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 P55804


[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 DHGP_ASPNG
Primary accession number P55804
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 28)
Name and origin of the protein
Protein name NADP(+)-dependent glycerol dehydrogenase [Fragments]
Synonym EC 1.1.1.72
Gene name None
From
Aspergillus niger [TaxID: 5061] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
DOI=10.1074/jbc.272.9.5544; PubMed=9038161 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway.";
J. Biol. Chem. 272:5544-5554(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
3D structure databases
ModBase P55804.
Ontologies
GO
GO:0047956; Molecular function: glycerol dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
PANTHER PTHR11732; Aldo/ket_red; 1.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; PARTIAL.
PS00062; ALDOKETO_REDUCTASE_2; PARTIAL.
PS00063; ALDOKETO_REDUCTASE_3; PARTIAL.
BLOCKS P55804.
ProtoNet P55804.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   <1   >99  >99     NADP(+)-dependent glycerol dehydrogenase. PRO_0000124676
NON_CONS   19    20         
NON_CONS   38    39         
NON_CONS   52    53         
NON_CONS   64    65         
NON_CONS   70    71         
NON_CONS   85    86         
NON_TER   1     1         
NON_TER   99    99         
Sequence information
Length: 99 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 10672 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: 4BC9A366B8F75332 [This is a checksum on the sequence]
        10         20         30         40         50         60 
IPGVGFGTFA NEGATGXTYL KVDYIDLFLV HWPIAAEKAI GVSNWTIEGL EKENILPEAY 

        70         80         90 
SPLGIESNFK XGGYTLAQVL IAXGLSIQLT DXXYXAVNK 

P55804 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!