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P49364 (GCST_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Aminomethyltransferase, mitochondrial

EC=2.1.2.10
Alternative name(s):
Glycine cleavage system T protein
Short name=GCVT
Gene names
Name:GDCST
Synonyms:GDCT
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Mitochondrion.

Sequence similarities

Belongs to the GcvT family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionAminotransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglycine catabolic process

Inferred from electronic annotation. Source: InterPro

methylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentglycine cleavage complex

Inferred from direct assay PubMed 3143355. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminomethyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

transaminase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion
Chain31 – 408378Aminomethyltransferase, mitochondrial
PRO_0000010763

Sites

Binding site2351Substrate By similarity
Binding site2661Substrate By similarity
Binding site4041Substrate By similarity

Experimental info

Sequence conflict981V → I in CAA52800. Ref.1
Sequence conflict1141H → N in CAA52800. Ref.1
Sequence conflict1401D → E in CAA52800. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49364 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 41BB4724AC910793

FASTA40844,285
        10         20         30         40         50         60 
MRGGLWQLGQ SITRRLANGG DKKAVARRCF ATESELKKTV LYDFHVAHGG KMVPFAGWSM 

        70         80         90        100        110        120 
PIQYKDSIMD STLNCRQNGS LFDVSHMCGL SLKGKDVVSF LEKLVIADVA ALAHGTGTLT 

       130        140        150        160        170        180 
VFTNEKGGAI DDSVITKVTD DHLYLVVNAG CRDKDLAHIE EHMKAFKAKG GDVSWHIHDE 

       190        200        210        220        230        240 
RSLLALQGPL AAPVLQHLTK EDLSKLYFGE FRVLDINGSQ CFLTRTGYTG EDGFEISVPS 

       250        260        270        280        290        300 
EHGVELAKAL LEKSEGKIRL TGLGARDSLR LEAGLCLYGN DLEQHITPIE AGLTWAIGKR 

       310        320        330        340        350        360 
RRAEGGFLGA DVILKQLADG PSIRRVGFIS SGPPPRSHSE IQDEGGNNIG EVTSGGFSPC 

       370        380        390        400 
LKKNIAIGYV KSGLHKAGTK VKIIIRGKQN EGVVTKMPFV PTKYYKPS 

« Hide

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.
PIRS38370.
S56661.

3D structure databases

ProteinModelPortalP49364.
SMRP49364. Positions 36-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49364. 1 interaction.

Proteomic databases

PRIDEP49364.
ProMEXP49364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.1360.120. 2 hits.
InterProIPR006223. GCS_T.
IPR013977. GCV_T_C.
IPR006222. GCV_T_N.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]
PANTHERPTHR13847:SF5. PTHR13847:SF5. 1 hit.
PfamPF01571. GCV_T. 1 hit.
PF08669. GCV_T_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00528. gcvT. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCST_PEA
AccessionPrimary (citable) accession number: P49364
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 15, 1998
Last modified: March 19, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families