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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

gsdA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.

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 (gsdA), Glucose-6-phosphate 1-dehydrogenase (ABL_10158)
  2. no protein annotated in this organism
  3. 6-phosphogluconate dehydrogenase, decarboxylating (ABL_05082), 6-phosphogluconate dehydrogenase, decarboxylating (gndA), 6-phosphogluconate dehydrogenase, decarboxylating (ABL_04763)
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 sitei63NADPBy similarity1
Binding sitei164NADP; via carbonyl oxygenBy similarity1
Binding sitei164SubstrateBy similarity1
Binding sitei232SubstrateBy similarity1
Binding sitei251SubstrateBy similarity1
Active sitei256Proton acceptorBy similarity1
Binding sitei350SubstrateBy similarity1
Binding sitei384SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 36NADPBy 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:gsdA
Synonyms:g6pdh
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000681021 – 510Glucose-6-phosphate 1-dehydrogenaseAdd BLAST510

Proteomic databases

PaxDbiP48826.
PRIDEiP48826.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00002664.

Structurei

3D structure databases

ProteinModelPortaliP48826.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 198Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0563. Eukaryota.
COG0364. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTIARTEE RQNAGTMELK DDTVIIVLGA SGDLAKKKTF PALFGLYRNK
60 70 80 90 100
FLPKGIKIVG YARTNMDHEE YLRRVRSYIK TPTKEIEEQL DSFCQFCTYI
110 120 130 140 150
SGQYDKDDSF INLNKHLEEI EKGQKEQNRI YYMALPPSVF TTVSDQLKRN
160 170 180 190 200
CYPKNGVARI IVEKPFGKDL QSSRDLQKAL EPNWKEEEIF RIDHYLGKEM
210 220 230 240 250
VKNILIMRFG NEFFNATWNR HHIDNVQITF KEPFGTEGRG GYFDEFGIIR
260 270 280 290 300
DVMQNHLLQV LTLLAMERPI SFSAEDIRDE KVRVLRAMDA IEPKNVIIGQ
310 320 330 340 350
YGKSLDGSKP AYKEDETVPQ DSRCPTFCAM VAYIKNERWD GVPFIMKAGK
360 370 380 390 400
ALNEQKTEIR IQFRDVTSGI FKDIPRNELV IRVQPNESVY IKMNSKLPGL
410 420 430 440 450
SMQTVVTELD LTYRRRFSDL KIPEAYESLI LDALKGDHSN FVRDDELDAS
460 470 480 490 500
WRIFTPLLHY LDDNKEIIPM EYPYGSRGPA VLDDFTASFG YKFSDAAGYQ
510
WPLTSTPNRL
Length:510
Mass (Da):58,950
Last modified:February 1, 1996 - v1
Checksum:iFDDF3F5025483AF6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135L → F in CAA54840 (PubMed:7753033).Curated1
Sequence conflicti508 – 510NRL → TVCK in CAA54840 (PubMed:7753033).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87942 mRNA. Translation: CAA61194.1.
X77829 Genomic DNA. Translation: CAA54840.1.
PIRiS54720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87942 mRNA. Translation: CAA61194.1.
X77829 Genomic DNA. Translation: CAA54840.1.
PIRiS54720.

3D structure databases

ProteinModelPortaliP48826.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00002664.

Proteomic databases

PaxDbiP48826.
PRIDEiP48826.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0563. Eukaryota.
COG0364. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG6PD_ASPNG
AccessioniPrimary (citable) accession number: P48826
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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.