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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861NADP 1By similarity
Binding sitei101 – 1011SubstratePROSITE-ProRule annotation
Active sitei106 – 1061Proton acceptorBy similarity
Binding sitei163 – 1631NADP 2By similarity
Binding sitei179 – 1791NADP 2By similarity
Binding sitei185 – 1851NADP 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 458NADP 1By similarity

GO - Molecular functioni

  1. glucose-6-phosphate dehydrogenase activity Source: UniProtKB
  2. NADP binding Source: InterPro

GO - Biological processi

  1. glucose 6-phosphate metabolic process Source: UniProtKB
  2. NADP metabolic process Source: UniProtKB
  3. pentose-phosphate shunt Source: UniProtKB-UniPathway
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 191190Glucose-6-phosphate 1-dehydrogenasePRO_0000068082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei173 – 1731N6-acetyllysineBy similarity

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

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.
SMRiP15588. Positions 27-191.
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]

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)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi52 – 532Curated
Non-adjacent residuesi100 – 1012Curated
Non-adjacent residuesi131 – 1322Curated

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.
SMRiP15588. Positions 27-191.
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]
ProtoNetiSearch...

Publicationsi

  1. "Molecular studies of marsupial X chromosomes reveal limited sequence homology of mammalian X-linked genes."
    Kaslow D.C., Migeon B.R., Persico M.G., Zollo M., Vandeberg J.L., Samollow P.B.
    Genomics 1:19-28(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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 1, 2014
This is version 85 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

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.