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Q6GIL8 (G3P1_STAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:SAR0828
OrganismStaphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]
Taxonomic identifier282458 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length336 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 term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 336336Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145685

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

Secondary structure

1 ......................................................................... 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6GIL8 [UniParc].

Last modified July 19, 2004. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX571856 Genomic DNA. Translation: CAG39837.1.
RefSeqYP_040254.1. NC_002952.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HQ4X-ray2.20O/P/Q/R1-336[»]
3K73X-ray2.50O/P/Q/R1-336[»]
3K9QX-ray2.50O/P/Q/R1-336[»]
3KSDX-ray2.20O/P/Q/R1-336[»]
3KSZX-ray2.60O/P/Q/R1-336[»]
3KV3X-ray2.50O/P/Q/R1-336[»]
3L4SX-ray2.20O/P/Q/R1-336[»]
3L6OX-ray2.20O/P/Q/R1-336[»]
3LC1X-ray2.00O/P/Q/R1-336[»]
3LC2X-ray2.80O/P/Q/R1-336[»]
3LC7X-ray2.50O/P/Q/R1-336[»]
3LVFX-ray1.70O/P/Q/R1-336[»]
3VAZX-ray3.19A/B/O/P/Q/R1-336[»]
ProteinModelPortalQ6GIL8.
SMRQ6GIL8. Positions 1-336.
ModBaseSearch...

Protein-protein interaction databases

STRING282458.SAR0828.

Proteomic databases

PRIDEQ6GIL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG39837; CAG39837; SAR0828.
GeneID2860688.
KEGGsar:SAR0828.
PATRIC19545193. VBIStaAur71814_0829.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHOG000071678.
KOK00134.
OMAIVYNTNH.
ProtClustDBCLSK884889.

Enzyme and pathway databases

BioCycSAUR282458:GJA5-831-MONOMER.
UniPathwayUPA00109; UER00184.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
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]
PANTHERPTHR10836. PTHR10836. 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...

Other

EvolutionaryTraceQ6GIL8.

Entry information

Entry nameG3P1_STAAR
AccessionPrimary (citable) accession number: Q6GIL8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 19, 2004
Last modified: May 1, 2013
This is version 69 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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