Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal - Trypanosoma brucei brucei

Contribute

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P90593 (GPDA_TRYBB)

Last modified June 16, 2009. Version 55. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal
EC=1.1.1.8

Gene names

Name:

GPD

Organism

Trypanosoma brucei brucei

Taxonomic identifier

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + NAD⁺ = glycerone phosphate + NADH.
Subcellular location	Glycosome.
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Cellular component	Glycosome
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro glycosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

354

Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal

PRO_0000138083

Regions

Nucleotide binding

6

NAD By similarity

Region

2

Substrate binding By similarity

Motif

3

Microbody targeting signal Potential

Sites

Active site

1

Proton acceptor By similarity

Binding site

1

NAD By similarity

Binding site

1

NAD; via amide nitrogen By similarity

Binding site

1

Substrate By similarity

Binding site

1

NAD; via amide nitrogen By similarity

Binding site

1

NAD By similarity

Binding site

1

NAD By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P90593-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 12CE19AEDA9E4EC9
Show »

354

37,783

        10         20         30         40         50         60 
MVSGVTYLKR GAVFGSGAFG TALACVLAKK CESVSVWHMN ANEARVVNQK HENVYFLPGA 

        70         80         90        100        110        120 
PLPANLTFTA DAEECAKGAE IVLFVIPTQF LRGFLQKNSH ILRNHVVSRN VPVVMCSKGI 

       130        140        150        160        170        180 
ERSSLLFPAQ ILEEFLPNYP IGVIAGPSFA IEVAKGMLTN VCTAAADINM ARKIQRIMTT 

       190        200        210        220        230        240 
SDGSFRCWAT TDVIGCEIAS AMKNVLAIAS GALKGLGTEN NARAALISRG LLEIRDLTLA 

       250        260        270        280        290        300 
LGGTGEAVFG LPGLGDLLLT CSSELSRNFT VGMKLGQGIS LEEIKRTSKA VAEGVATAEP 

       310        320        330        340        350 
LERLAKKHNA DLPICHEVYN VLYANGCAKR SFKKLNSCKL ADEGLPALPR TSKM

References

[1]

"Cloning and characterization of the NAD-linked glycerol-3-phosphate dehydrogenases of Trypanosoma brucei brucei and Leishmania mexicana mexicana and expression of the trypanosome enzyme in Escherichia coli."
Kohl L., Drmota T., Thi C.-D., Callens M., van Beeumen J., Opperdoes F.R., Michels P.A.M.
Mol. Biochem. Parasitol. 76:159-173(1996) [PubMed: 8920004] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 427.

Cross-references

Sequence databases
	X89738 Genomic DNA. Translation: CAA61890.1.
PIR	T48649.
3D structure databases
HSSP	HSSP built from PDB template 1EVY based on UniProtKB P90551.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.8. 74165.
Family and domain databases
InterPro	IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. IPR006168. NAD-dep_Gly3P_DH. IPR017751. NAD-dep_Gly3P_DH_euk. IPR011128. NAD-dep_Gly3P_DH_N. IPR006109. NAD_Gly3P_DH_C. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR11728. NAD_Gly3P_DH. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
ProDom	PD001278. NAD_Gly3P_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03376. glycerol3P_DH. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPDA_TRYBB

Accession

Primary (citable) accession number: P90593

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents