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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

PGD

Organism
Sus scrofa (Pig)
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 sitei29 – 291Substrate; via amide nitrogenBy similarity
Binding sitei56 – 561SubstrateBy similarity
Binding sitei214 – 2141Substrate; shared with dimeric partnerBy similarity
Binding sitei220 – 2201Substrate; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi245 – 2484NADP; shared with dimeric partnerBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. D-gluconate metabolic process Source: UniProtKB-KW
  2. pentose-phosphate shunt Source: UniProtKB
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 250›2506-phosphogluconate dehydrogenase, decarboxylatingPRO_0000090065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP14332.
PRIDEiP14332.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003687.

Structurei

3D structure databases

ProteinModelPortaliP14332.
SMRiP14332. Positions 1-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0362.
HOGENOMiHOG000255147.
HOVERGENiHBG000029.
InParanoidiP14332.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P14332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IEITANILKF QDADGKHLLP KIRDSAGQKG TGKWTAISAL EYGVPVTLIG
60 70 80 90 100
EAVFARCLSS LKDERVQASK KLKGPQKIQF SGDKKSFLED IRKALYASKI
110 120 130 140 150
ISYTQGFMLL RQAAAEFGWS STTEHRLMWR GGCIIRSVFL GKIKDAFDRN
160 170 180 190 200
PGLQNLLLDD FFKSAVEDCQ DSWRRAVSTG VQTGIPMPCF TTALSFYDGY
210 220 230 240 250
RHEMLPANLI QAQRDYFGAH TYELLAKPGH FVHTNWTGHG GSVSSSSYNA
Length:250
Mass (Da):27,806
Last modified:October 10, 2003 - v3
Checksum:i8BBB0655D9A40C36
GO

Sequence cautioni

The sequence CAA34633.1 differs from that shown. Reason: Frameshift at positions 226 and 249. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16638 mRNA. Translation: CAA34633.1. Frameshift.
PIRiA48325.
UniGeneiSsc.30761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16638 mRNA. Translation: CAA34633.1. Frameshift.
PIRiA48325.
UniGeneiSsc.30761.

3D structure databases

ProteinModelPortaliP14332.
SMRiP14332. Positions 1-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003687.

Proteomic databases

PaxDbiP14332.
PRIDEiP14332.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0362.
HOGENOMiHOG000255147.
HOVERGENiHBG000029.
InParanoidiP14332.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation, characterization and chromosomal assignment of a partial cDNA for porcine 6-phosphogluconate dehydrogenase."
    Harbitz I., Chowdhary B., Chowdhary R., Kran S., Frengen E., Gustavsson I., Davies W.
    Hereditas 112:83-88(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Analysis of the gluconate (gnt) operon of Bacillus subtilis."
    Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.
    Mol. Microbiol. 5:1081-1089(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFTS.

Entry informationi

Entry namei6PGD_PIG
AccessioniPrimary (citable) accession number: P14332
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 10, 2003
Last modified: March 4, 2015
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.