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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

Pgd

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 oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.By similarity

Catalytic activityi

6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041NADPBy similarity
Binding sitei104 – 1041SubstrateBy similarity
Active sitei184 – 1841Proton acceptorBy similarity
Active sitei191 – 1911Proton donorBy similarity
Binding sitei192 – 1921SubstrateBy similarity
Binding sitei259 – 2591Substrate; via amide nitrogenBy similarity
Binding sitei286 – 2861SubstrateBy similarity
Binding sitei445 – 4451Substrate; shared with dimeric partnerBy similarity
Binding sitei451 – 4511Substrate; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 166NADPBy similarity
Nucleotide bindingi34 – 363NADPBy similarity
Nucleotide bindingi76 – 783NADPBy similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. phosphogluconate dehydrogenase (decarboxylating) activity Source: UniProtKB-EC

GO - Biological processi

  1. D-gluconate metabolic process Source: UniProtKB-KW
  2. pentose-phosphate shunt Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization, Pentose shunt

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating (EC:1.1.1.44)
Gene namesi
Name:Pgd
OrganismiCeratitis capitata (Mediterranean fruit fly) (Tephritis capitata)
Taxonomic identifieri7213 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaTephritoideaTephritidaeCeratitisCeratitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4814816-phosphogluconate dehydrogenase, decarboxylatingPRO_0000090068Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP41570.
SMRiP41570. Positions 3-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 1323Substrate bindingBy similarity
Regioni187 – 1882Substrate bindingBy similarity

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_decarbox.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41570-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAKADIALI GLAVMGQNLV LNMNDKGFVV CAYNRTVEKV NQFLKNEAKG
60 70 80 90 100
TNVIGATSLQ DMVNKLKLPR KIMLLVKAGS AVDDFIQQLV PLLSPGDVII
110 120 130 140 150
DGGNSEYQDT ARRCDELRAK KILYVGSGVS GGEEGARHGP SLMPGGHPEA
160 170 180 190 200
WPLIQPIFQS ICAKADKEPC CEWVGEGGAG HFVKMVHNGI EYGDMQLICE
210 220 230 240 250
AYQIMKALGL SQAEMATEFE KWNSEELDSF LIEITRDILN YQDDRGYLLE
260 270 280 290 300
RIRDTAGQKG TGKWTAISAL QYGVPVTLIG EAVFSRCLSA LKDERVAASK
310 320 330 340 350
QLKGPNVNAK VEDLPKFLNH IKHALYCSKI VSYAQGFMLM REAAKENNWN
360 370 380 390 400
LNYGGIALMW RGGCIIRSVF LGNIKDAYTR NPQLSNLLLD DFFKKAIEVG
410 420 430 440 450
QNSWRQVVAN AFLWGIPVPA LSTALSFYDG YRTEKLPANL LQAQRDYFGA
460 470 480
HTYELLGAEG KFVHTNWTGT GGNVSASTYQ A
Length:481
Mass (Da):52,964
Last modified:November 1, 1995 - v1
Checksum:iF0ABB506AD1B86D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67873 mRNA. Translation: AAB29396.1.
RefSeqiNP_001266319.1. NM_001279390.1.

Genome annotation databases

GeneIDi101451876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67873 mRNA. Translation: AAB29396.1.
RefSeqiNP_001266319.1. NM_001279390.1.

3D structure databases

ProteinModelPortaliP41570.
SMRiP41570. Positions 3-472.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101451876.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_decarbox.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
PROSITEiPS00461. 6PGD. 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 namei6PGD_CERCA
AccessioniPrimary (citable) accession number: P41570
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 76 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.