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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

ZW

Organism
Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841NADP 1By similarity
Binding sitei184 – 1841NADP 1; via carbonyl oxygenBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Binding sitei252 – 2521SubstrateBy similarity
Binding sitei271 – 2711SubstrateBy similarity
Active sitei276 – 2761Proton acceptorBy similarity
Binding sitei370 – 3701NADP 2By similarity
Binding sitei373 – 3731SubstrateBy similarity
Binding sitei378 – 3781SubstrateBy similarity
Binding sitei379 – 3791NADP 2By similarity
Binding sitei383 – 3831NADP 2By similarity
Binding sitei406 – 4061NADP 2By similarity
Binding sitei408 – 4081SubstrateBy similarity
Binding sitei500 – 5001NADP 2By similarity
Binding sitei516 – 5161NADP 2By similarity
Binding sitei522 – 5221NADP 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 578NADP 1By similarity
Nucleotide bindingi414 – 4163NADP 2By similarity
Nucleotide bindingi434 – 4363NADP 2By 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
Alternative name(s):
Zwischenferment
Gene namesi
Name:ZW
OrganismiCeratitis capitata (Mediterranean fruit fly) (Tephritis capitata)
Taxonomic identifieri7213 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaTephritoideaTephritidaeCeratitisCeratitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 526526Glucose-6-phosphate 1-dehydrogenasePRO_0000068090Add
BLAST

Proteomic databases

PRIDEiP41571.

Structurei

3D structure databases

ProteinModelPortaliP41571.
SMRiP41571. Positions 44-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni214 – 2185Substrate 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.

P41571-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATQHFTNGS ATDDGETALE HIIKSLETPT MKCEGTHFDS HVPHTFVIFG
60 70 80 90 100
ASGDLAKKKI YPTLWWLYRD NLLPKSTKFC GYARSKLTIE ELRAKCHQYM
110 120 130 140 150
KVQPDEQAKY EEFWQNHDYA AGSYDQRSDF VALKERLSSL ESCNCSCNRI
160 170 180 190 200
FYLALPPSVF ERVTVNIKDI CLAERGWNRV IIEKPFGRDD VTSKKLSDHL
210 220 230 240 250
ASLFHEDQLY RIDHYLGKEM VQNLMTIRFA NKILNSTWNR ENIASVLITF
260 270 280 290 300
KEPFGTQGRG GYFDEFGIIR DVMQNHLLQI LSLVAMEKPT SCQPDDIRDE
310 320 330 340 350
KVKVLKSIPA LTLDDMVLGQ YVGNPNGVGE QREGYLDDPT VSNDSNTPTY
360 370 380 390 400
AQGVLRINNE RWDGVPFILR CGKALDERKA VVRIQYRDVP GDIFEGNSKR
410 420 430 440 450
NELVIRVQPG EALYFKMMTK SPGITFDIEE TELDLTYEHR YKNSYLPDAY
460 470 480 490 500
ERLILDVFCG SQMHFVRSDE LSEAWRIFTP VLNEIENNKV KPIPYVFGSR
510 520
GPKEADQKTS ENNFKYYGSY KWIGKK
Length:526
Mass (Da):60,592
Last modified:November 1, 1995 - v1
Checksum:i4047EBF7444C4917
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67872 mRNA. Translation: AAB29395.1.
RefSeqiNP_001266304.1. NM_001279375.1.

Genome annotation databases

GeneIDi101453374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67872 mRNA. Translation: AAB29395.1.
RefSeqiNP_001266304.1. NM_001279375.1.

3D structure databases

ProteinModelPortaliP41571.
SMRiP41571. Positions 44-518.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP41571.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101453374.

Organism-specific databases

CTDi32974.

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. "Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase from the mediterranean fruit fly Ceratitis capitata: correlating genetic and physical maps of chromosome 5."
    Scott M.J., Kriticou D., Robinson A.S.
    Insect Mol. Biol. 1:213-222(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiG6PD_CERCA
AccessioniPrimary (citable) accession number: P41571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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.