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Reviewed, UniProtKB/Swiss-Prot P0A037 (G3P1_STAAW)

Last modified February 9, 2010. Version 37. 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 1
      Short name=GAPDH 1
    EC=1.2.1.12
Gene names
Name: gapA1
Synonyms: gap, gapA
Ordered Locus Names: MW0734
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

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Protein attributes

Sequence length336 AA.
Sequence statusComplete.
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 – 336336Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145687

Regions

Nucleotide binding12 – 132NAD By similarity
Region150 – 1523Glyceraldehyde 3-phosphate binding By similarity
Region211 – 2122Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1511Nucleophile By similarity
Binding site341NAD By similarity
Binding site1811Glyceraldehyde 3-phosphate By similarity
Binding site1981Glyceraldehyde 3-phosphate By similarity
Binding site2341Glyceraldehyde 3-phosphate By similarity
Binding site3161NAD By similarity
Site1781Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
P0A037-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 37A6CEA9376779E5

FASTA33636,281
        10         20         30         40         50         60 
MAVKVAINGF GRIGRLAFRR IQEVEGLEVV AVNDLTDDDM LAHLLKYDTM QGRFTGEVEV 

        70         80         90        100        110        120 
VDGGFRVNGK EVKSFSEPDA SKLPWKDLNI DVVLECTGFY TDKDKAQAHI EAGAKKVLIS 

       130        140        150        160        170        180 
APATGDLKTI VFNTNHQELD GSETVVSGAS CTTNSLAPVA KVLNDDFGLV EGLMTTIHAY 

       190        200        210        220        230        240 
TGDQNTQDAP HRKGDKRRAR AAAENIIPNS TGAAKAIGKV IPEIDGKLDG GAQRVPVATG 

       250        260        270        280        290        300 
SLTELTVVLE KQDVTVEQVN EAMKNASNES FGYTEDEIVS SDVVGMTYGS LFDATQTRVM 

       310        320        330 
SVGDRQLVKV AAWYDNEMSY TAQLVRTLAY LAELSK

« 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

EMBL
GenBank
DDBJ		BA000033 Genomic DNA. Translation: BAB94599.1.
RefSeqNP_645551.1.

3D structure databases

SMRP0A037. Positions 4-334.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0A037.

Genome annotation databases

GeneID1002845.
GenomeReviewsGene locus MW0734 in contig BA000033_GR.
KEGGsam:MW0734.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHBG571736.
OMAGKQLVKT.

Enzyme and pathway databases

BioCycSAUR196620:MW0734-MONOMER.

Family and domain databases

InterProIPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020832. GlycerAld_3-P_DH_cat_sub.
IPR020831. GlycerAld_3-P_DH_family.
IPR020828. GlycerAld_3-P_DH_NAD(P)_bd.
IPR000173. GlycerAld_3-P_DH_subfam.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[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.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3P1_STAAW
AccessionPrimary (citable) accession number: P0A037
Secondary accession number(s): Q9Z5C5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: February 9, 2010
This is version 37 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