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Q9HJ16 (G1PDH_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 69. 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:Ta1158
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma

Protein attributes

Sequence length352 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 – 352352Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157355

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
Q9HJ16 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 79612CC0F03C3BEA

FASTA35238,496
        10         20         30         40         50         60 
MEFQKFRTMH FPRDVYIGHD VLEHIVDVVG ENSRNKNAII VSGDLTYELA GRKVHDLLST 

        70         80         90        100        110        120 
YGYEVHVFLA GNANYDTLER IEYESLDIQA GIVIGVGGGA KIDLAKKLAF DRKLPFVSVP 

       130        140        150        160        170        180 
TAPSHDGIAS PRASLRRNGI SYSEEGAMPI GVIADTAIMI KAPYRYLAAG AADVISNLSA 

       190        200        210        220        230        240 
VKDWKLAHRL KGEEFSSSAA AMSEYSAQEV LSQINEIKKY EESSVWLVTK NILASGTAMA 

       250        260        270        280        290        300 
IAGNSRPGSG SEHLFAHALE AAGVENMLHG EMCAMGTVIS MYLHDENWQQ IKEAFDNLGI 

       310        320        330        340        350 
SIRSRDYGIE DEIVINALRT AHAIRPERYT ILGESDMSYD AAVKALELTG II

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed: 11029001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL445066 Genomic DNA. Translation: CAC12283.1.
RefSeqNP_394614.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HJ16.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1456658.
GenomeReviewsGene locus Ta1158 in contig AL139299_GR.
KEGGtac:Ta1158.
NMPDRfig|273075.1.peg.1136.

Phylogenomic databases

HOGENOMHBG672951.
OMACGVGTIM.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycTACI273075:TA1158-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_THEAC
AccessionPrimary (citable) accession number: Q9HJ16
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 69 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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