Reviewed, UniProtKB/Swiss-Prot Q6FWJ7 (GPD2_CANGA)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD+] 2
    EC=1.1.1.8

Gene names

Name:	GPD2
Ordered Locus Names:	CAGL0C05137g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH.
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 422	422	Glycerol-3-phosphate dehydrogenase [NAD+] 2		PRO_0000138087
Regions
	Nucleotide binding	69 – 74	6	NAD By similarity
	Region	338 – 339	2	Substrate binding By similarity
Sites
	Active site	273	1	Proton acceptor By similarity
	Binding site	157	1	NAD By similarity
	Binding site	180	1	NAD; via amide nitrogen By similarity
	Binding site	180	1	Substrate By similarity
	Binding site	213	1	NAD; via amide nitrogen By similarity
	Binding site	338	1	NAD By similarity
	Binding site	367	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FWJ7-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 4BDF81C8757F3EB9	FASTA	422	47,005
	10 20 30 40 50 60 MFVRLARIPR ITRHYRLGLF STQPKPKPNE YLYYRNKHKS KMEAPIKRSS SAVSLVELER 70 80 90 100 110 120 EPFKVTVIGS GNWGTTIAKV VAENTKANPQ VFQERVDMWV FDENIDGTML TEIINTKHQN 130 140 150 160 170 180 VKYLPNIDLP ENLVANPDLL KSVEGADILV FNIPHQFLPK IVDQLRGHVE PHVRAISCLK 190 200 210 220 230 240 GFEVGKKGVQ LLSTYITEEL GIECGALSGA NLAPEVAKEH WSETTVAYHI PKDYQGDGMD 250 260 270 280 290 300 VDHKVLKLLF HRPYFHVSVI DDVAGISIAG ALKNVVALGC GFVEGLGWGN NAAAAIQRVG 310 320 330 340 350 360 LGEIIKFGQM FFPESRVETY YQESAGVADL ITTCSGGRNV RVATHMAKTG KSAEDSEKEL 370 380 390 400 410 420 LNGQSAQGVI TCKEVHEWLS TCEMIEEFPL FEAVYKIVYE DVPMHKLPEM IEELDDIVVA GQ

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380949 Genomic DNA. Translation: CAG58303.1.
RefSeq	XP_445397.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2886789.
KEGG	cgr:CAGL0C05137g.
Phylogenomic databases
HOGENOM	Q6FWJ7.
Family and domain databases
InterPro	IPR013328. DHase_multihelical. IPR016040. NAD(P)-bd. IPR017751. NAD-dep_Gly3P_DH_euk. IPR006168. NAD-dep_Gly3P_DHase. IPR011128. NAD-dep_Gly3P_DHase_N. IPR006109. NAD_Gly3P_DHase_C. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR11728. NAD_Gly3P_DH. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
ProDom	PD001278. NAD_Gly3P_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPD2_CANGA

Accession

Primary (citable) accession number: Q6FWJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 19, 2004
Last modified:	November 25, 2008
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)