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Reviewed, UniProtKB/Swiss-Prot P64181 (G3P2_STAAW)

Last modified June 16, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: MW1630
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

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Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145696

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

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Sequences

Sequence LengthMass (Da)Tools
P64181-1 [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

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References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

BA000033 Genomic DNA. Translation: BAB95495.1.
RefSeqNP_646447.1.

3D structure databases

HSSPHSSP built from PDB template 1GD1 based on UniProtKB P00362.
ModBaseSearch...

Genome annotation databases

GeneID1003742.
GenomeReviewsGene locus MW1630 in contig BA000033_GR.
KEGGsam:MW1630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP64181.
OMAP64181. TNPHSAI.

Enzyme and pathway databases

BioCycSAUR196620:MW1630-MON.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]
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.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3P2_STAAW
AccessionPrimary (citable) accession number: P64181
Secondary accession number(s): Q99TH5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents