NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-55.
TISSUE=Liver;
PubMed=2002038 [NCBI, ExPASy, EBI, Israel, Japan]
Okamura-Ikeda K., Fujiwara K., Yamamoto M., Hiraga K., Motokawa Y.;
"Isolation and sequence determination of cDNA encoding T-protein of the glycine cleavage system.";
J. Biol. Chem. 266:4917-4921(1991).

Comments

FUNCTION: The glycine cleavage system catalyzes the degradation of glycine.
CATALYTIC ACTIVITY: [Protein]-S⁸-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH₃.
SUBUNIT: The glycine cleavage system is composed of four proteins: P, T, L and H.
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the gcvT family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M59799; AAA30786.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A23707; A23707.

NP_803451.1; -.

3D structure databases

SMR

P25285; 26-396.

ModBase

P25285.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (traceable author statement from AgBase).
GO:0004047;	Molecular function: aminomethyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031405;	Molecular function: lipoic acid binding (inferred from direct assay from AgBase).
GO:0008483;	Molecular function: transaminase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006546;	Biological process: glycine catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013977; GCV_T_C.
IPR006222; GCV_T_N.
IPR006223; GcvT.
Graphical view of domain structure.

Pfam

PF01571; GCV_T; 1.
PF08669; GCV_T_C; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF006487; GcvT; 1.

TIGRFAMs

TIGR00528; gcvT; 1.

ProtoNet

P25285.

Genome annotation databases

Ensembl

ENSBTAG00000002321; Bos taurus. [Contig view]

GeneID

280719; -.

KEGG

bta:280719; -.

Phylogenomic databases

HOVERGEN

P25285; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aminotransferase; Direct protein sequencing; Mitochondrion; Transferase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 22`	`22`	`Mitochondrion.`
`CHAIN`	`23 397`	`375`	`Aminomethyltransferase, mitochondrial.`	`PRO_0000010753`

Sequence information

Length: 397 AA [This is the length of the unprocessed precursor]

Molecular weight: 42869 Da [This is the MW of the unprocessed precursor]

CRC64: 3FE5D598B78AB6FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSRLSSRLQ ALASAPCRSL SCAQDVLHRT PLYDFHLAHG GKMVAFAGWS LPVQYRDSHV 

        70         80         90        100        110        120 
NSHLHTRQHC SLFDVSHMLQ TKIFGCDRVK LMESLVVGDI AELKPNQGTL SLFTNEAGGI 

       130        140        150        160        170        180 
LDDLIVTSAS EGHLYVVSNA GCREKDLTLM QDKVRELQNK GSDVALEVMD NALLALQGPT 

       190        200        210        220        230        240 
AAQVLQAGVA DDLRKLPFMT SAVMEVFGVS GCRVTRCGYT GEDGVEISVP AAEAVHLAAA 

       250        260        270        280        290        300 
LLKNPEVKLA GLAARDSLRL EAGLCLYGND IDEHTTPVEG SLSWTLGKRR RAAMDFPGAS 

       310        320        330        340        350        360 
VIVPQLKSKA QRRRVGLMCD GAPVRAQSPI LSPEGTVIGA VTSGCPSPCL KKNVAMGYVP 

       370        380        390 
YEYSRPGTPL LVEVRRKQQP AVVSKMPFVS TNYYILK

P25285 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools