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Reviewed, UniProtKB/Swiss-Prot A0RXV2 (G1PDH_CENSY)

Last modified November 3, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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):
    sn-glycerol-1-phosphate dehydrogenase
    Enantiomeric glycerophosphate synthase
Gene names
Name: egsA
Ordered Locus Names: CENSYa_1547
OrganismCenarchaeum symbiosum [Complete proteome] [HAMAP]
Taxonomic identifier46770 [NCBI]
Taxonomic lineageArchaea › Thaumarchaeota › Cenarchaeales › Cenarchaeaceae › Cenarchaeum

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Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Catalytic activity

sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the glycerol-1-phosphate dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497
PRO_0000350643

Regions

Nucleotide binding103 – 1075NAD By similarity
Nucleotide binding125 – 1284NAD By similarity

Sites

Metal binding1761Zinc; catalytic By similarity
Metal binding2551Zinc; catalytic By similarity
Metal binding2711Zinc; catalytic By similarity
Binding site1301Substrate By similarity
Binding site1341NAD By similarity
Binding site1761Substrate By similarity
Binding site2591Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
A0RXV2-1 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: BB45E00B2CB08C4E

FASTA35436,863
        10         20         30         40         50         60 
MPGGRDPMPS HTMELPRLIV IGEGNMGDLG PFLGSLGGPR TVSLISGRTV QGATGRKIEG 

        70         80         90        100        110        120 
SLKRSGIKWS WHMAGTNDPE SIASVQEAVR SDESGMAVGI GGGRAVDTAK MAAFKLGIPF 

       130        140        150        160        170        180 
VSVPTAASHD GIASPFVSIK GDKPHSITAT APLGVFVDIG VIRKAPARLL ASGCGDLVAN 

       190        200        210        220        230        240 
MIAVRDWELG RDRKGEYYGR YAASLALMSA KIVMENAARF AREGVDERVV VEALISAGVA 

       250        260        270        280        290        300 
SCIAGSSRPC SGAEHLFSHA LDRIAPGAGL HGEKCGIGSI MMAKLQGQDW KGIAGALKSV 

       310        320        330        340        350 
GAPTTARQIG LDREDLIEAL MTAQGLRPER YTILEEAGMS RRRAAALARV TGVA

« Hide

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References

[1]"Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum."
Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.
Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006) [PubMed: 17114289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A.

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Cross-references

Sequence databases

DP000238 Genomic DNA. Translation: ABK78169.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GenomeReviewsGene locus CENSYa_1547 in contig DP000238_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYTAVLDW.

Family and domain databases

HAMAPMF_00497.
[Tree]
InterProIPR002658. DHQ_synth_AroB.
IPR016205. Glycerol_DH.
[Graphical view]
PfamPF01761. DHQ_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameG1PDH_CENSY
AccessionPrimary (citable) accession number: A0RXV2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 9, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents