Q979B1 (G1PDH_THEVO) 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:	TV1251
ORF Names:	TVG1288826

Organism

Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]

Taxonomic identifier

273116 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma

Protein attributes

Sequence length	352 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
Subcellular location	Cytoplasm Potential HAMAP MF_00497_A.
Sequence similarities	Belongs to the glycerol-1-phosphate dehydrogenase family.
Sequence caution	The sequence BAB60393.1 differs from that shown. Reason: Erroneous initiation.

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 – 352	352	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_0000157356
Regions
	Nucleotide binding	99 – 103	5	NAD By similarity
	Nucleotide binding	121 – 124	4	NAD By similarity
Sites
	Metal binding	173	1	Zinc; catalytic By similarity
	Metal binding	253	1	Zinc; catalytic By similarity
	Metal binding	269	1	Zinc; catalytic By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	130	1	NAD By similarity
	Binding site	173	1	Substrate By similarity
	Binding site	257	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q979B1 [UniParc]. Last modified December 5, 2001. Version 2. Checksum: 2D122A30CE231536	FASTA	352	38,482
	10 20 30 40 50 60 MEFQKYRTMH FPRDVYIGHD VLNRVLDVVD QNSRTRDVII VTGNTTYELA GKKIVEILAS 70 80 90 100 110 120 SPYEVHLSFA GEANYENLKK IEEETNDVNA GIIIGVGGGT KIDLAKKLAY DKNLPFISIP 130 140 150 160 170 180 TSPSHDGIAS PRASLRRNGI SYSEEGAMPI GVIADTSVMI KAPYRYLAAG AADVISNISA 190 200 210 220 230 240 VKDWKLAHRL RGEEFSSSAA AMSEYSAQEV ISQVGEIRKY DESSVWLVTK NILASGTAMA 250 260 270 280 290 300 IAGNSRPGSG SEHLFAHALE AAGVNNMLHG EMCAMGTIVS LYLHDDNWQK IRDVFESLGV 310 320 330 340 350 SVKARDYGLK EEVVIEALRR AHAIRPERYT ILGESDMSYD AAVKALELTG II

References

[1]

"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium." Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M. Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed: 11121031] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000011 Genomic DNA. Translation: BAB60393.1. Different initiation.
RefSeq	NP_111746.1. NC_002689.2.
3D structure databases
ProteinModelPortal	Q979B1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1441367.
GenomeReviews	Gene locus TV1251 in contig BA000011_GR.
NMPDR	fig|273116.1.peg.1227.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG672951.
OMA	DKPALHG.
ProtClustDB	PRK00843.
Family and domain databases
HAMAP	MF_00497_A. G1P_dehydrogenase_A. [Tree]
InterPro	IPR023002. G1P_dehydrogenase_arc. IPR016205. Glycerol_DH. [Graphical view]
PIRSF	PIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

G1PDH_THEVO

Accession

Primary (citable) accession number: Q979B1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	December 5, 2001
Last modified:	September 21, 2011
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program