ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O60037


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name 6PGD_CUNEL
Primary accession number O60037
Secondary accession numbers None
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name 6-phosphogluconate dehydrogenase, decarboxylating
Synonym EC 1.1.1.44
Gene name
Name: 6-PGD
From
Cunninghamella elegans [TaxID: 4853] 
Taxonomy Eukaryota; Fungi; Fungi incertae sedis; Basal fungal lineages; Mucoromycotina; Mucorales; Cunninghamellaceae; Cunninghamella.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 36112 / DSM 8217;
DOI=10.1111/j.1574-6968.1998.tb13346.x; PubMed=9868787 [NCBI, ExPASy, EBI, Israel, Japan]
Wang R.F., Khan A.A., Cao W.W., Cerniglia C.E.;
"Identification and sequencing of a cDNA encoding 6-phosphogluconate dehydrogenase from a fungus, Cunninghamella elegans and expression of the gene in Escherichia coli.";
FEMS Microbiol. Lett. 169:397-402(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y17297; CAA76734.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P00349; 2PGD. [HSSP ENTRY / PDB]
SMR O60037; 4-476.
ModBase O60037.
Ontologies
GO
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004616; Molecular function: phosphogluconate dehydrogenase (decarboxylating) activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006098; Biological process: pentose-phosphate shunt (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006183; 6-phosphogluconate_DHase.
IPR006114; 6PGDH_C.
IPR006113; 6PGDH_decarbox.
IPR006115; 6PGDH_NAD-bd.
IPR006184; 6PGdom_BS.
IPR013328; DHase_multihelical.
IPR012284; Fibritin/6PGD_C-extension.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
Pfam PF00393; 6PGD; 1.
PF03446; NAD_binding_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00076; 6PGDHDRGNASE.
TIGRFAMs TIGR00873; gnd; 1.
PROSITE PS00461; 6PGD; 1.
Other
ProtoNet O60037.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
NADP; Oxidoreductase; Pentose shunt.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   485  485     6-phosphogluconate dehydrogenase, decarboxylating. PRO_0000090073
Sequence information
Length: 485 AA [This is the length of the unprocessed precursor] Molecular weight: 53102 Da [This is the MW of the unprocessed precursor] CRC64: F7E6DDFF3D21EFB2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVEAVADIGL IGLAVMGQNL ILNMNDHGFV VCAYNRTTSK VDDFLANEAK GTNVVGAHSV 

        70         80         90        100        110        120 
EELCAKLKRP RKVMLLVKAG SAVDAFIDQL LPHLEEGDII IDGGNSHFPD SIRRTKELEA 

       130        140        150        160        170        180 
KGILFVGSGV SGGEEGARYG PSLMPGGNSK AWEHIQPIFQ AIAAKAPDGA SCCEWVGETG 

       190        200        210        220        230        240 
AGHYVKMVHN GIEYGDMQLI TEVYQILHEG LGLSHDEMAD IFEEWNKGDL DSFLIEITRD 

       250        260        270        280        290        300 
ILRFKDTDGQ PLVTKIRDTA GQKGTGKWTA IDSLDRGIPV TLIGEAVYSR CLSSLKDERV 

       310        320        330        340        350        360 
RASKILQGPS SSKFTGDKKT FIAQLGQALY AAKIVSYAQG YMLMRQAAKD YEWKLNNAGI 

       370        380        390        400        410        420 
ALMWRGGCII RSVFLGKIRD AYTKNPELEN LLFDDFFKDA TAKAQDAWRN VTAQAVLMGI 

       430        440        450        460        470        480 
PTPALSTALN FYDGLRHEIL PANLLQAQRD YFGAHTYELL HTPGKWVHTN WTGRGGNVSA 


STYDA 

O60037 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!