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P63335 (6PGD_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
6-phosphogluconate dehydrogenase, decarboxylating
EC=1.1.1.44
Gene names
Name:gnd
Ordered Locus Names:MW1464
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Ontologies

Keywords
   Biological processGluconate utilization
Pentose shunt
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-gluconate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

phosphogluconate dehydrogenase (decarboxylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4684686-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090057

Regions

Nucleotide binding9 – 146NADP By similarity
Nucleotide binding32 – 343NADP By similarity
Nucleotide binding73 – 753NADP By similarity
Region127 – 1293Substrate binding By similarity
Region185 – 1862Substrate binding By similarity

Sites

Active site1821Proton acceptor By similarity
Active site1891Proton donor By similarity
Binding site1011NADP By similarity
Binding site1011Substrate By similarity
Binding site1901Substrate By similarity
Binding site2591Substrate; via amide nitrogen By similarity
Binding site2861Substrate By similarity
Binding site4441Substrate; shared with dimeric partner By similarity
Binding site4501Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
P63335 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 61A5C2CAF3CCD011

FASTA46851,803
        10         20         30         40         50         60 
MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV 

        70         80         90        100        110        120 
NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN 

       130        140        150        160        170        180 
FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY 

       190        200        210        220        230        240 
VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK 

       250        260        270        280        290        300 
LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK 

       310        320        330        340        350        360 
ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR 

       370        380        390        400        410        420 
EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF 

       430        440        450        460 
SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000033 Genomic DNA. Translation: BAB95329.1.
RefSeqNP_646281.1. NC_003923.1.

3D structure databases

ProteinModelPortalP63335.
SMRP63335. Positions 3-467.
ModBaseSearch...

Protein-protein interaction databases

STRING196620.MW1464.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB95329; BAB95329; BAB95329.
GeneID1003576.
KEGGsam:MW1464.
PATRIC19569536. VBIStaAur44266_1529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0362.
HOGENOMHOG000255147.
KOK00033.
OMAKQQIGVI.
ProtClustDBPRK09287.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-1488-MONOMER.
UniPathwayUPA00115; UER00410.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 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]
PfamPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFPIRSF000109. 6PGD. 1 hit.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR00873. gnd. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name6PGD_STAAW
AccessionPrimary (citable) accession number: P63335
Secondary accession number(s): Q99TY2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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