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A9A874 (G1PDH_METM6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:MmarC6_0730
OrganismMethanococcus maripaludis (strain C6 / ATCC BAA-1332) [Complete proteome] [HAMAP]
Taxonomic identifier444158 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length334 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 – 334334Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350654

Regions

Nucleotide binding77 – 815NAD By similarity
Nucleotide binding99 – 1024NAD By similarity

Sites

Metal binding1471Zinc; catalytic By similarity
Metal binding2251Zinc; catalytic By similarity
Metal binding2461Zinc; catalytic By similarity
Binding site1041Substrate By similarity
Binding site1081NAD By similarity
Binding site1471Substrate By similarity
Binding site2291Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A9A874 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 6BE4CD76C69DC1C6

FASTA33436,774
        10         20         30         40         50         60 
MIVIPRYTII KEKASGRIPE ILDNLNLKNP LVITGKNTKK YNKDFDFIYY DEIETSDLEN 

        70         80         90        100        110        120 
IKNYAKDYDS IIGIGGGRPI DIGKLIAHKS KKPFLSVPTT ASNDGIASPI VSLTQPSYMT 

       130        140        150        160        170        180 
EAPIAIIADI DIIKKSPKKL LSAGMGDIVS NITAVLDWEL GKIEKSEKYS DSSGIFSKTI 

       190        200        210        220        230        240 
AIELMDYVLN SNLEEYPKKL VKALIGSGIS IAIAHSSRPA SGSEHLFSHA LDTMKEKYDI 

       250        260        270        280        290        300 
DTTSLHGEQC GVGTLAIAQI YLEEGKLEVE TFEMLKNSLK AVDAPVTAEQ LGFDEEIIIE 

       310        320        330 
ALSSANTLRK RHTILRNGIS KEKAREILEK SEII 

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C6 / ATCC BAA-1332.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000867 Genomic DNA. Translation: ABX01547.1.
RefSeqYP_001548779.1. NC_009975.1.

3D structure databases

ProteinModelPortalA9A874.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9A874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5737801.
GenomeReviewsGene locus MmarC6_0730 in contig CP000867_GR.
KEGGmmx:MmarC6_0730.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG672951.
OMACGVGTIM.
ProtClustDBCLSK876301.

Enzyme and pathway databases

BioCycMMAR444158:MMARC6_0730-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_METM6
AccessionPrimary (citable) accession number: A9A874
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 37 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