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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene
N/A
Organism
Cyberlindnera jadinii (Torula yeast) (Pichia jadinii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.

Pathway: 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
  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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491NADPBy similarity
Binding sitei149 – 1491NADP; via carbonyl oxygenBy similarity
Binding sitei149 – 1491SubstrateBy similarity
Binding sitei217 – 2171SubstrateBy similarity
Binding sitei236 – 2361SubstrateBy similarity
Active sitei241 – 2411Proton acceptorBy similarity
Binding sitei335 – 3351SubstrateBy similarity
Binding sitei369 – 3691SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228NADPBy similarity

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
OrganismiCyberlindnera jadinii (Torula yeast) (Pichia jadinii)
Taxonomic identifieri4903 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeCyberlindnera

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Glucose-6-phosphate 1-dehydrogenasePRO_0000068105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylserine

Keywords - PTMi

Acetylation

Structurei

3D structure databases

ProteinModelPortaliP11410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni179 – 1835Substrate bindingBy similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11410-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SYDSFGDRVT IIVFGASGDL ARKKTFPALF GLFREKQLPS TVQIIGYARS
60 70 80 90 100
HLSDKDFKDY ISSHFKGGDD KTKEDFLNLC SYISDPYDTD EGYKKLEARC
110 120 130 140 150
QEYESKHNVK VPERLFYLAL PPSVFHTVCE QVKKNVYPKN EKSRIIIEKP
160 170 180 190 200
FGRDLETYRE LQKQISPLFT EDEVYRIDHY LGKEMVKNLL VLRFGNELFS
210 220 230 240 250
GIWNNKHITS VQISFKEAFG TEGRGGYFDN IGIIRDVMQN HLLQVLTLLT
260 270 280 290 300
MERPVSFDPE AVRDEKVKVL KAFDKIDVND VLLGQYGKSE DGTKPGYLDD
310 320 330 340 350
STVKPNSKAV TYAAFRVNIH NERWDGVPIV LRAGKALDEG KAEIRIQFKP
360 370 380 390 400
VAKGMFKEIQ RNELVIRIQP NEAIYLKINS KIPGISTETS LTDLDLTYST
410 420 430 440 450
RYSKDFWIPE AYEALIRDCY LGNHSNFVRD DELEVSWKLF TPLLEAVEKE
460 470 480 490
ENVKLESYPY GSKGPKELRK YLIDHGYVFN DPGTYQWPLT NTDVK
Length:495
Mass (Da):57,029
Last modified:April 1, 1993 - v2
Checksum:iB6944216F4B4C8D8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071H → G.
Natural varianti138 – 1381P → M.
Natural varianti416 – 4161I → T.

Sequence databases

PIRiS11078.
S29381.

Cross-referencesi

Sequence databases

PIRiS11078.
S29381.

3D structure databases

ProteinModelPortaliP11410.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure."
    Jeffery J., Persson B., Wood I., Bergman T., Jeffery R., Joernvall H.
    Eur. J. Biochem. 212:41-49(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine residue in the Pichia jadinii enzyme reveals a limited structural variation in a functionally significant segment."
    Jeffery J., Wood I., McLeod A., Jeffery R., Joernvall H.
    Biochem. Biophys. Res. Commun. 160:1290-1295(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 177-187.
    Strain: ATCC 9950 / CBS 5609 / DSM 2361 / NBRC 0998 / NRRL Y-900.
  3. "Alcoholytic deblocking of N-terminally acetylated peptides and proteins for sequence analysis."
    Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.
    FEBS Lett. 390:199-202(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10.

Entry informationi

Entry nameiG6PD_CYBJA
AccessioniPrimary (citable) accession number: P11410
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 1, 1993
Last modified: March 4, 2015
This is version 95 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

Direct protein sequencing

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.