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Protein

Glycerol-3-phosphate dehydrogenase [NAD(P)+]

Gene

gpsA

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H.UniRule annotation

Kineticsi

  1. KM=40 µM for NADPH1 Publication
  2. KM=1 mM for dihydroxyacetone phosphate1 Publication
  1. Vmax=44 µmol/min/mg enzyme1 Publication

Temperature dependencei

Optimum temperature is 70 degrees Celsius.1 Publication

Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33NADPUniRule annotation1
Binding sitei49NADPCurated1
Binding sitei105SubstrateUniRule annotation1
Binding sitei141NADP; via amide nitrogenUniRule annotation1
Active sitei192Proton acceptorUniRule annotation1
Binding sitei259NADPUniRule annotation1
Binding sitei289NADPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 12NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

SABIO-RKO29390.
UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(P)+]UniRule annotation (EC:1.1.1.94UniRule annotation)
Alternative name(s):
NAD(P)H-dependent glycerol-3-phosphate dehydrogenaseUniRule annotation
Gene namesi
Name:gpsAUniRule annotation
Ordered Locus Names:AF_0871
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001380681 – 335Glycerol-3-phosphate dehydrogenase [NAD(P)+]Add BLAST335

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224325.AF0871.

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi10 – 22Combined sources13
Beta strandi25 – 29Combined sources5
Helixi32 – 34Combined sources3
Helixi35 – 42Combined sources8
Turni48 – 50Combined sources3
Beta strandi56 – 60Combined sources5
Helixi62 – 64Combined sources3
Helixi65 – 69Combined sources5
Beta strandi73 – 77Combined sources5
Helixi81 – 83Combined sources3
Helixi84 – 91Combined sources8
Turni92 – 94Combined sources3
Beta strandi99 – 102Combined sources4
Beta strandi106 – 110Combined sources5
Beta strandi113 – 116Combined sources4
Helixi117 – 122Combined sources6
Helixi129 – 131Combined sources3
Beta strandi132 – 138Combined sources7
Helixi141 – 145Combined sources5
Beta strandi150 – 155Combined sources6
Helixi159 – 169Combined sources11
Beta strandi174 – 180Combined sources7
Helixi182 – 209Combined sources28
Helixi214 – 235Combined sources22
Helixi239 – 243Combined sources5
Turni245 – 247Combined sources3
Helixi248 – 253Combined sources6
Turni254 – 256Combined sources3
Helixi258 – 268Combined sources11
Helixi273 – 282Combined sources10
Helixi289 – 303Combined sources15
Helixi309 – 319Combined sources11
Helixi324 – 332Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TXGX-ray1.70A/B1-335[»]
ProteinModelPortaliO29390.
SMRiO29390.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO29390.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni259 – 260Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00456. Archaea.
COG0240. LUCA.
KOiK00057.
OMAiPCTSYEL.

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.

Sequencei

Sequence statusi: Complete.

O29390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVSILGAGA MGSALSVPLV DNGNEVRIWG TEFDTEILKS ISAGREHPRL
60 70 80 90 100
GVKLNGVEIF WPEQLEKCLE NAEVVLLGVS TDGVLPVMSR ILPYLKDQYI
110 120 130 140 150
VLISKGLIDF DNSVLTVPEA VWRLKHDLRE RTVAITGPAI AREVAKRMPT
160 170 180 190 200
TVVFSSPSES SANKMKEIFE TEYFGVEVTT DIIGTEITSA LKNVYSIAIA
210 220 230 240 250
WIRGYESRKN VEMSNAKGVI ATRAINEMAE LIEILGGDRE TAFGLSGFGD
260 270 280 290 300
LIATFRGGRN GMLGELLGKG LSIDEAMEEL ERRGVGVVEG YKTAEKAYRL
310 320 330
SSKINADTKL LDSIYRVLYE GLKVEEVLFE LATFK
Length:335
Mass (Da):36,785
Last modified:January 1, 1998 - v1
Checksum:iE6B87240B92BD059
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90367.1.
PIRiG69358.
RefSeqiWP_010878372.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90367; AAB90367; AF_0871.
GeneIDi24794469.
KEGGiafu:AF_0871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90367.1.
PIRiG69358.
RefSeqiWP_010878372.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TXGX-ray1.70A/B1-335[»]
ProteinModelPortaliO29390.
SMRiO29390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90367; AAB90367; AF_0871.
GeneIDi24794469.
KEGGiafu:AF_0871.

Phylogenomic databases

eggNOGiarCOG00456. Archaea.
COG0240. LUCA.
KOiK00057.
OMAiPCTSYEL.

Enzyme and pathway databases

UniPathwayiUPA00940.
SABIO-RKO29390.

Miscellaneous databases

EvolutionaryTraceiO29390.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiGPDA_ARCFU
AccessioniPrimary (citable) accession number: O29390
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has a strong preference for NADP over NAD.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.