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Q8TW08 (G1PDH_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. 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

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
Synonyms:gldA
Ordered Locus Names:MK1230
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length353 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
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 – 353353Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157343

Regions

Nucleotide binding99 – 1035NAD By similarity
Nucleotide binding121 – 1244NAD By similarity

Sites

Metal binding1731Zinc; catalytic By similarity
Metal binding2531Zinc; catalytic By similarity
Metal binding2691Zinc; catalytic By similarity
Binding site1261Substrate By similarity
Binding site1301NAD By similarity
Binding site1731Substrate By similarity
Binding site2571Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TW08 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 64A575C0A35AA30A

FASTA35337,642
        10         20         30         40         50         60 
MSVPKKRMQL PREVVVGSNV LPEVPKLLRS VGVPDGVVAV FSGRTTMKIA GNEVADHLEE 

        70         80         90        100        110        120 
AGYQTSPVIV KGSTGDDVKK ALEALDEIDA DVVAAVGGGK VIDVAKVASY RRGIPFISVP 

       130        140        150        160        170        180 
TSASHDGIAS PFASIRREGR PYSEPAQAPL AILADIEVIR EAPERLIRAG VGDVVSNVTA 

       190        200        210        220        230        240 
VKDWRLAHRL RNEPYSEYAS SLSLMAARIV MKNAKPIGKL LPEGIKKLVQ ALISGGVAMS 

       250        260        270        280        290        300 
IAGSSRPCSG SEHLFSHALD VIAERPALHG EQCGVGTIIM EYLHGGNWRE IRETLETAGA 

       310        320        330        340        350 
PTTAEDLGVS DEEIIEALCR AHKIRPDRYT ILGDKGLTRE AAERAAEETG VIQ 

« Hide

References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM02443.1.
RefSeqNP_614513.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TW08.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1477825.
GenomeReviewsGene locus MK1230 in contig AE009439_GR.
KEGGmka:MK1230.
NMPDRfig|190192.1.peg.1226.

Phylogenomic databases

HOGENOMHBG672951.
OMAAIHGELV.
PhylomeDBQ8TW08.

Enzyme and pathway databases

BioCycMKAN190192:MK1230-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_METKA
AccessionPrimary (citable) accession number: Q8TW08
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2002
Last modified: December 14, 2011
This is version 65 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