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A6VIL2 (G1PDH_METM7) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 33. 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:MmarC7_1225
OrganismMethanococcus maripaludis (strain C7 / ATCC BAA-1331) [Complete proteome] [HAMAP]
Taxonomic identifier426368 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

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_0000350655

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
A6VIL2 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: BA036FA8E6A3EF63

FASTA33436,763
        10         20         30         40         50         60 
MIVIPRYTII KEKASIRIPE ILDNLNLKNP LVITGKNTQK YNKDFDFIYY DEIETSDLEN 

        70         80         90        100        110        120 
LKNYTKDYDS VIGIGGGRPI DIGKLIAHKS KKPFLSVPTT ASNDGIASPI VSLTQPSYMT 

       130        140        150        160        170        180 
EAPIAIIADT EIIKKSPKKL LSAGMGDIVS NITAVLDWEL GKIEKLEKYS DSSGIFSKTI 

       190        200        210        220        230        240 
AIELMDYVLN SDLEEYPKKL VKALIGSGIS IAIAHSSRPA SGSEHLFSHA LDNMKEKYGI 

       250        260        270        280        290        300 
DTNSLHGEQC GVGTLAIAQI YLEEGKIEVE TVEMIKNSLK AVDAPVTAKQ LGFDEEILSE 

       310        320        330 
ALSSAHSLRN RHTILRNGLS KEKAREILEK SEII

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C7."
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., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C7 / ATCC BAA-1331.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000745 Genomic DNA. Translation: ABR66288.1.
RefSeqYP_001330439.1. NC_009637.1.

3D structure databases

ProteinModelPortalA6VIL2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6VIL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5328036.
GenomeReviewsGene locus MmarC7_1225 in contig CP000745_GR.
KEGGmmz:MmarC7_1225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMADKPALHG.
ProtClustDBCLSK876301.

Enzyme and pathway databases

BioCycMMAR426368:MMARC7_1225-MONOMER.

Family and domain databases

HAMAPMF_00497_A. G1P_dehydrogenase_A.
[Tree]
InterProIPR023002. G1P_dehydrogenase_arc.
[Graphical view]
KOK00096.
ProtoNetSearch...

Entry information

Entry nameG1PDH_METM7
AccessionPrimary (citable) accession number: A6VIL2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: August 21, 2007
Last modified: November 16, 2011
This is version 33 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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