Reviewed, UniProtKB/Swiss-Prot O44104 (G3P2_DROPS)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
    EC=1.2.1.12
Alternative name(s):
    Glyceraldehyde-3-phosphate dehydrogenase II
      Short name=GAPDH II

Gene names

Name:	Gapdh2
ORF Names:	GA21397

Organism

Drosophila pseudoobscura pseudoobscura (Fruit fly) [Complete proteome]

Taxonomic identifier

46245 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Sequence caution	The sequence EAL29271.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 332	332	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145524
Regions
	Nucleotide binding	11 – 12	2	NAD By similarity
	Region	148 – 150	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	208 – 209	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	149	1	Nucleophile By similarity
	Binding site	32	1	NAD By similarity
	Binding site	77	1	NAD; via carbonyl oxygen By similarity
	Binding site	179	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	231	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	313	1	NAD By similarity
	Site	176	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O44104-1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: 9E58BEB163B59983	FASTA	332	35,312
	10 20 30 40 50 60 MSKIGINGFG RIGRLVLRAA IDKGASVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE 70 80 90 100 110 120 GGFLVVNGQK ITVFSERDPA NINWASAGAE YVVESTGVFT TIEKASTHLK GGAKKVVISA 130 140 150 160 170 180 PSADAPMFVC GVNLDAYKPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA 190 200 210 220 230 240 TQKTVDGPSG KLWRDGRGAA QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV 250 260 270 280 290 300 DLTVRLGKGA SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL 310 320 330 NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution." Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L. , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., Gibbs R.A. Genome Res. 15:1-18(2005) [PubMed: 15632085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MV2-25.
[2]	"The molecular clock revisited: the rate of synonymous vs. replacement change in Drosophila." Zeng L.-W., Comeron J.M., Chen B., Kreitman M. Genetica 102:369-382(1998) [PubMed: 9720289] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH475410 Genomic DNA. Translation: EAL29271.1. Sequence problems. AF025809 mRNA. Translation: AAB87894.1.
RefSeq	XP_001352353.1.
3D structure databases
HSSP	HSSP built from PDB template 1DSS based on UniProtKB P56649.
SMR	O44104. Positions 2-332.
ModBase	Search...
Genome annotation databases
GeneID	4811785.
KEGG	dpo:Dpse_GA21397.
Organism-specific databases
FlyBase	FBgn0012698. Dpse\Gapdh2.
Phylogenomic databases
OMA	O44104. SRDDIEV.
Enzyme and pathway databases
BRENDA	1.2.1.12. 190795.
Family and domain databases
InterPro	IPR000173. GlycerAld_3-P_DH. IPR006424. Glyceraldehyde-3-P_DH_1. [Graphical view]
PANTHER	PTHR10836. GAP_DH. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P2_DROPS

Accession

Primary (citable) accession number: O44104
Secondary accession number(s): Q29CT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project