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Protein

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

Gene

gpsA

Organism
Staphylococcus aureus (strain COL)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

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 sitei106 – 1061NAD; via amide nitrogenUniRule annotation
Binding sitei106 – 1061SubstrateUniRule annotation
Binding sitei141 – 1411NAD; via amide nitrogenUniRule annotation
Active sitei192 – 1921Proton acceptorUniRule annotation
Binding sitei256 – 2561NADUniRule annotation
Binding sitei282 – 2821NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 136NADUniRule 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

NAD

Enzyme and pathway databases

BioCyciSAUR93062:GCEP-1483-MONOMER.
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:SACOL1514
OrganismiStaphylococcus aureus (strain COL)
Taxonomic identifieri93062 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000530 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Glycerol-3-phosphate dehydrogenase [NAD(P)+]PRO_0000138023Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL1514.

Structurei

3D structure databases

ProteinModelPortaliQ5HFU9.
SMRiQ5HFU9. Positions 6-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni256 – 2572Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CSF. Bacteria.
COG0240. LUCA.
HOGENOMiHOG000246854.
KOiK00057.
OMAiRNHTAGR.

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.

Q5HFU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKITVFGMG SFGTALANVL AENGHDVLMW GKNQDAVDEL NTCHTNKKYL
60 70 80 90 100
KYAKLDVNII ATSDMTKAIQ FADIYLMALP TKAMREVASQ INDKLTSKKT
110 120 130 140 150
FIHVAKGIEN GTFKRVSEMI EDSISPEYNA GIGVLSGPSH AEEVVVKQPT
160 170 180 190 200
TVAASSKDKS VSKLTQDLFM NDYLRVYTND DLIGVELGGA LKNIIAVASG
210 220 230 240 250
IVAGIGYGDN AKAALMTRGL AEISRLGEKL GADPMTFLGL GGIGDLIVTC
260 270 280 290 300
TSTHSRNFTL GYKLGQGESM DQALSEMNMV VEGIYTTKSV YHLAKEKNVD
310 320 330
MPITNALYRV LFENISVKEC VKDLMERDKK SE
Length:332
Mass (Da):36,071
Last modified:February 15, 2005 - v1
Checksum:iF1D44E7E0DD002F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW36709.1.
RefSeqiWP_000161738.1. NC_002951.2.

Genome annotation databases

EnsemblBacteriaiAAW36709; AAW36709; SACOL1514.
KEGGisac:SACOL1514.
PATRICi19529245. VBIStaAur112458_1477.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW36709.1.
RefSeqiWP_000161738.1. NC_002951.2.

3D structure databases

ProteinModelPortaliQ5HFU9.
SMRiQ5HFU9. Positions 6-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1514.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW36709; AAW36709; SACOL1514.
KEGGisac:SACOL1514.
PATRICi19529245. VBIStaAur112458_1477.

Phylogenomic databases

eggNOGiENOG4105CSF. Bacteria.
COG0240. LUCA.
HOGENOMiHOG000246854.
KOiK00057.
OMAiRNHTAGR.

Enzyme and pathway databases

UniPathwayiUPA00940.
BioCyciSAUR93062:GCEP-1483-MONOMER.

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_STAAC
AccessioniPrimary (citable) accession number: Q5HFU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: September 7, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.