Skip Header

Contribute Send feedback
Read comments (?) or add your own

A9A2U8 (G1PDH_NITMS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Nmar_1729
OrganismNitrosopumilus maritimus (strain SCM1)
Taxonomic identifier436308 [NCBI]
Taxonomic lineageArchaea › Thaumarchaeota › marine archaeal group 1 › Nitrosopumilales › Nitrosopumilaceae › Nitrosopumilus

Protein attributes

Sequence length354 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

Homodimer 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
Reference 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 – 354354Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350660

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

Sequences

Sequence LengthMass (Da)Tools
A9A2U8 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 38EE02914BB39305

FASTA35438,594
        10         20         30         40         50         60 
MTKNQDRMKS HTMELPRQIV VGEKNINEFG EFLHNLTKPK KVSLISGIHV KKVLRQRIEK 

        70         80         90        100        110        120 
SLKTKRIKFV WHTSKDNQIS TLNRIEKEVK KDRSDMIAGI GGGRSVDTAK LISFNLDIPF 

       130        140        150        160        170        180 
VSVPTAASHD GVSSPFVSVK SDKPHSIVAT APLGVFVDID IIKKAPSRLL ASGCGDLVAN 

       190        200        210        220        230        240 
IIAVKDWQLG HQKTGEYYGT YSAELAMMSA MMVLDNSSKY AKNGLDARVI VEALISAGVA 

       250        260        270        280        290        300 
SCIAGSSRPC SGAEHLFSHA LDKIAPGKGL HGEKCGIGSI MIAKLQGQDW KKIVKTLKDV 

       310        320        330        340        350 
GAPTTAKQIG LTEDQIIDAL IIAQDLRPER YTILKEVEMT DRKAKSLAKS TKVI

« Hide

References

[1]"Complete sequence of Nitrosopumilus maritimus SCM1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Stahl D., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000866 Genomic DNA. Translation: ABX13625.1.
RefSeqYP_001583063.1. NC_010085.1.

3D structure databases

ProteinModelPortalA9A2U8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9A2U8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5774203.
GenomeReviewsGene locus Nmar_1729 in contig CP000866_GR.
KEGGnmr:Nmar_1729.

Phylogenomic databases

HOGENOMHBG672951.
OMADKPALHG.

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_NITMS
AccessionPrimary (citable) accession number: A9A2U8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 34 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents