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Protein

Glycerol-1-phosphate dehydrogenase [NAD(P)+]

Gene

egsA

Organism
Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.UniRule annotation

Catalytic activityi

sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.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)DescriptionActionsGraphical viewLength
Binding sitei124SubstrateUniRule annotation1
Binding sitei128NADUniRule annotation1
Metal bindingi171Zinc; catalyticUniRule annotation1
Binding sitei171SubstrateUniRule annotation1
Metal bindingi251Zinc; catalyticUniRule annotation1
Binding sitei255SubstrateUniRule annotation1
Metal bindingi267Zinc; catalyticUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi97 – 101NADUniRule annotation5
Nucleotide bindingi119 – 122NADUniRule annotation4

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

Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-1-phosphate dehydrogenase [NAD(P)+]UniRule annotation (EC:1.1.1.261UniRule annotation)
Short name:
G1P dehydrogenaseUniRule annotation
Short name:
G1PDHUniRule annotation
Alternative name(s):
Enantiomeric glycerophosphate synthaseUniRule annotation
sn-glycerol-1-phosphate dehydrogenaseUniRule annotation
Gene namesi
Name:egsAUniRule annotation
Ordered Locus Names:M1425_1382
OrganismiSulfolobus islandicus (strain M.14.25 / Kamchatka #1)
Taxonomic identifieri427317 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001350 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002064791 – 351Glycerol-1-phosphate dehydrogenase [NAD(P)+]Add BLAST351

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliC3MVE1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycerol-1-phosphate dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000228570.
KOiK00096.
OMAiYSEYAAH.

Family and domain databases

CDDicd08173. Gro1PDH. 1 hit.
HAMAPiMF_00497_A. G1P_dehydrogenase_A. 1 hit.
InterProiIPR023002. G1P_dehydrogenase_arc.
IPR032837. G1PDH.
[Graphical view]
PfamiPF13685. Fe-ADH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C3MVE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVKEHVISL PRRVFVGHDI IYDISIYFSQ LGITSPFLIV TGTKYTKKIA
60 70 80 90 100
DKVIENLPKD AKYEVIEIDT ATLDDVYKVE EVVKKVNPNI LLGIGGGKVI
110 120 130 140 150
DVTKYAAFRN NLEFVSIPTS PSHDGITSPF ASIKGLQKPV SVKAKEPLAI
160 170 180 190 200
IADIEILSLS PRRLINAGIG DTIGKIIAVR DWRLAAKLRG EYYGDYTASL
210 220 230 240 250
ALMSAKHAFQ CTKIINKDIK YGVRMLIEAL ISSGVAMGMA GSTRPASGSE
260 270 280 290 300
HLFAHAVELL HPEGVLHGEL VGLGTIIMAY LHGINWKIIR DRLKKIGFPV
310 320 330 340 350
KAKDLGLSDE EVIKALTIAH TIRPERYTIL GDRGLTWSSA EKIARVTKII

D
Length:351
Mass (Da):38,549
Last modified:June 16, 2009 - v1
Checksum:i19228161FEC430A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001400 Genomic DNA. Translation: ACP38136.1.
RefSeqiWP_012711381.1. NC_012588.1.

Genome annotation databases

EnsemblBacteriaiACP38136; ACP38136; M1425_1382.
GeneIDi7814193.
KEGGisia:M1425_1382.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001400 Genomic DNA. Translation: ACP38136.1.
RefSeqiWP_012711381.1. NC_012588.1.

3D structure databases

ProteinModelPortaliC3MVE1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACP38136; ACP38136; M1425_1382.
GeneIDi7814193.
KEGGisia:M1425_1382.

Phylogenomic databases

HOGENOMiHOG000228570.
KOiK00096.
OMAiYSEYAAH.

Enzyme and pathway databases

UniPathwayiUPA00940.

Family and domain databases

CDDicd08173. Gro1PDH. 1 hit.
HAMAPiMF_00497_A. G1P_dehydrogenase_A. 1 hit.
InterProiIPR023002. G1P_dehydrogenase_arc.
IPR032837. G1PDH.
[Graphical view]
PfamiPF13685. Fe-ADH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG1PDH_SULIM
AccessioniPrimary (citable) accession number: C3MVE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: November 2, 2016
This is version 46 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.