A3DN28 (G1PDH_STAMF) 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:	Smar_0939

Organism

Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP]

Taxonomic identifier

399550 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus

Protein attributes

Sequence length	355 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
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 – 355	355	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_0000350661
Regions
	Nucleotide binding	101 – 105	5	NAD By similarity
	Nucleotide binding	123 – 126	4	NAD By similarity
Sites
	Metal binding	175	1	Zinc; catalytic By similarity
	Metal binding	255	1	Zinc; catalytic By similarity
	Metal binding	271	1	Zinc; catalytic By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	132	1	NAD By similarity
	Binding site	175	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3DN28 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: E24F8CEA368C0C48	FASTA	355	38,601
	10 20 30 40 50 60 MLNRSIHEIT LPLKVIIGSN ILDKIPDYLL KMKLTNQYKA GIITGPTTYN VAGKIVEEAM 70 80 90 100 110 120 KNNGYIVEVW KARDARIETA NQIVEETKKH GIKIFLGVGG GKSIDLAKYA AYKNNGYMIS 130 140 150 160 170 180 VPTAASHDGI ASPFASLKGT SKPTSTPTTT PYAIIADIDM ISKAPPRLIR SGVGDLLGKL 190 200 210 220 230 240 TAVKDWQLAH RLKGEYYGEY AAQLALLSAK HVIRYHELIA SGNPDGIRIV VEALISSGVA 250 260 270 280 290 300 MCIAGSSRPA SGSEHLFSHA LDLLAPGKAL HGEQVALGTI MMLYLYGDPK WKKIKRIMKK 310 320 330 340 350 IGLPTTAEEI GIPIETIVKA LTIAHKIRPN RYTILGEKGL TEEAAWRLVR ETGII

References

[1]

"The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota." Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N. BMC Genomics 10:145-145(2009) [PubMed: 19341479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1.

[2]

"Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1." Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C. Stand. Genomic Sci. 1:183-188(2009) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000575 Genomic DNA. Translation: ABN70038.1.
RefSeq	YP_001040946.1. NC_009033.1.
3D structure databases
ProteinModelPortal	A3DN28.
ModBase	Search...
Protein-protein interaction databases
STRING	A3DN28.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4907415.
GenomeReviews	Gene locus Smar_0939 in contig CP000575_GR.
KEGG	smr:Smar_0939.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	AIHGELV.
PhylomeDB	A3DN28.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	SMAR399550:SMAR_0939-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_STAMF

Accession

Primary (citable) accession number: A3DN28

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	March 20, 2007
Last modified:	November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program