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A5UJW3 (G1PDH_METS3) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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):
Enantiomeric glycerophosphate synthase
sn-glycerol-1-phosphate dehydrogenase
Gene names
Name:egsA
Ordered Locus Names:Msm_0286
OrganismMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP]
Taxonomic identifier420247 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanobrevibacter

Protein attributes

Sequence length348 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

Subunit structure

Homooctamer By similarity. 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 – 348348Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_1000050603

Regions

Nucleotide binding94 – 985NAD By similarity
Nucleotide binding116 – 1194NAD By similarity

Sites

Metal binding1681Zinc; catalytic By similarity
Metal binding2481Zinc; catalytic By similarity
Metal binding2641Zinc; catalytic By similarity
Binding site1211Substrate By similarity
Binding site1251NAD By similarity
Binding site1681Substrate By similarity
Binding site2521Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UJW3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: ABC788628BABB2CC

FASTA34837,378
        10         20         30         40         50         60 
MNTRKIQMPR EVYIGPDVIY ETGEICKDLH LDNKVLVLTG PNTYDIAAKH AIESLENQDI 

        70         80         90        100        110        120 
EVDVKIVEKV SYDSVEEVSE MITSGTNVLG VGGGKVIDVA KLASYDKNVF FVSMPTTASH 

       130        140        150        160        170        180 
DGIVSPLASI KNPKTSTSAK AHAPIAVIAD SKIIANSPFR LLSAGCADLI SNFTAIKDWQ 

       190        200        210        220        230        240 
LAHRLKNESY SESAASLSIM SAKMITDNVD SIKPGLEESA RLVVKTLFSS GMAISIAGSS 

       250        260        270        280        290        300 
RPASGSEHTF SHALDKILDK PCLHGEQCGV GTILMMYLYG GDWKFIRDSL KAVGAPTSAK 

       310        320        330        340 
ELGISDENVI DALTMAHTIR PERYTILGDN GISEDAAYEL ALKTGVIK

« Hide

References

[1]"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut."
Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed: 17563350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PS / ATCC 35061 / DSM 861.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000678 Genomic DNA. Translation: ABQ86491.1.
RefSeqYP_001272859.1. NC_009515.1.

3D structure databases

ProteinModelPortalA5UJW3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5UJW3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5216745.
GenomeReviewsGene locus Msm_0286 in contig CP000678_GR.
KEGGmsi:Msm_0286.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMACGVGTIM.
ProtClustDBCLSK2791098.

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_METS3
AccessionPrimary (citable) accession number: A5UJW3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: November 16, 2011
This is version 38 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

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