Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P90551

- GPDA_LEIME

UniProt

P90551 - GPDA_LEIME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971NADBy similarity
Binding sitei125 – 1251NAD; via amide nitrogen2 Publications
Binding sitei125 – 1251Substrate1 Publication
Binding sitei157 – 1571NAD; via amide nitrogen2 Publications
Active sitei210 – 2101Proton acceptorCurated
Binding sitei274 – 2741NADBy similarity
Binding sitei298 – 2981NAD; via amide nitrogen2 Publications
Binding sitei300 – 3001NAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 276NAD2 Publications

GO - Molecular functioni

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

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-KW
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(+)], glycosomalPRO_0000262292Add
BLAST

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1
366
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP90551.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi364 – 3663Microbody targeting signalSequence Analysis

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTKQHSAKD ELLYLNKAVV FGSGAFGTAL AMVLSKKCRE VCVWHMNEEE
60 70 80 90 100
VRLVNEKREN VLFLKGVQLA SNITFTSDVE KAYNGAEIIL FVIPTQFLRG
110 120 130 140 150
FFEKSGGNLI AYAKEKQVPV LVCTKGIERS TLKFPAEIIG EFLPSPLLSV
160 170 180 190 200
LAGPSFAIEV ATGVFTCVSI ASADINVARR LQRIMSTGDR SFVCWATTDT
210 220 230 240 250
VGCEVASAVK NVLAIGSGVA NGLGMGLNAR AALIMRGLLE IRDLTAALGG
260 270 280 290 300
DGSAVFGLAG LGDLQLTCSS ELSRNFTVGK KLGKGLPIEE IQRTSKAVAE
310 320 330 340 350
GVATADPLMR LAKQLKVKMP LCHQIYEIVY KKKNPRDALA DLLSCGLQDE
360
GLPPLFKRSA STPSKL
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: October 29, 2014
This is version 85 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