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P99067 (G3P2_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase 2
Short name=GAPDH 2
EC=1.2.1.12
Gene names
Name:gapA2
Synonyms:gapB
Ordered Locus Names:SA1510
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145693

Regions

Nucleotide binding12 – 132NAD By similarity
Region152 – 1543Glyceraldehyde 3-phosphate binding By similarity
Region211 – 2122Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1531Nucleophile By similarity
Binding site781NAD; via carbonyl oxygen By similarity
Binding site1831Glyceraldehyde 3-phosphate By similarity
Binding site1981Glyceraldehyde 3-phosphate By similarity
Binding site2341Glyceraldehyde 3-phosphate By similarity
Binding site3131NAD By similarity
Site1801Activates thiol group during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P99067 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 0757DE38BC89F14C

FASTA34136,979
        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

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000018 Genomic DNA. Translation: BAB42777.1.
PIRD89952.
RefSeqNP_374798.1. NC_002745.2.

3D structure databases

ProteinModelPortalP99067.
SMRP99067. Positions 2-330.
ModBaseSearch...

Protein-protein interaction databases

STRINGP99067.

2D gel databases

SWISS-2DPAGEP99067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000001631; EBSTAP00000001631; EBSTAG00000001631.
GeneID1124355.
GenomeReviewsGene locus SA1510 in contig BA000018_GR.
KEGGsau:SA1510.
PATRIC19575320. VBIStaAur116463_1630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0057.
GeneTreeEBGT00050000024492.
HOGENOMHBG571736.
OMAYDIFSNA.
PhylomeDBP99067.
ProtClustDBCLSK885496.

Enzyme and pathway databases

BioCycSAUR158879:SA1510-MONOMER.

Family and domain databases

InterProIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00134.
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P2_STAAN
AccessionPrimary (citable) accession number: P99067
Secondary accession number(s): Q99TH5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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