Reviewed, UniProtKB/Swiss-Prot P55804 (DHGP_ASPNG)

Names and origin

Protein names	Recommended name:     NADP(+)-dependent glycerol dehydrogenase     EC=1.1.1.72
Organism	Aspergillus niger
Taxonomic identifier	5061 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	99 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Glycerol + NADP+ = D-glyceraldehyde + NADPH.
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glycerol dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›99	›99	NADP(+)-dependent glycerol dehydrogenase		PRO_0000124676
Experimental info
	Non-adjacent residues	19 – 20	2
	Non-adjacent residues	38 – 39	2
	Non-adjacent residues	52 – 53	2
	Non-adjacent residues	64 – 65	2
	Non-adjacent residues	70 – 71	2
	Non-adjacent residues	85 – 86	2
	Non-terminal residue	1	1
	Non-terminal residue	99	1

Sequences

	Sequence		Length	Mass (Da)
	P55804-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 4BC9A366B8F75332	FASTA	99	10,672
	10 20 30 40 50 60 IPGVGFGTFA NEGATGXTYL KVDYIDLFLV HWPIAAEKAI GVSNWTIEGL EKENILPEAY 70 80 90 SPLGIESNFK XGGYTLAQVL IAXGLSIQLT DXXYXAVNK

References

[1]

"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." Norbeck J., Blomberg A. J. Biol. Chem. 272:5544-5554(1997) [PubMed: 9038161] [Abstract] Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.72. 277.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. [Graphical view]
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
ProDom	PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. Partial match. PS00062. ALDOKETO_REDUCTASE_2. Partial match. PS00063. ALDOKETO_REDUCTASE_3. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHGP_ASPNG

Accession

Primary (citable) accession number: P55804

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)