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Q6L0R7 (G1PDH_PICTO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-1-phosphate dehydrogenase [NAD(P)+]

Short name=G1P dehydrogenase
Short name=G1PDH
EC=1.1.1.261
Alternative name(s):
Enantiomeric glycerophosphate synthase
sn-glycerol-1-phosphate dehydrogenase
Gene names
Name:egsA
Ordered Locus Names:PTO0850
OrganismPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) [Complete proteome] [HAMAP]
Taxonomic identifier263820 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP MF_00497_A

Catalytic activity

sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00497_A

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497_A

Subcellular location

Cytoplasm Potential HAMAP MF_00497_A.

Sequence similarities

Belongs to the glycerol-1-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycerol-1-phosphate dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157346

Regions

Nucleotide binding97 – 1015NAD By similarity
Nucleotide binding119 – 1224NAD By similarity

Sites

Metal binding1711Zinc; catalytic By similarity
Metal binding2511Zinc; catalytic By similarity
Metal binding2671Zinc; catalytic By similarity
Binding site1241Substrate By similarity
Binding site1281NAD By similarity
Binding site1711Substrate By similarity
Binding site2551Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6L0R7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: DA3D632F5653284B

FASTA35037,580
        10         20         30         40         50         60 
MNFNKIKSMH FPSDVYIGHD AILNIGSVVS KFLKSGEVLL ITGENTYNIA GKKVLSNLND 

        70         80         90        100        110        120 
FDVNVIIASR ATRDSIKSIE ESLKNRRSGI VLGVGGGSKI DIAKKIAYDL GIPFISVPTT 

       130        140        150        160        170        180 
PSHDGIASPR ASIYDGKSVY SEEATMPSAI VADTSIMVLA PYRYVAAGAA DVISNITAVL 

       190        200        210        220        230        240 
DWKLANRLKG EEFSSTAAVM SEYAGRELIE RSSMIQPGLE ESIWLVTKQI LASGAAMAIA 

       250        260        270        280        290        300 
GSSRPASGSE HLFSHAIEIL GPGSSIHGEQ CAMGSLISMY LHGGDWELLK NTYRKIGLNT 

       310        320        330        340        350 
RAESYGIGRE VAIKALSIAH RIRPSRYTIL GESDLSYNVA ERILSITGII 

« Hide

References

[1]"Genome sequence of Picrophilus torridus and its implications for life around pH 0."
Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., Schepers B., Dock C., Antranikian G., Liebl W.
Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004) [PubMed: 15184674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017261 Genomic DNA. Translation: AAT43435.1.
RefSeqYP_023628.1. NC_005877.1.

3D structure databases

ProteinModelPortalQ6L0R7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2845253.
GenomeReviewsGene locus PTO0850 in contig AE017261_GR.
KEGGpto:PTO0850.
NMPDRfig|263820.1.peg.850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG672951.
OMACGVGTIM.
PhylomeDBQ6L0R7.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycPTOR263820:PTO0850-MONOMER.

Family and domain databases

HAMAPMF_00497_A. G1P_dehydrogenase_A.
[Tree]
InterProIPR023002. G1P_dehydrogenase_arc.
IPR016205. Glycerol_DH.
[Graphical view]
KOK00096.
PIRSFPIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG1PDH_PICTO
AccessionPrimary (citable) accession number: Q6L0R7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 5, 2004
Last modified: December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families