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Q12X59 (G1PDH_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Mbur_1032
OrganismMethanococcoides burtonii (strain DSM 6242) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length357 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 – 357357Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350650

Regions

Nucleotide binding104 – 1085NAD By similarity
Nucleotide binding126 – 1294NAD By similarity

Sites

Metal binding1781Zinc; catalytic By similarity
Metal binding2581Zinc; catalytic By similarity
Metal binding2741Zinc; catalytic By similarity
Binding site1311Substrate By similarity
Binding site1351NAD By similarity
Binding site1781Substrate By similarity
Binding site2621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12X59 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 96478130593BDEC6

FASTA35737,880
        10         20         30         40         50         60 
MDVTHDMNGQ KKWMQLPRNV VIGNGVINEV RDVCTDLKLI DNALVVTGKS TKGIAGEIVQ 

        70         80         90        100        110        120 
DSLQDAGQNV ELVISESASM KEVERIRKHA IESGTKYFLG VGSGKTIDVA KLAATDLEVP 

       130        140        150        160        170        180 
FISVPTAASH DGIVSSRASI KDGKTTTSVQ ANAPMAVIAD TEIIANAPYR LLAAGCGDII 

       190        200        210        220        230        240 
SNCTAVLDWQ LASRLQNVQF SEYAAALASM TAQILIDSAD SIKPELESSV RMVVKALVSS 

       250        260        270        280        290        300 
GVAMSIAGSS RPASGSEHMF SHALDRVADE PALHGEQCGV GTILMMYLHG GDWKKISDAL 

       310        320        330        340        350 
KLIGAPTTAK ELGIEDKYIL EALVLSHTIR PERYTILGTG LTPDAAEIVA RKTKVIS 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE51967.1.
RefSeqYP_565717.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12X59.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12X59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3998772.
GenomeReviewsGene locus Mbur_1032 in contig CP000300_GR.
KEGGmbu:Mbur_1032.
NMPDRfig|259564.8.peg.979.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMACGVGTIM.
PhylomeDBQ12X59.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycMBUR259564:MBUR_1032-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_METBU
AccessionPrimary (citable) accession number: Q12X59
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 43 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