Reviewed, UniProtKB/Swiss-Prot O28599 (G1PDH_ARCFU)

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
Synonyms:	gldA
Ordered Locus Names:	AF_1674

Organism

Archaeoglobus fulgidus [Complete proteome] [HAMAP]

Taxonomic identifier

2234 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	351 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
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 – 351	351	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000157339
Regions
	Nucleotide binding	93 – 97	5	NAD By similarity
	Nucleotide binding	115 – 118	4	NAD By similarity
Sites
	Metal binding	167	1	Zinc; catalytic By similarity
	Metal binding	247	1	Zinc; catalytic By similarity
	Metal binding	263	1	Zinc; catalytic By similarity
	Binding site	120	1	Substrate By similarity
	Binding site	124	1	NAD By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	251	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O28599-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 085DB6592BAEF66A	FASTA	351	38,450
	10 20 30 40 50 60 MRFKTVDLPY HVYIGENVIS KLPKVLRSLD ANYFLLLTDE VVKNLVVVNL KETLKDFEYD 70 80 90 100 110 120 MMLVESAKME EARKIVLRGG FADYDAVVGV GGGKVLDVSK VVSSELNASM ISVPTTASHD 130 140 150 160 170 180 GIASPVASFK ENGKPISIST NPPSAVIADL NIIKNCPIRL LRSGYGDLVS NISSVKDWQL 190 200 210 220 230 240 ARDLVGEDYN EVAASIAVMP AQLMVSKADE LDLTLPPHLL MLLRGLIMSG VAIAFVGSSR 250 260 270 280 290 300 PASGAEHKFS HALDYLGYGN GTHGEQVALG TIIMEYLHEK YYGRGDWEQI KMSLEKVHAP 310 320 330 340 350 TTAKEIGLTR EQVIEALMLA TKLRKKRFTI LEAVKPTKEE FELVVEKTGV A

References

[1]

"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000782 Genomic DNA. Translation: AAB89576.1.
PIR	A69459.
RefSeq	NP_070502.1.
3D structure databases
HSSP	HSSP built from PDB template 1JPU based on UniProtKB P32816.
ModBase	Search...
Genome annotation databases
GeneID	1484897.
GenomeReviews	Gene locus AF_1674 in contig AE000782_GR.
KEGG	afu:AF1674.
NMPDR	fig|224325.1.peg.1663.
TIGR	AF_1674.
Phylogenomic databases
HOGENOM	O28599.
OMA	ADWELAH.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_1674-MON.
BRENDA	1.1.1.261. 7576.
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_ARCFU

Accession

Primary (citable) accession number: O28599

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 63 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)