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A4YIZ1 (G1PDH_METS5) 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:Msed_2255
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Metallosphaera

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.

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_1000072433

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
A4YIZ1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: B2D356C62A728040

FASTA35137,968
        10         20         30         40         50         60 
MEIHEHIIEL PKKVYVGNGI LSKLRDYLFQ LNVLEPVLVV TGPNVRKIVI DEVAKGLNEI 

        70         80         90        100        110        120 
GKIEFIEVLD SSIDEVNRVE EKAKQLNPKF VLGIGGGKTI DVAKYVAYKL NVNFISIPTA 

       130        140        150        160        170        180 
PSHDGITSPF ASIKGLGKPV SVKAKMPYAI IADINVLSSA PRRLINSGIG DTIGKLVAVR 

       190        200        210        220        230        240 
DWKLASKLTG EYYGDYTASL ALLSAKHALS CTRIIHRDLK YSVSLLTEAL ISSGVAMGMA 

       250        260        270        280        290        300 
GSTRPASGSE HLFAHAVDLL QPNAALHGEL VGMGSIIMAY IHGINWREIR NALDRIGAPT 

       310        320        330        340        350 
TAKQLGIPND VIIKALTIAH TIRPERYTIL GDRGLTWASA EKVARDTGVI E

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed: 18083856] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000682 Genomic DNA. Translation: ABP96393.1.
RefSeqYP_001192317.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YIZ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4YIZ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5104316.
GenomeReviewsGene locus Msed_2255 in contig CP000682_GR.
KEGGmse:Msed_2255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMACGVGTIM.
PhylomeDBA4YIZ1.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycMSED399549:MSED_2255-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_METS5
AccessionPrimary (citable) accession number: A4YIZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 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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