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Protein

Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic

Gene

GAPA

Organism
Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121NADPBy similarity
Binding sitei156 – 1561NADP; via carbonyl oxygenBy similarity
Active sitei231 – 2311NucleophilePROSITE-ProRule annotation
Sitei258 – 2581Activates thiol group during catalysisBy similarity
Binding sitei261 – 2611Glyceraldehyde 3-phosphateBy similarity
Binding sitei276 – 2761Glyceraldehyde 3-phosphateBy similarity
Binding sitei312 – 3121Glyceraldehyde 3-phosphateBy similarity
Binding sitei394 – 3941NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 892NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Calvin cycle

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic (EC:1.2.1.13)
Alternative name(s):
NADP-dependent glyceraldehydephosphate dehydrogenase
Gene namesi
Name:GAPA
OrganismiChondrus crispus (Carrageen Irish moss) (Polymorpha crispa)
Taxonomic identifieri2769 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaFlorideophyceaeGigartinalesGigartinaceaeChondrus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7676ChloroplastSequence analysisAdd
BLAST
Chaini77 – 414338Glyceraldehyde-3-phosphate dehydrogenase, chloroplasticPRO_0000010419Add
BLAST

Proteomic databases

PRIDEiP34919.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP34919.
SMRiP34919. Positions 78-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 2323Glyceraldehyde 3-phosphate bindingBy similarity
Regioni289 – 2902Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

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]
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
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.

P34919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFVAPVATV RATTKSSVCQ VQGRSTFAQF SGMKKVNQSS RLQPAQSGSA
60 70 80 90 100
FGGYSDANDA FYTRVSGIVA ATFGPTMKVR VAINGFGRIG RNFIRCWAGR
110 120 130 140 150
SDSNMEVVCI NDTSGVKTAS HLLKYDSILG TFDADVSAGE DTISVNGKTI
160 170 180 190 200
KIVSNRNPLQ LPWKEMNIDI VVEATGVFVD APGAGKHIEA GAKKVLITAP
210 220 230 240 250
GKGDGIGTFV VGVNEKDYSH DKYDIVSNAS CTTNCMAPFM KVLDDEFGVV
260 270 280 290 300
RGMMTTTHSY TGDQRLLDAG HRDLRRARSA ALNIVPTTTG AAKAVALVVP
310 320 330 340 350
SLKGKLNGIA LRVPTPNVSV CDVVMQVNKK TFKEEVNGAL LKASEGAMKG
360 370 380 390 400
IIKYSDEPLV SCDHRGTDES TIIDSSLTMV MGDDMIKVVA WYDNEWGYSQ
410
RVVDLGEVMA RQWK
Length:414
Mass (Da):44,459
Last modified:February 1, 1994 - v1
Checksum:i065DE62CE1064111
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73035 mRNA. Translation: CAA51516.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73035 mRNA. Translation: CAA51516.1.

3D structure databases

ProteinModelPortaliP34919.
SMRiP34919. Positions 78-414.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP34919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00116.

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]
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The evolutionary origin of red algae as deduced from the nuclear genes encoding cytosolic and chloroplast glyceraldehyde-3-phosphate dehydrogenases from Chondrus crispus."
    Liaud M.-F., Valentin C., Martin W., Bouget F.Y., Kloareg B., Cerff R.
    J. Mol. Evol. 38:319-327(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Stackhouse.

Entry informationi

Entry nameiG3PA_CHOCR
AccessioniPrimary (citable) accession number: P34919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 9, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.