Mass (Da):41,995
Last modified:January 11, 2001 - v2
Checksum:i8061C294196516E1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54 – 56SKV → GKG in CAA39630 (PubMed:2263480).Curated3
Sequence conflicti126 – 127CD → WH in CAA39630 (PubMed:2263480).Curated2
Sequence conflicti153Missing in CAA39630 (PubMed:2263480).Curated1
Sequence conflicti154R → S in CAA39630 (PubMed:2263480).Curated1
Sequence conflicti209F → S in CAA39630 (PubMed:2263480).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56162 Genomic DNA. Translation: CAA39630.1.
CU329671 Genomic DNA. Translation: CAA22119.1.
D50796 Genomic DNA. Translation: BAA09424.1.
PIRiT39895.
RefSeqiNP_596682.1. NM_001022605.2.

Genome annotation databases

EnsemblFungiiSPBC215.05.1; SPBC215.05.1:pep; SPBC215.05.
GeneIDi2540455.
KEGGispo:SPBC215.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56162 Genomic DNA. Translation: CAA39630.1.
CU329671 Genomic DNA. Translation: CAA22119.1.
D50796 Genomic DNA. Translation: BAA09424.1.
PIRiT39895.
RefSeqiNP_596682.1. NM_001022605.2.

3D structure databases

ProteinModelPortaliP21696.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276983. 43 interactors.
MINTiMINT-4687624.

PTM databases

iPTMnetiP21696.
SwissPalmiP21696.

Proteomic databases

MaxQBiP21696.
PRIDEiP21696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC215.05.1; SPBC215.05.1:pep; SPBC215.05.
GeneIDi2540455.
KEGGispo:SPBC215.05.

Organism-specific databases

EuPathDBiFungiDB:SPBC215.05.
PomBaseiSPBC215.05. gpd1.

Phylogenomic databases

HOGENOMiHOG000246855.
InParanoidiP21696.
KOiK00006.
OMAiCDTIKDH.
OrthoDBiEOG092C3ZQP.
PhylomeDBiP21696.

Enzyme and pathway databases

ReactomeiR-SPO-1483166. Synthesis of PA.
R-SPO-75109. Triglyceride Biosynthesis.

Miscellaneous databases

PROiP21696.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
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]
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGPD1_SCHPO
AccessioniPrimary (citable) accession number: P21696
Secondary accession number(s): O94310, P78927
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 145 of the entry and version 2 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.