SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q29492

- G6PD_MACRO

UniProt

Q29492 - G6PD_MACRO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glucose-6-phosphate 1-dehydrogenase
Gene
G6PD
Organism
Macropus robustus (Wallaroo) (Euro)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721NADP 1 By similarity
Binding sitei147 – 1471NADP 1 By similarity
Binding sitei171 – 1711NADP 1; via carbonyl oxygen By similarity
Binding sitei171 – 1711Substrate By similarity
Binding sitei239 – 2391Substrate By similarity
Binding sitei258 – 2581Substrate By similarity
Active sitei263 – 2631Proton acceptor By similarity
Binding sitei357 – 3571NADP 2 By similarity
Binding sitei360 – 3601Substrate By similarity
Binding sitei365 – 3651Substrate By similarity
Binding sitei366 – 3661NADP 2 By similarity
Binding sitei370 – 3701NADP 2 By similarity
Binding sitei393 – 3931NADP 2 By similarity
Binding sitei395 – 3951Substrate By similarity
Binding sitei487 – 4871NADP 2 By similarity
Binding sitei503 – 5031NADP 2 By similarity
Binding sitei509 – 5091NADP 2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 458NADP 1 By similarity
Nucleotide bindingi401 – 4033NADP 2 By similarity
Nucleotide bindingi421 – 4233NADP 2 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. NADP metabolic process Source: UniProtKB
  2. glucose 6-phosphate 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
OrganismiMacropus robustus (Wallaroo) (Euro)
Taxonomic identifieri9319 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDiprotodontiaMacropodidaeMacropus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 515514Glucose-6-phosphate 1-dehydrogenaseUniRule annotation
PRO_0000068084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei89 – 891N6-acetyllysine By similarity
Modified residuei171 – 1711N6-acetyllysine By similarity
Modified residuei403 – 4031N6-acetyllysine By similarity
Modified residuei432 – 4321N6-acetyllysine By similarity
Modified residuei497 – 4971N6-acetyllysine By similarity

Post-translational modificationi

Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity By similarity.

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ29492.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ29492.
SMRiQ29492. Positions 28-515.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2055Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000856.

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.

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

Q29492-1 [UniParc]FASTAAdd to Basket

« Hide

MAEQVALSRT QVCGILREEL YQGDAFHQSD THIFIIMGAS GDLAKKKIYP    50
TIWWLFRDGL LPEDTFIVGY ARSNLTVDDI RKQSEPYFKA TPEENLKLEE 100
FFSRNSYVAG QYDEPASFQR LNAHMNSLHH GSQANRLFYL ALPPTVYEAV 150
TKNIKETCMS QIGWNRVIVE KPFGKDLQSS DKLSNHISSL FHEDQIYRID 200
HYLGKEMVQN LMVLRFGNRI FGPIWNRDNI ACVIFTFKEP FGTLGRGGYF 250
DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVRA 300
TDVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD 350
GVPFILRCGK ALNERKAEVR LQFRDVAGDI FQRQCKRNEL VIRVQPNEAV 400
YTKMMTKKPG MFFNPEESEL DLTYGNRYKD VKLPDAYERL ILDVFCGSQM 450
HFVRSDELRE AWRIFTPLLH HIEKEKTQPI AYVYGSRGPP EADELMKRVG 500
FQYEGTYKWV NPHKL 515
Length:515
Mass (Da):59,315
Last modified:January 23, 2007 - v3
Checksum:iD49BA95185A78952
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13899 mRNA. Translation: AAA76599.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13899 mRNA. Translation: AAA76599.1 .

3D structure databases

ProteinModelPortali Q29492.
SMRi Q29492. Positions 28-515.
ModBasei Search...

Proteomic databases

PRIDEi Q29492.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000856.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00408 .

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00966. G6PD.
InterProi IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23429. PTHR23429. 1 hit.
Pfami PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000110. G6PD. 1 hit.
PRINTSi PR00079. G6PDHDRGNASE.
TIGRFAMsi TIGR00871. zwf. 1 hit.
PROSITEi PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Full-length cDNA sequence of X-linked G6PD of an Australian marsupial, the wallaroo."
    Loebel D.A., Longhurst T.J., Johnston P.G.
    Mamm. Genome 6:198-201(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiG6PD_MACRO
AccessioniPrimary (citable) accession number: Q29492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 83 of the entry and version 3 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