Reviewed, UniProtKB/Swiss-Prot Q6G8N9 (G3P2_STAAS)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
      Short name=GAPDH 2
    EC=1.2.1.12

Gene names

Name:	gapA2
Synonyms:	gapB
Ordered Locus Names:	SAS1615

Organism

Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]

Taxonomic identifier

282459 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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 – 341	341	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145695
Regions
	Nucleotide binding	12 – 13	2	NAD By similarity
	Region	152 – 154	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	211 – 212	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	153	1	Nucleophile By similarity
	Binding site	78	1	NAD; via carbonyl oxygen By similarity
	Binding site	183	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	198	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	234	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	313	1	NAD By similarity
	Site	180	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G8N9-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 0757DE38BC89F14C	FASTA	341	36,979
	10 20 30 40 50 60 MSTNIAINGM GRIGRMVLRI ALQNKNLNVV AINASYPPET IAHLINYDTT HGKYNLKVEP 70 80 90 100 110 120 IENGLQVGDH KIKLVADRNP ENLPWKELDI DIAIDATGKF NHGDKAIAHI KAGAKKVLLT 130 140 150 160 170 180 GPSKGGHVQM VVKGVNDNQL DIEAFDIFSN ASCTTNCIGP VAKVLNNQFG IVNGLMTTVH 190 200 210 220 230 240 AITNDQKNID NPHKDLRRAR SCNESIIPTS TGAAKALKEV LPELEGKLHG MALRVPTKNV 250 260 270 280 290 300 SLVDLVVDLE KEVTAEEVNQ AFENAGLEGI IEVEHQPLVS VDFNTNPNSA IIDAKSTMVM 310 320 330 340 SGNKVKVIAW YDNEWGYSNR VVDVAEQIGA LLTSKETVSA S

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571857 Genomic DNA. Translation: CAG43417.1.
RefSeq	YP_043734.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6G8N9.
Genome annotation databases
GeneID	2863482.
GenomeReviews	Gene locus SAS1615 in contig BX571857_GR.
KEGG	sas:SAS1615.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6G8N9.
OMA	TNPHSAI.
Enzyme and pathway databases
BioCyc	SAUR282459:SAS1615-MON.
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_STAAS

Accession

Primary (citable) accession number: Q6G8N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)