ID   GCST_MESCR              Reviewed;         408 AA.
AC   P93256;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Aminomethyltransferase, mitochondrial;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
DE            Short=GCVT;
DE   Flags: Precursor;
GN   Name=GDCST;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Michalowski C.B., Bohnert H.J.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC         aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC         5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC         NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U79769; AAB38502.1; -; mRNA.
DR   PIR; T12566; T12566.
DR   AlphaFoldDB; P93256; -.
DR   SMR; P93256; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   InterPro; IPR006223; GCS_T.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; PTHR43757; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Mitochondrion; Transferase; Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..408
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010762"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  44406 MW;  2C40133E69714FA2 CRC64;
     MRGGGLWQLG QSVTRRLAQA EKKVIARRCF ASEADLKKTA LYDFHVANGG KMVPFAGWSM
     PIQYKDSIMD STINCRENGS LFDVAHMCGL SLKGKDCIPF LEKLVVGDIA GLAPGTGTLS
     VLTNEKGGAI DDTVITKVTD DHIYLVVNAG CREKDLAHIE EHMKAFKAKG GDVSWHIHDE
     RSLLALQGPL AAPVLQHLTK EDLSKFYFGQ FTFLDINGFP CYLTRTGYTG EDGFEISVPN
     EYAVDLAKAM LEKSEGKVRL TGRGARDSLR LEAGLCLYGN DLEQHITPIE AGLTWAVGKR
     RRAEGGFLGA EVILKQIADG PPQRRVGFIS SGPPARGHSE IQNEKGESIG EITSGGFSPC
     LKKNIAMGYV KSGNHKAGTK VNILVRGKPY EGVVTKMPFV PTKYYKSP