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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NADPUniRule annotation
Binding sitei49 – 491NADPCurated
Binding sitei105 – 1051SubstrateUniRule annotation
Binding sitei141 – 1411NADP; via amide nitrogenUniRule annotation
Active sitei192 – 1921Proton acceptorUniRule annotation
Binding sitei259 – 2591NADPUniRule annotation
Binding sitei289 – 2891NADPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 126NADPUniRule annotation

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

BioCyciAFUL224325:GJBC-890-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Glycerol-3-phosphate dehydrogenase [NAD(P)+]PRO_0000138068Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224325.AF0871.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi10 – 2213Combined sources
Beta strandi25 – 295Combined sources
Helixi32 – 343Combined sources
Helixi35 – 428Combined sources
Turni48 – 503Combined sources
Beta strandi56 – 605Combined sources
Helixi62 – 643Combined sources
Helixi65 – 695Combined sources
Beta strandi73 – 775Combined sources
Helixi81 – 833Combined sources
Helixi84 – 918Combined sources
Turni92 – 943Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi113 – 1164Combined sources
Helixi117 – 1226Combined sources
Helixi129 – 1313Combined sources
Beta strandi132 – 1387Combined sources
Helixi141 – 1455Combined sources
Beta strandi150 – 1556Combined sources
Helixi159 – 16911Combined sources
Beta strandi174 – 1807Combined sources
Helixi182 – 20928Combined sources
Helixi214 – 23522Combined sources
Helixi239 – 2435Combined sources
Turni245 – 2473Combined sources
Helixi248 – 2536Combined sources
Turni254 – 2563Combined sources
Helixi258 – 26811Combined sources
Helixi273 – 28210Combined sources
Helixi289 – 30315Combined sources
Helixi309 – 31911Combined sources
Helixi324 – 3329Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO29390.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni259 – 2602Substrate bindingUniRule annotation

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.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXGX-ray1.70A/B1-335[»]
ProteinModelPortaliO29390.
SMRiO29390. Positions 1-335.
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.
BioCyciAFUL224325:GJBC-890-MONOMER.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: a glycerol-3-phosphate dehydrogenase with an unusual NADP+ preference."
    Sakasegawa S., Hagemeier C.H., Thauer R.K., Essen L.-O., Shima S.
    Protein Sci. 13:3161-3171(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

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: December 9, 2015
This is version 123 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.