A2BN26 (G1PDH_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	Hbut_1566

Organism

Hyperthermus butylicus (strain DSM 5456 / JCM 9403)

Taxonomic identifier

415426 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Pyrodictiaceae › Hyperthermus

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Phospholipid biosynthesis
Cellular component	Cytoplasm
Ligand	Metal-binding NAD NADP Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycerol-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 349	349	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_0000350645
Regions
	Nucleotide binding	95 – 99	5	NAD By similarity
	Nucleotide binding	117 – 120	4	NAD By similarity
Sites
	Metal binding	169	1	Zinc; catalytic By similarity
	Metal binding	249	1	Zinc; catalytic By similarity
	Metal binding	265	1	Zinc; catalytic By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	126	1	NAD By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	253	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2BN26 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: 29C79805D8EC2678	FASTA	349	37,815
	10 20 30 40 50 60 MLHRIELPQK IVVGSGAIDA LREVLEEFAG RNSSIAVISG PNVWRLYGER FRSIVEGFVE 70 80 90 100 110 120 YSFFEARNAS VEYAEKLLED VKAYSPSLVV GFGGGKSIDL AKYVAYRLGV RMISVPTSPS 130 140 150 160 170 180 HDGIASPFTS LKGLDKPHSV RTVTPAAIIA DIDIIASAPI RLIRAGAGDL IAKLTAIRDW 190 200 210 220 230 240 RLAHKLKGEY YGEYAAKLAL LSAKHVIEYA SQIGRGVKEA VRVLVEGLVS SGVAMCIAGS 250 260 270 280 290 300 TRPASGSEHL FAHALDLIAP GKALHGEEVA LGTIMMMYLH GGDWRHVRRT IRRLGLPVTA 310 320 330 340 KELGLSDEVI VKALTMAHRI RPERYTILGE SGLTWEAAER LARVTGVIG

References

[1]

"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C." Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P. Archaea 2:127-135(2007) [PubMed: 17350933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000493 Genomic DNA. Translation: ABM81387.1.
RefSeq	YP_001013732.1. NC_008818.1.
3D structure databases
ProteinModelPortal	A2BN26.
ModBase	Search...
Protein-protein interaction databases
STRING	A2BN26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4781507.
GenomeReviews	Gene locus Hbut_1566 in contig CP000493_GR.
KEGG	hbu:Hbut_1566.
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	AIHGELV.
PhylomeDB	A2BN26.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	HBUT415426:HBUT_1566-MONOMER.
Family and domain databases
HAMAP	MF_00497_A. G1P_dehydrogenase_A. [Tree]
InterPro	IPR023002. G1P_dehydrogenase_arc. IPR016205. Glycerol_DH. [Graphical view]
KO	K00096.
PIRSF	PIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

G1PDH_HYPBU

Accession

Primary (citable) accession number: A2BN26

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	February 20, 2007
Last modified:	November 16, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program