Skip Header

Contribute Send feedback
Read comments (?) or add your own

P12860 (G3PB_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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 B, chloroplastic
EC=1.2.1.13
Alternative name(s):
NADP-dependent glyceraldehydephosphate dehydrogenase subunit B
Gene names
Name:GAPB
Synonyms:GPB1
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH.

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Tetramer of either four A chains (GAPDH 2) or two A and two B chains (GAPDH 1).

Subcellular location

Plastid › chloroplast.

Miscellaneous

Plants contain three forms of GAPDH: a cytosolic form which participates in glycolysis and two chloroplast forms which participates in photosynthesis. These three forms are encoded by distinct genes.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processCalvin cycle
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processglucose metabolic process

Inferred from electronic annotation. Source: InterPro

reductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

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 (NADP+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8383Chloroplast
Chain84 – 451368Glyceraldehyde-3-phosphate dehydrogenase B, chloroplastic
PRO_0000010426

Regions

Nucleotide binding94 – 952NADP By similarity
Region237 – 2393Glyceraldehyde 3-phosphate binding By similarity
Region296 – 2972Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site2381Nucleophile By similarity
Binding site1181NADP By similarity
Binding site1631NADP; via carbonyl oxygen By similarity
Binding site2681Glyceraldehyde 3-phosphate By similarity
Binding site2831Glyceraldehyde 3-phosphate By similarity
Binding site3191Glyceraldehyde 3-phosphate By similarity
Binding site4021NADP By similarity
Site2651Activates thiol group during catalysis By similarity

Secondary structure

1 .................................................................. 451
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12860 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 45D826A6DA5B4837

FASTA45148,126
        10         20         30         40         50         60 
MASHAALAPS RIPASTRLAS KASQQYSFLT QCSFKRLDVA DFSGLRSSNS VTFTREASFH 

        70         80         90        100        110        120 
DVIAAQLTTK PTGAAPVRGE TVAKLKVAIN GFGRIGRNFL RCWHGRKDSP LDVVVVNDSG 

       130        140        150        160        170        180 
GVKSATHLLK YDSILGTFKA DVKIIDNETF SIDGKPIKVV SNRDPLKLPW AELGIDIVIE 

       190        200        210        220        230        240 
GTGVFVDGPG AGKHIQAGAK KVIITAPAKG SDIPTYVVGV NEKDYGHDVA NIISNASCTT 

       250        260        270        280        290        300 
NCLAPFVKVL DEELGIVKGT MTTTHSYTGD QRLLDASHRD LRRARAAALN IVPTSTGAAK 

       310        320        330        340        350        360 
AVSLVLPQLK GKLNGIALRV PTPNVSVVDL VVNIEKVGVT AEDVNNAFRK AAAGPLKGVL 

       370        380        390        400        410        420 
DVCDIPLVSV DFRCSDFSST IDSSLTMVMG GDMVKVVAWY DNEWGYSQRV VDLADLVANK 

       430        440        450 
WPGLEGSVAS GDPLEDFCKD NPADEECKLY E

« Hide

References

[1]"Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach."
Brinkmann H., Cerff R., Salomon M., Soll J.
Plant Mol. Biol. 13:81-94(1989) [PubMed: 2562762] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Seedling.
[2]"Functional studies of chloroplast glyceraldehyde-3-phosphate dehydrogenase subunits A and B expressed in Escherichia coli: formation of highly active A4 and B4 homotetramers and evidence that aggregation of the B4 complex is mediated by the B subunit carboxy terminus."
Baalmann E., Scheibe R., Cerff R., Martin W.
Plant Mol. Biol. 32:505-513(1996) [PubMed: 8980499] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II."
Ferri G., Stoppini M., Meloni M.L., Zapponi M.C., Iadarola P.
Biochim. Biophys. Acta 1041:36-42(1990) [PubMed: 2223845] [Abstract]
Cited for: PROTEIN SEQUENCE OF 83-451.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X15189 mRNA. Translation: CAA33263.1.
L76553 mRNA. Translation: AAD10218.1.
PIRDESPGB. S05553.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PKQX-ray3.60O/Q/T84-451[»]
ProteinModelPortalP12860.
SMRP12860. Positions 84-426.
ModBaseSearch...

Protein-protein interaction databases

IntActP12860. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
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 nameG3PB_SPIOL
AccessionPrimary (citable) accession number: P12860
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 14, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents