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Q2FPC7 (G1PDH_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 41. 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:Mhun_1136
OrganismMethanospirillum hungatei (strain JF-1 / DSM 864)
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

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
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 – 359359Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350651

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
Q2FPC7 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: A6C175F79048EA59

FASTA35938,362
        10         20         30         40         50         60 
MSTDPVQVLQ PDGFNKSRWT QLPRDVLIGH QAIMQLPDII ADIKPGRSVL LISGGTTREV 

        70         80         90        100        110        120 
AGNTVADILK DQYEVRRFVA GKLDADTLEA CSQASSSADF LIGVGGGRVI DCAKIVSYKQ 

       130        140        150        160        170        180 
GKPFISVPTA ASHDGIISGR ATLPTETGSV SVGAHPPIAV VADTGIISQA PHRLMASGCA 

       190        200        210        220        230        240 
DVISNYTAIL DWELAHRLRG EQISEYAIAL SKMTAEILVK DANLIKPGQE EAAWIVVKAL 

       250        260        270        280        290        300 
VSSGVSMAIA GSSRPASGGE HKFGHALERL MPGAALHGEA CGIGSIMTMY LHGGDWREIR 

       310        320        330        340        350 
SSLARIGAPT TPRELNIPDE VIVEALMKAR DIRPERFTIL DMGLTRESAE HLVQMLYEE 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-1 / DSM 864.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD40885.1.
RefSeqYP_502604.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FPC7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2FPC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3922514.
GenomeReviewsGene locus Mhun_1136 in contig CP000254_GR.
KEGGmhu:Mhun_1136.
NMPDRfig|323259.5.peg.1192.

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMACGVGTIM.
PhylomeDBQ2FPC7.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycMHUN323259:MHUN_1136-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_METHJ
AccessionPrimary (citable) accession number: Q2FPC7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: March 21, 2006
Last modified: November 16, 2011
This is version 41 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