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A2ST19 (G1PDH_METLZ) 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:Mlab_1308
OrganismMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) [Complete proteome] [HAMAP]
Taxonomic identifier410358 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanomicrobiales › Methanocorpusculaceae › Methanocorpusculum

Protein attributes

Sequence length360 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 – 360360Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350652

Regions

Nucleotide binding108 – 1125NAD By similarity
Nucleotide binding130 – 1334NAD By similarity

Sites

Metal binding1821Zinc; catalytic By similarity
Metal binding2621Zinc; catalytic By similarity
Metal binding2781Zinc; catalytic By similarity
Binding site1351Substrate By similarity
Binding site1391NAD By similarity
Binding site1821Substrate By similarity
Binding site2661Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A2ST19 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: BBEA30DD0F126546

FASTA36038,858
        10         20         30         40         50         60 
MEAKNNRILK DKTFDKSRWI QMPRDVIAGH DALLQLPNVI TDLGVTGPLL LLSGKTTLQT 

        70         80         90        100        110        120 
VGLEVLRLLE DRQVTSAVVG EITYEEIARV EDLAQNIGAV LIIAVGGGRV IDTAKVVSYN 

       130        140        150        160        170        180 
LDIQFISVPT AASHDGIASS RASIMTADGN VSVAAHPPLA IVADTGIIAG APHRLMAAGY 

       190        200        210        220        230        240 
ADMVANYTAV MDWDLSKSKT GEQVSEYAMT LSMITAELMV ENAEKIKAFD ENAAWIVVKA 

       250        260        270        280        290        300 
LFASGVAMSI AGSSRPASGG EHKFAHMLER LVPGKVLHGE ACGVGTIISM IMHEGDWKKI 

       310        320        330        340        350        360 
RNSLRLIGAP TTPKDLGISD EIVIEAILRA KEIRPERYTI FDEDITREQA ECLVARLYEE

« Hide

References

[1]"Complete genome sequence of Methanocorpusculum labreanum type strain Z."
Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:197-203(2009) [PubMed: 21304657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43576 / DSM 4855 / Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000559 Genomic DNA. Translation: ABN07475.1.
RefSeqYP_001030742.1. NC_008942.1.

3D structure databases

ProteinModelPortalA2ST19.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2ST19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4794656.
GenomeReviewsGene locus Mlab_1308 in contig CP000559_GR.
KEGGmla:Mlab_1308.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMADKPALHG.
PhylomeDBA2ST19.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycMLAB410358:MLAB_1308-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_METLZ
AccessionPrimary (citable) accession number: A2ST19
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: March 6, 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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