A8MC03 (G1PDH_CALMQ) 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:	Cmaq_1971

Organism

Caldivirga maquilingensis (strain ATCC 700844 / DSMZ 13496 / JCM 10307 / IC-167) [Complete proteome] [HAMAP]

Taxonomic identifier

397948 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Caldivirga

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
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.
Sequence caution	The sequence ABW02787.1 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_0000350642
Regions
	Nucleotide binding	91 – 95	5	NAD By similarity
	Nucleotide binding	113 – 116	4	NAD By similarity
Sites
	Metal binding	169	1	Zinc; catalytic By similarity
	Metal binding	249	1	Zinc; catalytic By similarity
	Metal binding	269	1	Zinc; catalytic By similarity
	Binding site	118	1	Substrate By similarity
	Binding site	122	1	NAD By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	253	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8MC03 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 7B217D01C4D79159	FASTA	352	38,302
	10 20 30 40 50 60 MVKGLELFEV PRQVVFGPNA IGKVSEVLTY LGLRRGLIIT GHIHSRHIAS KVSEQCVDCQ 70 80 90 100 110 120 IISDDEIELS DVVKGMSAFS DVDFIAGVGG GRVIDVSKVI AYKLNKHLIS IPTVASHDGI 130 140 150 160 170 180 ASPYISFLMQ DDLNKLGVGK VRKTPLAIIV DTGIVAEAPR VFLLAGIGEL LGKKVALMDW 190 200 210 220 230 240 RLGHRIKGED YSESAAMLAL SSHMIIMNNV NKLTRHGEEE TRIVVKALLG CGVAMAIAGS 250 260 270 280 290 300 TRPCSGSEHL FSHSLDLLAR EYGVKQAMHG MQVALSSVIM LYLHGANWRR IIKIMKMLGL 310 320 330 340 350 PTSFKELGYD KELVVEALMN AHRIRPDRYT ILGSNGLTRE AAEAALEQTG VI

References

[1]

"Complete sequence of Caldivirga maquilingensis IC-167." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700844 / DSMZ 13496 / JCM 10307 / IC-167.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000852 Genomic DNA. Translation: ABW02787.1. Different initiation.
RefSeq	YP_001541777.1. NC_009954.1.
3D structure databases
ProteinModelPortal	A8MC03.
ModBase	Search...
Protein-protein interaction databases
STRING	A8MC03.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5708445.
GenomeReviews	Gene locus Cmaq_1971 in contig CP000852_GR.
KEGG	cma:Cmaq_1971.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG672951.
ProtClustDB	CLSK899668.
Enzyme and pathway databases
BioCyc	CMAQ397948:CMAQ_1971-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_CALMQ

Accession

Primary (citable) accession number: A8MC03

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	September 23, 2008
Last modified:	January 25, 2012
This is version 33 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program