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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

G6PD

Organism
Didelphis virginiana (North American opossum) (Didelphis marsupialis virginiana)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).By similarity

Catalytic activityi

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.

Pathwayi: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glucose-6-phosphate 1-dehydrogenase (G6PD)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei86NADP 1By similarity1
Binding sitei101SubstratePROSITE-ProRule annotation1
Active sitei106Proton acceptorBy similarity1
Binding sitei163NADP 2By similarity1
Binding sitei179NADP 2By similarity1
Binding sitei185NADP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi38 – 45NADP 1By similarity8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase (EC:1.1.1.49)
Short name:
G6PD
Gene namesi
Name:G6PD
OrganismiDidelphis virginiana (North American opossum) (Didelphis marsupialis virginiana)
Taxonomic identifieri9267 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDidelphimorphiaDidelphidaeDidelphis

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000680822 – 191Glucose-6-phosphate 1-dehydrogenaseAdd BLAST190

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei8PhosphoserineBy similarity1
Modified residuei10PhosphothreonineBy similarity1
Modified residuei173N6-acetyllysineBy similarity1
Modified residuei179PhosphotyrosineBy similarity1

Post-translational modificationi

Acetylated by ELP3; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2; deacetylation stimulates its enzyme activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

Homotetramer; dimer of dimers. Interacts with SIRT2; the interaction is enhanced by H2O2 treatment (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP15588.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR001282. G6P_DH.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 2 hits.
PF00479. G6PD_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Fragments.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15588-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQVALSRT QVCGILREEL YQGDAFHQSD THIFIIMGAS GDLAKKKIYP
60 70 80 90 100
TIEPASFQRL NTHMNSLHHG AQANRLFYLA LPPIVYEAVT KNIKETCMSQ
110 120 130 140 150
DVMQNHLLQM LCLVAMEKPA STNSDDVRDE KDELQEAWRI FTPLLHHIER
160 170 180 190
EKTQPIPYVY GSRGPPEADE LMKRVGFQYE GTYKWVNPHK L
Length:191
Mass (Da):21,941
Last modified:April 1, 1990 - v1
Checksum:iE838F22AA83F4AFD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-adjacent residuesi52 – 53Curated2
Non-adjacent residuesi100 – 101Curated2
Non-adjacent residuesi131 – 132Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19637, M19636 Genomic DNA. Translation: AAA30971.1.
M19642 Genomic DNA. Translation: AAA30972.1. Sequence problems.
M19638 Genomic DNA. Translation: AAA30973.1.
M19639 Genomic DNA. Translation: AAA30974.1.
M19641, M19640 Genomic DNA. Translation: AAA30975.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19637, M19636 Genomic DNA. Translation: AAA30971.1.
M19642 Genomic DNA. Translation: AAA30972.1. Sequence problems.
M19638 Genomic DNA. Translation: AAA30973.1.
M19639 Genomic DNA. Translation: AAA30974.1.
M19641, M19640 Genomic DNA. Translation: AAA30975.1.

3D structure databases

ProteinModelPortaliP15588.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR001282. G6P_DH.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 2 hits.
PF00479. G6PD_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiG6PD_DIDVI
AccessioniPrimary (citable) accession number: P15588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 5, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.