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UniProtKB/Swiss-Prot entry P90551

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

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Entry information
Entry name GPDA_LEIME
Primary accession number P90551
Secondary accession numbers None
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on May 1, 1997 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 52)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal
Synonym EC 1.1.1.8
Gene name
Name: GPD
From
Leishmania mexicana [TaxID: 5665] 
Taxonomy Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
DOI=10.1016/0166-6851(95)02556-1; PubMed=8920004 [NCBI, ExPASy, EBI, Israel, Japan]
Kohl L., Drmota T., Thi C.-D., Callens M., van Beeumen J., Opperdoes F.R., Michels P.A.M.;
"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.";
Mol. Biochem. Parasitol. 76:159-173(1996).
[2]
 X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, AND SUBUNIT.
DOI=10.1016/S0969-2126(00)00135-0; PubMed=10801498 [NCBI, ExPASy, EBI, Israel, Japan]
Suresh S., Turley S., Opperdoes F.R., Michels P.A.M., Hol W.G.J.;
"A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana.";
Structure 8:541-552(2000).
[3]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD ANALOG.
DOI=10.1016/S1074-5521(02)00243-0; PubMed=12445769 [NCBI, ExPASy, EBI, Israel, Japan]
Choe J., Suresh S., Wisedchaisri G., Kennedy K.J., Gelb M.H., Hol W.G.J.;
"Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase.";
Chem. Biol. 9:1189-1197(2002).
[4]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, AND MUTAGENESIS OF LYS-125 AND LYS-210.
DOI=10.1016/S0022-2836(03)00421-2; PubMed=12758080 [NCBI, ExPASy, EBI, Israel, Japan]
Choe J., Guerra D., Michels P.A.M., Hol W.G.J.;
"Leishmania mexicana glycerol-3-phosphate dehydrogenase showed conformational changes upon binding a bi-substrate adduct.";
J. Mol. Biol. 329:335-349(2003).
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
X89739; CAA61891.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1EVY; X-ray; 1.75 A; A=1-366.[ExPASy / RCSB / EBI]
1EVZ; X-ray; 2.80 A; A=1-366.[ExPASy / RCSB / EBI]
1JDJ; X-ray; 2.20 A; A=1-366.[ExPASy / RCSB / EBI]
1M66; X-ray; 1.90 A; A=1-366.[ExPASy / RCSB / EBI]
1M67; X-ray; 2.50 A; A=1-366.[ExPASy / RCSB / EBI]
1N1E; X-ray; 1.90 A; A/B=1-366.[ExPASy / RCSB / EBI]
1N1G; X-ray; 2.50 A; A=1-366.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EVY; -.
1EVZ; -.
1JDJ; -.
1M66; -.
1M67; -.
1N1E; -.
1N1G; -.
ModBase P90551.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11728; NAD_Gly3P_DH; 1.
Pfam PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000114; Glycerol-3-P_dh; 1.
PRINTS PR00077; GPDHDRGNASE.
ProDom PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00957; NAD_G3PDH; 1.
BLOCKS P90551.
Other
ProtoNet P90551.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Glycosome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   366  366     Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal. PRO_0000262292
NP_BIND   22    27  6     NAD. 
REGION   274   275  2     Substrate binding. 
MOTIF   364   366  3     Microbody targeting signal (Potential). 
ACT_SITE   210   210        Proton acceptor (Probable). 
BINDING   97    97        NAD (By similarity). 
BINDING   125   125        NAD; via amide nitrogen. 
BINDING   125   125        Substrate. 
BINDING   157   157        NAD; via amide nitrogen. 
BINDING   274   274        NAD (By similarity). 
BINDING   298   298        NAD; via amide nitrogen. 
BINDING   300   300        NAD. 
MUTAGEN   125   125        K->A,M: Loss of activity. 
MUTAGEN   210   210        K->A,M: Loss of activity. 
STRAND   15    21  7      
HELIX   25    34  10      
TURN   35    37  3      
STRAND   38    44  7      
HELIX   48    57  10      
TURN   61    63  3      
STRAND   73    77  5      
HELIX   79    83  5      
STRAND   87    91  5      
HELIX   95   105  11      
HELIX   107   116  10      
STRAND   120   122  3      
TURN   129   131  3      
HELIX   135   139  5      
TURN   140   142  3      
HELIX   145   147  3      
STRAND   148   154  7      
HELIX   157   161  5      
STRAND   166   171  6      
HELIX   175   185  11      
STRAND   190   198  9      
HELIX   200   222  23      
HELIX   227   247  21      
TURN   253   256  4      
TURN   258   260  3      
HELIX   261   268  8      
HELIX   274   283  10      
HELIX   288   292  5      
HELIX   300   315  16      
HELIX   320   330  11      
HELIX   335   342  8      
HELIX   343   345  3      
STRAND   347   349  3      
Sequence information
Length: 366 AA [This is the length of the unprocessed precursor] Molecular weight: 39272 Da [This is the MW of the unprocessed precursor] CRC64: E47594525FC0CF44 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTKQHSAKD ELLYLNKAVV FGSGAFGTAL AMVLSKKCRE VCVWHMNEEE VRLVNEKREN 

        70         80         90        100        110        120 
VLFLKGVQLA SNITFTSDVE KAYNGAEIIL FVIPTQFLRG FFEKSGGNLI AYAKEKQVPV 

       130        140        150        160        170        180 
LVCTKGIERS TLKFPAEIIG EFLPSPLLSV LAGPSFAIEV ATGVFTCVSI ASADINVARR 

       190        200        210        220        230        240 
LQRIMSTGDR SFVCWATTDT VGCEVASAVK NVLAIGSGVA NGLGMGLNAR AALIMRGLLE 

       250        260        270        280        290        300 
IRDLTAALGG DGSAVFGLAG LGDLQLTCSS ELSRNFTVGK KLGKGLPIEE IQRTSKAVAE 

       310        320        330        340        350        360 
GVATADPLMR LAKQLKVKMP LCHQIYEIVY KKKNPRDALA DLLSCGLQDE GLPPLFKRSA 


STPSKL
P90551 in FASTA format

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