P49364 (GCST_PEA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 73.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Aminomethyltransferase, mitochondrial EC=2.1.2.10 Alternative name(s): Glycine cleavage system T protein Short name=GCVT | ||||
| Gene names |
| ||||
| Organism | Pisum sativum (Garden pea) | ||||
| Taxonomic identifier | 3888 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum![]() |
Protein attributes
| Sequence length | 408 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The glycine cleavage system catalyzes the degradation of glycine. |
| Catalytic activity | [Protein]-S(8)-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3. |
| Subunit structure | The glycine cleavage system is composed of four proteins: P, T, L and H. |
| Subcellular location | |
| Sequence similarities | Belongs to the GcvT family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Molecular function | Aminotransferase Transferase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | glycine catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | glycine cleavage complex Inferred from direct assay PubMed 3143355. Source: UniProtKB mitochondrionInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | aminomethyltransferase activity Inferred from electronic annotation. Source: EC transaminase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 30 | 30 | Mitochondrion | ||||||
| Chain | 31 – 408 | 378 | Aminomethyltransferase, mitochondrial | PRO_0000010763 | |||||
Sites | |||||||||
| Binding site | 235 | 1 | Substrate By similarity | ||||||
| Binding site | 266 | 1 | Substrate By similarity | ||||||
| Binding site | 404 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 98 | 1 | V → I in CAA52800. Ref.1 | ||||||
| Sequence conflict | 114 | 1 | H → N in CAA52800. Ref.1 | ||||||
| Sequence conflict | 140 | 1 | D → E in CAA52800. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Glycine decarboxylase complex from higher plants. Molecular cloning, tissue distribution and mass spectrometry analyses of the T protein." Bourguignon J., Vauclare P., Merand V., Forest E., Neuburger M., Douce R. Eur. J. Biochem. 217:377-386(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Leaf. |
| [2] | "T-protein of the glycine decarboxylase multienzyme complex: evidence for partial similarity to formyltetrahydrofolate synthetase." Kopriva S., Turner S.R., Rawsthorne S., Bauwe H. Plant Mol. Biol. 27:1215-1220(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf. |
| [3] | "The gene encoding T protein of the glycine decarboxylase complex involved in the mitochondrial step of the photorespiratory pathway in plants exhibits features of light-induced genes." Vauclare P., Macherel D., Douce R., Bourguignon J. Plant Mol. Biol. 37:309-318(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X74793 mRNA. Translation: CAA52800.1. Z25861 mRNA. Translation: CAA81080.1. AJ222771 Genomic DNA. Translation: CAA10976.1. |
| PIR | S38370. S56661. |
3D structure databases | |
| ProteinModelPortal | P49364. |
| SMR | P49364. Positions 36-406. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P49364. 1 interaction. |
Proteomic databases | |
| PRIDE | P49364. |
| ProMEX | P49364. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.30.1360.120. 2 hits. |
| InterPro | IPR013977. GCV_T_C. IPR006222. GCV_T_N. IPR006223. GcvT. IPR027266. TrmE/GcvT_dom1. [Graphical view] |
| PANTHER | PTHR13847:SF5. PTHR13847:SF5. 1 hit. |
| Pfam | PF01571. GCV_T. 1 hit. PF08669. GCV_T_C. 1 hit. [Graphical view] |
| PIRSF | PIRSF006487. GcvT. 1 hit. |
| TIGRFAMs | TIGR00528. gcvT. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GCST_PEA | ||||||||
| Accession | Primary (citable) accession number: P49364 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
