SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P25856

- G3PA1_ARATH

UniProt

P25856 - G3PA1_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic

Gene
GAPA1, GAPA, At3g26650, MLJ15.4, MLJ15_5
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH By similarity.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951NADP
Binding sitei140 – 1401NADP; via carbonyl oxygen
Active sitei213 – 2131Nucleophile By similarity
Sitei240 – 2401Activates thiol group during catalysis By similarity
Binding sitei243 – 2431Glyceraldehyde 3-phosphate By similarity
Binding sitei258 – 2581Glyceraldehyde 3-phosphate By similarity
Binding sitei294 – 2941Glyceraldehyde 3-phosphate By similarity
Binding sitei376 – 3761NADP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 722NADP

GO - Molecular functioni

  1. glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity Source: UniProtKB-EC
  2. NAD binding Source: InterPro
  3. NADP binding Source: InterPro
  4. protein binding Source: IntAct

GO - Biological processi

  1. glucose metabolic process Source: InterPro
  2. reductive pentose-phosphate cycle Source: TAIR
  3. response to cold Source: TAIR
  4. response to light stimulus Source: TAIR
  5. response to sucrose Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Calvin cycle

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciARA:AT3G26650-MONOMER.
MetaCyc:AT3G26650-MONOMER.
BRENDAi1.2.1.13. 399.
UniPathwayiUPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic (EC:1.2.1.13)
Alternative name(s):
NADP-dependent glyceraldehydephosphate dehydrogenase A subunit 1
Gene namesi
Name:GAPA1
Synonyms:GAPA
Ordered Locus Names:At3g26650
ORF Names:MLJ15.4, MLJ15_5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G26650.

Subcellular locationi

Plastidchloroplast membrane; Peripheral membrane protein. Plastidchloroplast stroma 2 Publications

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. chloroplast envelope Source: TAIR
  4. chloroplast membrane Source: UniProtKB-SubCell
  5. chloroplast stroma Source: TAIR
  6. chloroplast thylakoid membrane Source: TAIR
  7. membrane Source: TAIR
  8. stromule Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6060Chloroplast By similarityAdd
BLAST
Chaini61 – 396336Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplasticPRO_0000010416Add
BLAST

Proteomic databases

PaxDbiP25856.
PRIDEiP25856.

2D gel databases

SWISS-2DPAGEP25856.
World-2DPAGE0003:P25856.

Expressioni

Tissue specificityi

Expressed in leaves and stems.1 Publication

Inductioni

Repressed by darkness and sucrose.1 Publication

Gene expression databases

ArrayExpressiP25856.
GenevestigatoriP25856.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CP12-2Q9LZP94EBI-1554434,EBI-449218

Protein-protein interaction databases

BioGridi7607. 6 interactions.
IntActiP25856. 2 interactions.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 687
Helixi71 – 8111
Beta strandi87 – 948
Helixi99 – 1079
Turni110 – 1123
Beta strandi119 – 12911
Beta strandi132 – 1376
Helixi142 – 1443
Helixi147 – 1504
Beta strandi154 – 1574
Beta strandi159 – 1613
Helixi165 – 1739
Beta strandi177 – 1837
Beta strandi186 – 1883
Turni194 – 1963
Helixi198 – 2003
Beta strandi206 – 2094
Helixi213 – 22917
Beta strandi231 – 24111
Beta strandi248 – 2503
Turni256 – 2594
Helixi262 – 2643
Beta strandi267 – 2693
Helixi273 – 2808
Helixi282 – 2843
Turni285 – 2873
Beta strandi288 – 2969
Beta strandi301 – 31111
Helixi315 – 32713
Turni328 – 3336
Beta strandi334 – 3374
Helixi343 – 3464
Beta strandi352 – 3565
Helixi357 – 3593
Beta strandi361 – 3633
Turni364 – 3663
Beta strandi367 – 3748
Helixi378 – 39316

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K2BX-ray2.60A/B/C/D/E/F/G/H/O/Q60-396[»]
3QV1X-ray2.00A/B/C/D/E/F60-396[»]
3RVDX-ray2.70A/B/C/D/E/F/G/H/O/Q61-396[»]
ProteinModelPortaliP25856.
SMRiP25856. Positions 60-396.

Miscellaneous databases

EvolutionaryTraceiP25856.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni212 – 2143Glyceraldehyde 3-phosphate binding By similarity
Regioni271 – 2722Glyceraldehyde 3-phosphate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0057.
HOGENOMiHOG000071679.
InParanoidiP25856.
KOiK05298.
OMAiKYDSLHG.
PhylomeDBiP25856.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25856-1 [UniParc]FASTAAdd to Basket

« Hide

MASVTFSVPK GFTEFSGLRS SSASLPFGKK LSSDEFVSIV SFQTSAMGSS    50
GGYRKGVTEA KLKVAINGFG RIGRNFLRCW HGRKDSPLDI IAINDTGGVK 100
QASHLLKYDS TLGIFDADVK PSGETAISVD GKIIQVVSNR NPSLLPWKEL 150
GIDIVIEGTG VFVDREGAGK HIEAGAKKVI ITAPGKGDIP TYVVGVNADA 200
YSHDEPIISN ASCTTNCLAP FVKVLDQKFG IIKGTMTTTH SYTGDQRLLD 250
ASHRDLRRAR AAALNIVPTS TGAAKAVALV LPNLKGKLNG IALRVPTPNV 300
SVVDLVVQVS KKTFAEEVNA AFRDSAEKEL KGILDVCDEP LVSVDFRCSD 350
FSTTIDSSLT MVMGDDMVKV IAWYDNEWGY SQRVVDLADI VANNWK 396
Length:396
Mass (Da):42,490
Last modified:May 2, 2002 - v3
Checksum:iFFD7FD662FB222FC
GO

Sequence cautioni

The sequence AAD10209.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721I → M in AAA32793. 1 Publication
Sequence conflicti172 – 1721I → M in AAD10209. 1 Publication
Sequence conflicti172 – 1721I → M in CAA66816. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64114 mRNA. Translation: AAD10209.1. Different initiation.
M64117 Genomic DNA. Translation: AAA32793.1.
S45910 Genomic DNA. Translation: AAB23532.1.
X98130 Genomic DNA. Translation: CAA66816.1.
AB026648 Genomic DNA. Translation: BAB01730.1.
CP002686 Genomic DNA. Translation: AEE77191.1.
AY058140 mRNA. Translation: AAL25556.1.
AY058107 mRNA. Translation: AAL24215.1.
AF428431 mRNA. Translation: AAL16200.1.
AY075637 mRNA. Translation: AAL91645.1.
AY142053 mRNA. Translation: AAM98317.1.
PIRiJQ1285.
RefSeqiNP_566796.2. NM_113576.3.
UniGeneiAt.20459.
At.23357.
At.3405.

Genome annotation databases

EnsemblPlantsiAT3G26650.1; AT3G26650.1; AT3G26650.
GeneIDi822277.
KEGGiath:AT3G26650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64114 mRNA. Translation: AAD10209.1 . Different initiation.
M64117 Genomic DNA. Translation: AAA32793.1 .
S45910 Genomic DNA. Translation: AAB23532.1 .
X98130 Genomic DNA. Translation: CAA66816.1 .
AB026648 Genomic DNA. Translation: BAB01730.1 .
CP002686 Genomic DNA. Translation: AEE77191.1 .
AY058140 mRNA. Translation: AAL25556.1 .
AY058107 mRNA. Translation: AAL24215.1 .
AF428431 mRNA. Translation: AAL16200.1 .
AY075637 mRNA. Translation: AAL91645.1 .
AY142053 mRNA. Translation: AAM98317.1 .
PIRi JQ1285.
RefSeqi NP_566796.2. NM_113576.3.
UniGenei At.20459.
At.23357.
At.3405.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3K2B X-ray 2.60 A/B/C/D/E/F/G/H/O/Q 60-396 [» ]
3QV1 X-ray 2.00 A/B/C/D/E/F 60-396 [» ]
3RVD X-ray 2.70 A/B/C/D/E/F/G/H/O/Q 61-396 [» ]
ProteinModelPortali P25856.
SMRi P25856. Positions 60-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 7607. 6 interactions.
IntActi P25856. 2 interactions.

2D gel databases

SWISS-2DPAGE P25856.
World-2DPAGE 0003:P25856.

Proteomic databases

PaxDbi P25856.
PRIDEi P25856.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G26650.1 ; AT3G26650.1 ; AT3G26650 .
GeneIDi 822277.
KEGGi ath:AT3G26650.

Organism-specific databases

TAIRi AT3G26650.

Phylogenomic databases

eggNOGi COG0057.
HOGENOMi HOG000071679.
InParanoidi P25856.
KOi K05298.
OMAi KYDSLHG.
PhylomeDBi P25856.

Enzyme and pathway databases

UniPathwayi UPA00116 .
BioCyci ARA:AT3G26650-MONOMER.
MetaCyc:AT3G26650-MONOMER.
BRENDAi 1.2.1.13. 399.

Miscellaneous databases

EvolutionaryTracei P25856.

Gene expression databases

ArrayExpressi P25856.
Genevestigatori P25856.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR020831. 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 ]
PANTHERi PTHR10836. PTHR10836. 1 hit.
Pfami PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000149. GAP_DH. 1 hit.
PRINTSi PR00078. G3PDHDRGNASE.
SMARTi SM00846. Gp_dh_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
PROSITEi PS00071. GAPDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosomal mapping of nuclear genes encoding chloroplast and cytosolic glyceraldehyde-3-phosphate-dehydrogenase from Arabidopsis thaliana."
    Shih M.-C., Heinrich P., Goodman H.M.
    Gene 104:133-138(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Sequence analysis of an 81 kb contig from Arabidopsis thaliana chromosome III."
    Quigley F., Dao P., Cottet A., Mache R.
    Nucleic Acids Res. 24:4313-4318(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: cv. Columbia.
    Tissue: Shoot.
  3. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  7. "Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana."
    Marri L., Sparla F., Pupillo P., Trost P.
    J. Exp. Bot. 56:73-80(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  8. "Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in Arabidopsis."
    Munoz-Bertomeu J., Cascales-Minana B., Mulet J.M., Baroja-Fernandez E., Pozueta-Romero J., Kuhn J.M., Segura J., Ros R.
    Plant Physiol. 151:541-558(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase (isoform A4) from Arabidopsis thaliana in complex with NAD."
    Fermani S., Sparla F., Marri L., Thumiger A., Pupillo P., Falini G., Trost P.
    Acta Crystallogr. F 66:621-626(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 60-396 IN COMPLEX WITH NAD, SUBUNIT.
  10. "Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly."
    Fermani S., Trivelli X., Sparla F., Thumiger A., Calvaresi M., Marri L., Falini G., Zerbetto F., Trost P.
    J. Biol. Chem. 287:21372-21383(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 60-396 IN COMPLEX WITH NAD, SUBUNIT.

Entry informationi

Entry nameiG3PA1_ARATH
AccessioniPrimary (citable) accession number: P25856
Secondary accession number(s): Q41184, Q9LSE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants contain three types of GAPDH: NAD-dependent cytosolic forms which participate in glycolysis, NAD-dependent chloroplastic forms which participate in plastidic glycolysis and NADP-depedent chloroplastic forms which participate in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). All the forms are encoded by distinct genes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi