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A7I9R4 (G1PDH_METB6) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 36. 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:Mboo_1960
OrganismMethanoregula boonei (strain 6A8) [Complete proteome] [HAMAP]
Taxonomic identifier456442 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanomicrobiales › Genera incertae sedis › Methanoregula

Protein attributes

Sequence length359 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 – 359359Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350649

Regions

Nucleotide binding107 – 1115NAD By similarity
Nucleotide binding129 – 1324NAD By similarity

Sites

Metal binding1811Zinc; catalytic By similarity
Metal binding2611Zinc; catalytic By similarity
Metal binding2771Zinc; catalytic By similarity
Binding site1341Substrate By similarity
Binding site1381NAD By similarity
Binding site1811Substrate By similarity
Binding site2651Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7I9R4 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 0DF5D14961CFA788

FASTA35938,384
        10         20         30         40         50         60 
MSPDAIKLLK EKVFDKSKWM QLPRDVVIGH DVLGQIAPVC EDLKLGRSAL LISGKNTMDR 

        70         80         90        100        110        120 
AGKTVQDVIG KTCDVMVYIS DEISPAVIKD AEKAAKDVDF VIGVGGGRVI DTAKIVSYNL 

       130        140        150        160        170        180 
DRQFVSVPTA ASHDGIASAR ASVPTGEGNV SLEAHPPIAI IADTCIIASA PHRLLAAGCA 

       190        200        210        220        230        240 
DVISNYTAIL DWEMAHRIKG EPMSEYAVAL SKMTAEILVK NADLIRPNQE QSAWFVTKAL 

       250        260        270        280        290        300 
VSSGVAMSIA GSSRPASGGE HKFSHALDRL APNKALHGES CGIGTIISMY LHGGDWRGIR 

       310        320        330        340        350 
QSLRTIGAPV TPTDVGIADE IAVEALLMAK TIRPERFTIF DMGITRDSAE KLIQMLYAD

« Hide

References

[1]"Complete sequence of Candidatus Methanoregula boonei 6A8."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Zinder S., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 6A8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000780 Genomic DNA. Translation: ABS56475.1.
RefSeqYP_001405118.1. NC_009712.1.

3D structure databases

ProteinModelPortalA7I9R4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7I9R4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5409997.
GenomeReviewsGene locus Mboo_1960 in contig CP000780_GR.
KEGGmbn:Mboo_1960.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMACGVGTIM.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycCMET456442:MBOO_1960-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_METB6
AccessionPrimary (citable) accession number: A7I9R4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: September 11, 2007
Last modified: November 16, 2011
This is version 36 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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