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P90551

- GPDA_LEIME

UniProt

P90551 - GPDA_LEIME

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Protein
Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal
Gene
GPD
Organism
Leishmania mexicana
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971NAD By similarity
Binding sitei125 – 1251NAD; via amide nitrogen
Binding sitei125 – 1251Substrate
Binding sitei157 – 1571NAD; via amide nitrogen
Active sitei210 – 2101Proton acceptor Inferred
Binding sitei274 – 2741NAD By similarity
Binding sitei298 – 2981NAD; via amide nitrogen
Binding sitei300 – 3001NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 276NADUniRule annotation

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. glycerol-3-phosphate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP90551.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal (EC:1.1.1.8)
Gene namesi
Name:GPD
OrganismiLeishmania mexicana
Taxonomic identifieri5665 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

Glycosome 1 Publication

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
  2. glycosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1251K → A or M: Loss of activity. 1 Publication
Mutagenesisi210 – 2101K → A or M: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomalUniRule annotation
PRO_0000262292Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 217
Helixi25 – 3410
Turni35 – 373
Beta strandi38 – 447
Helixi48 – 5710
Turni61 – 633
Beta strandi73 – 775
Helixi79 – 835
Beta strandi87 – 915
Helixi95 – 10511
Helixi107 – 11610
Beta strandi120 – 1223
Turni129 – 1313
Helixi135 – 1395
Turni140 – 1423
Helixi145 – 1473
Beta strandi148 – 1547
Helixi157 – 1615
Beta strandi166 – 1716
Helixi175 – 18511
Beta strandi190 – 1989
Helixi200 – 22223
Helixi227 – 24721
Turni253 – 2564
Turni258 – 2603
Helixi261 – 2688
Helixi274 – 28310
Helixi288 – 2925
Helixi300 – 31516
Helixi320 – 33011
Helixi335 – 3428
Helixi343 – 3453

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVYX-ray1.75A1-366[»]
1EVZX-ray2.80A1-366[»]
1JDJX-ray2.20A1-366[»]
1M66X-ray1.90A1-366[»]
1M67X-ray2.50A1-366[»]
1N1EX-ray1.90A/B1-366[»]
1N1GX-ray2.50A1-366[»]
ProteinModelPortaliP90551.
SMRiP90551. Positions 9-357.

Miscellaneous databases

EvolutionaryTraceiP90551.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 2752Substrate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi364 – 3663Microbody targeting signal Reviewed prediction

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P90551-1 [UniParc]FASTAAdd to Basket

« Hide

MSTKQHSAKD ELLYLNKAVV FGSGAFGTAL AMVLSKKCRE VCVWHMNEEE    50
VRLVNEKREN VLFLKGVQLA SNITFTSDVE KAYNGAEIIL FVIPTQFLRG 100
FFEKSGGNLI AYAKEKQVPV LVCTKGIERS TLKFPAEIIG EFLPSPLLSV 150
LAGPSFAIEV ATGVFTCVSI ASADINVARR LQRIMSTGDR SFVCWATTDT 200
VGCEVASAVK NVLAIGSGVA NGLGMGLNAR AALIMRGLLE IRDLTAALGG 250
DGSAVFGLAG LGDLQLTCSS ELSRNFTVGK KLGKGLPIEE IQRTSKAVAE 300
GVATADPLMR LAKQLKVKMP LCHQIYEIVY KKKNPRDALA DLLSCGLQDE 350
GLPPLFKRSA STPSKL 366
Length:366
Mass (Da):39,272
Last modified:May 1, 1997 - v1
Checksum:iE47594525FC0CF44
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89739 Genomic DNA. Translation: CAA61891.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89739 Genomic DNA. Translation: CAA61891.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EVY X-ray 1.75 A 1-366 [» ]
1EVZ X-ray 2.80 A 1-366 [» ]
1JDJ X-ray 2.20 A 1-366 [» ]
1M66 X-ray 1.90 A 1-366 [» ]
1M67 X-ray 2.50 A 1-366 [» ]
1N1E X-ray 1.90 A/B 1-366 [» ]
1N1G X-ray 2.50 A 1-366 [» ]
ProteinModelPortali P90551.
SMRi P90551. Positions 9-357.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P90551.

Miscellaneous databases

EvolutionaryTracei P90551.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPi MF_00394. NAD_Glyc3P_dehydrog.
InterProi IPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11728. PTHR11728. 1 hit.
Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSi PR00077. GPDHDRGNASE.
SUPFAMi SSF48179. SSF48179. 1 hit.
PROSITEi PS00957. NAD_G3PDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  2. "A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana."
    Suresh S., Turley S., Opperdoes F.R., Michels P.A.M., Hol W.G.J.
    Structure 8:541-552(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.
  3. "Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase."
    Choe J., Suresh S., Wisedchaisri G., Kennedy K.J., Gelb M.H., Hol W.G.J.
    Chem. Biol. 9:1189-1197(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD ANALOG.
  4. "Leishmania mexicana glycerol-3-phosphate dehydrogenase showed conformational changes upon binding a bi-substrate adduct."
    Choe J., Guerra D., Michels P.A.M., Hol W.G.J.
    J. Mol. Biol. 329:335-349(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, MUTAGENESIS OF LYS-125 AND LYS-210.

Entry informationi

Entry nameiGPDA_LEIME
AccessioniPrimary (citable) accession number: P90551
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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