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Q59931 (GAPN_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
EC=1.2.1.9
Alternative name(s):
Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]
Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
Triosephosphate dehydrogenase
Gene names
Name:gapN
Ordered Locus Names:SMU_676
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH.

Subunit structure

Homotetramer. Ref.3

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
PRO_0000056579

Regions

Nucleotide binding230 – 25122NADP
Region154 – 1552Substrate binding
Region283 – 2853Substrate binding

Sites

Active site2501 By similarity
Active site2841 By similarity
Binding site1031Substrate
Binding site1511NADP
Binding site1771NADP
Binding site1801NADP
Binding site2151NADP
Binding site3771NADP
Binding site4371Substrate

Experimental info

Sequence conflict581S → A in AAA91091. Ref.1
Sequence conflict851V → I in AAA91091. Ref.1
Sequence conflict3471A → T in AAA91091. Ref.1

Secondary structure

1 ................................................................................. 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59931 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: F0A2770AB89552DC

FASTA47551,194
        10         20         30         40         50         60 
MTKQYKNYVN GEWKLSENEI KIYEPASGAE LGSVPAMSTE EVDYVYASAK KAQPAWRSLS 

        70         80         90        100        110        120 
YIERAAYLHK VADILMRDKE KIGAVLSKEV AKGYKSAVSE VVRTAEIINY AAEEGLRMEG 

       130        140        150        160        170        180 
EVLEGGSFEA ASKKKIAVVR REPVGLVLAI SPFNYPVNLA GSKIAPALIA GNVIAFKPPT 

       190        200        210        220        230        240 
QGSISGLLLA EAFAEAGLPA GVFNTITGRG SEIGDYIVEH QAVNFINFTG STGIGERIGK 

       250        260        270        280        290        300 
MAGMRPIMLE LGGKDSAIVL EDADLELTAK NIIAGAFGYS GQRCTAVKRV LVMESVADEL 

       310        320        330        340        350        360 
VEKIREKVLA LTIGNPEDDA DITPLIDTKS ADYVEGLIND ANDKGAAALT EIKREGNLIC 

       370        380        390        400        410        420 
PILFDKVTTD MRLAWEEPFG PVLPIIRVTS VEEAIEISNK SEYGLQASIF TNDFPRAFGI 

       430        440        450        460        470 
AEQLEVGTVH INNKTQRGTD NFPFLGAKKS GAGIQGVKYS IEAMTTVKSV VFDIK

« Hide

References

« Hide 'large scale' references
[1]"Sequence, expression, and function of the gene for the nonphosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus mutans."
Boyd D.A., Cvitkovitch D.G., Hamilton I.R.
J. Bacteriol. 177:2622-2627(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NG5 / Serotype c.
[2]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.
[3]"Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans."
Cobessi D., Tete-Favier F., Marchal S., Azza S., Branlant G., Aubry A.
J. Mol. Biol. 290:161-173(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH NADP, HOMOTETRAMERIZATION.
[4]"Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans."
Cobessi D., Tete-Favier F., Marchal S., Branlant G., Aubry A.
J. Mol. Biol. 300:141-152(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.
[5]"Invariant Thr244 is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans."
Pailot A., D'Ambrosio K., Corbier C., Talfournier F., Branlant G.
Biochem. J. 400:521-530(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L38521 Genomic DNA. Translation: AAA91091.1.
AE014133 Genomic DNA. Translation: AAN58410.1.
PIRA57151.
RefSeqNP_721104.1. NC_004350.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUHX-ray1.82A/B/C/D1-475[»]
1QI1X-ray3.00A/B/C/D1-475[»]
1QI6X-ray2.50A/B/C/D1-475[»]
2ESDX-ray2.55A/B/C/D1-475[»]
2EUHX-ray2.60A/B/C/D1-475[»]
2ID2X-ray2.50A/B/C/D1-475[»]
2QE0X-ray2.19A/B/C/D1-475[»]
ProteinModelPortalQ59931.
SMRQ59931. Positions 2-475.
ModBaseSearch...

Protein-protein interaction databases

STRING210007.SMU.676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58410; AAN58410; SMU_676.
GeneID1028095.
KEGGsmu:SMU_676.
PATRIC19663537. VBIStrMut61772_0601.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
KOK00131.
OMAYLHKVAD.
ProtClustDBCLSK873260.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13095.
SABIO-RKQ59931.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ59931.

Entry information

Entry nameGAPN_STRMU
AccessionPrimary (citable) accession number: Q59931
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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