Reviewed, UniProtKB/Swiss-Prot P58460 (G1PDH_SULTO)

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):
    sn-glycerol-1-phosphate dehydrogenase
    Enantiomeric glycerophosphate synthase

Gene names

Name:	egsA
Ordered Locus Names:	ST0344

Organism

Sulfolobus tokodaii [Complete proteome] [HAMAP]

Taxonomic identifier

111955 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential.
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
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-dehydroquinate synthase activity Inferred from electronic annotation. Source: InterPro glycerol-1-phosphate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: HAMAP zinc 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 – 350	350	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000157354
Regions
	Nucleotide binding	96 – 100	5	NAD By similarity
	Nucleotide binding	118 – 121	4	NAD By similarity
Sites
	Metal binding	170	1	Zinc; catalytic By similarity
	Metal binding	250	1	Zinc; catalytic By similarity
	Metal binding	266	1	Zinc; catalytic By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	127	1	NAD By similarity
	Binding site	170	1	Substrate By similarity
	Binding site	254	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58460-1 [UniParc]. Last modified December 5, 2001. Version 1. Checksum: 539461CC2F6BD310	FASTA	350	37,792
	10 20 30 40 50 60 MELKEHIIDL PKKVYIGYDI IDNIKEYILS LNLSGPFLIV TGPLVRKIIT DKIIENFKDE 70 80 90 100 110 120 SVEVVEVKIA SIDEVNKVEE MAKGSRINTI IGVGGGNIID VAKYVAYRIG KEFVSLPTAP 130 140 150 160 170 180 SHDGITSPFA SIKGLGKPTS VKAKGPIAII ADINVLASAP RRLINAGIGD TIGKITAVRD 190 200 210 220 230 240 WQLAAKLRGE YYGDYTASLA LMSAKHALSC AKILDKDVRA GVRVLTEALI SSGVAMGMAG 250 260 270 280 290 300 STRPASGSEH LFAHAIEILY PDKALHGELV ALGTILMAYI HGINWKKIKK AMKKVGLPTK 310 320 330 340 350 AKQLGIPDEI IIKALTIAHT IRPERYTILG DRGLTWEAAE KIAKETGIID

References

[1]

"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7." Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H. DNA Res. 8:123-140(2001) [PubMed: 11572479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000023 Genomic DNA. Translation: BAB65322.1.
RefSeq	NP_376213.1.
3D structure databases
HSSP	HSSP built from PDB template 1JQA based on UniProtKB P32816.
ModBase	Search...
Genome annotation databases
GeneID	1458263.
GenomeReviews	Gene locus ST0344 in contig BA000023_GR.
KEGG	sto:ST0344.
NMPDR	fig|273063.1.peg.381.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P58460.
OMA	YTAVLDW.
Enzyme and pathway databases
BRENDA	1.1.1.261. 261167.
Family and domain databases
HAMAP	MF_00497. [Tree]
InterPro	IPR002658. DHQ_synth_AroB. IPR016205. Glycerol_DH. [Graphical view]
Pfam	PF01761. DHQ_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

G1PDH_SULTO

Accession

Primary (citable) accession number: P58460

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	December 5, 2001
Last modified:	November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)