Skip Header

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

Q4JB01 (G1PDH_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 50. 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
Ordered Locus Names:Saci_0640
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length351 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.

Sequence caution

The sequence AAY80028.1 differs from that shown. Reason: Erroneous initiation.

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 – 351351Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157352

Regions

Nucleotide binding97 – 1015NAD By similarity
Nucleotide binding119 – 1224NAD By similarity

Sites

Metal binding1711Zinc; catalytic By similarity
Metal binding2511Zinc; catalytic By similarity
Metal binding2671Zinc; catalytic By similarity
Binding site1241Substrate By similarity
Binding site1281NAD By similarity
Binding site1711Substrate By similarity
Binding site2551Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JB01 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: 307FAC9F0BC9B20B

FASTA35138,584
        10         20         30         40         50         60 
MEIKEHIINL PKHIYTGYGI LDNFRNYLQT LNLPQPFLVI TGPVIHQEIF SKRIEEHIKD 

        70         80         90        100        110        120 
FKYEVVIVNK SDLSEAEKVE DIARQKGIKT ILGVGGGTVI DIAKFTAYKI DREFISIPTS 

       130        140        150        160        170        180 
PSHDGITSPF AAIKGLGKPI SIKAKEPLAI ISDVEILASA PRRLINAGIG DTLGKITAVR 

       190        200        210        220        230        240 
DWRLAHKLRG EYYGDYTASL ALMSARHALS CTKIINKDIR AGVRVLTEAL ISSGVAMGMA 

       250        260        270        280        290        300 
GSTRPASGSE HLFAHAIELL YPNLGLHGEL VALGTIMMAY IHGINWRRIR RAMKKIGLPV 

       310        320        330        340        350 
TSKQIGIPDE GIIKALTIAH SIRPERYTIL GDRGLTWESA EKIARETGVI S 

« Hide

References

[1]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed: 15995215] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000077 Genomic DNA. Translation: AAY80028.1. Different initiation.
RefSeqYP_255321.1. NC_007181.1.

3D structure databases

ProteinModelPortalQ4JB01.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3474123.
GenomeReviewsGene locus Saci_0640 in contig CP000077_GR.
KEGGsai:Saci_0640.
NMPDRfig|330779.3.peg.2076.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG672951.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycSACI330779:SACI_0640-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_SULAC
AccessionPrimary (citable) accession number: Q4JB01
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 23, 2008
Last modified: November 16, 2011
This is version 50 of the entry and version 2 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