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Protein

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

Gene

GPD

Organism
Leishmania mexicana
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei97NADBy similarity1
Binding sitei125NAD; via amide nitrogen2 Publications1
Binding sitei125Substrate1 Publication1
Binding sitei157NAD; via amide nitrogen2 Publications1
Active sitei210Proton acceptorCurated1
Binding sitei274NADBy similarity1
Binding sitei298NAD; via amide nitrogen2 Publications1
Binding sitei300NAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi22 – 27NAD2 Publications6

GO - Molecular functioni

GO - Biological processi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125K → A or M: Loss of activity. 1 Publication1
Mutagenesisi210K → A or M: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002622921 – 366Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomalAdd BLAST366

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 21Combined sources7
Helixi25 – 34Combined sources10
Turni35 – 37Combined sources3
Beta strandi38 – 44Combined sources7
Helixi48 – 57Combined sources10
Turni61 – 63Combined sources3
Beta strandi73 – 77Combined sources5
Helixi79 – 83Combined sources5
Beta strandi87 – 91Combined sources5
Helixi95 – 105Combined sources11
Helixi107 – 116Combined sources10
Beta strandi120 – 122Combined sources3
Turni129 – 131Combined sources3
Helixi135 – 139Combined sources5
Turni140 – 142Combined sources3
Helixi145 – 147Combined sources3
Beta strandi148 – 154Combined sources7
Helixi157 – 161Combined sources5
Beta strandi166 – 171Combined sources6
Helixi175 – 185Combined sources11
Beta strandi190 – 198Combined sources9
Helixi200 – 222Combined sources23
Helixi227 – 247Combined sources21
Turni253 – 256Combined sources4
Turni258 – 260Combined sources3
Helixi261 – 268Combined sources8
Helixi274 – 283Combined sources10
Helixi288 – 292Combined sources5
Helixi300 – 315Combined sources16
Helixi320 – 330Combined sources11
Helixi335 – 342Combined sources8
Helixi343 – 345Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP90551.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni274 – 275Substrate binding2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi364 – 366Microbody targeting signalSequence analysis3

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
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.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P90551-1 [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:
EMBLi
GenBanki
DDBJi
Links Updated
X89739 Genomic DNA. Translation: CAA61891.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89739 Genomic DNA. Translation: CAA61891.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP90551.

Miscellaneous databases

EvolutionaryTraceiP90551.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
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.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 94 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.