P14332 (6PGD_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating
EC=1.1.1.44

Gene names

Name:

PGD

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	250 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH By similarity.
Catalytic activity	6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the 6-phosphogluconate dehydrogenase family.
Sequence caution	The sequence CAA34633.1 differs from that shown. Reason: Frameshift at positions 226 and 249.

Ontologies

Keywords
Biological process	Gluconate utilization Pentose shunt
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 250	›250	6-phosphogluconate dehydrogenase, decarboxylating		PRO_0000090065
Regions
	Nucleotide binding	245 – 248	4	NADP; shared with dimeric partner By similarity
Sites
	Binding site	29	1	Substrate; via amide nitrogen By similarity
	Binding site	56	1	Substrate By similarity
	Binding site	214	1	Substrate; shared with dimeric partner By similarity
	Binding site	220	1	Substrate; shared with dimeric partner By similarity
Amino acid modifications
	Modified residue	77	1	N6-acetyllysine By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P14332 [UniParc]. Last modified October 10, 2003. Version 3. Checksum: 8BBB0655D9A40C36	FASTA	250	27,806
	10 20 30 40 50 60 IEITANILKF QDADGKHLLP KIRDSAGQKG TGKWTAISAL EYGVPVTLIG EAVFARCLSS 70 80 90 100 110 120 LKDERVQASK KLKGPQKIQF SGDKKSFLED IRKALYASKI ISYTQGFMLL RQAAAEFGWS 130 140 150 160 170 180 STTEHRLMWR GGCIIRSVFL GKIKDAFDRN PGLQNLLLDD FFKSAVEDCQ DSWRRAVSTG 190 200 210 220 230 240 VQTGIPMPCF TTALSFYDGY RHEMLPANLI QAQRDYFGAH TYELLAKPGH FVHTNWTGHG 250 GSVSSSSYNA

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16638 mRNA. Translation: CAA34633.1. Frameshift.
PIR	A48325.
UniGene	Ssc.30761.
3D structure databases
ProteinModelPortal	P14332.
SMR	P14332. Positions 1-241.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000003687.
Proteomic databases
PaxDb	P14332.
PRIDE	P14332.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG0362.
HOGENOM	HOG000255147.
HOVERGEN	HBG000029.
OrthoDB	EOG4C2H9D.
Enzyme and pathway databases
UniPathway	UPA00115; UER00410.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit. 1.20.5.320. 1 hit.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR006114. 6PGDH_C. IPR006184. 6PGdom_BS. IPR013328. DH_multihelical. IPR012284. Fibritin/6PGD_C-extension. [Graphical view]
Pfam	PF00393. 6PGD. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
PROSITE	PS00461. 6PGD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

6PGD_PIG

Accession

Primary (citable) accession number: P14332

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 10, 2003
Last modified:	April 3, 2013
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program