ID   GCST_FLATR              Reviewed;         407 AA.
AC   O23936;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Flaveria trinervia (Clustered yellowtops) (Oedera trinervia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Tageteae; Flaveria.
OX   NCBI_TaxID=4227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RA   Cossu R., Bauwe H.;
RT   "The GDCST gene encoding T-protein of the glycine cleavage system in the C4
RT   plant Flaveria trinervia.";
RL   (er) Plant Gene Register PGR98-007(1998).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine.
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}.
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DR   EMBL; Z99769; CAB16917.1; -; Genomic_DNA.
DR   AlphaFoldDB; O23936; -.
DR   SMR; O23936; -.
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   3: Inferred from homology;
KW   Aminotransferase; Mitochondrion; Transferase; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..407
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010761"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  44285 MW;  08E3DD9C329F9891 CRC64;
     MRGGLWQVGQ SITRRLGQSD KKTIVRRWYA SEADLKKTVL YDFHVANGGK MVPFAGWSMP
     IQYKDSIMES TINCRENGSL FDVSHMCGLS LKGKDCVAFL EKLVVADVAG LAPGTGSLTV
     FTNEKGGAID DSVITKVTDD HIYLVVNAGC RDKDLAHIEQ HMKAFKAKGG DVSWHIHDER
     SLLALQGPLA GSTLQHLTKD DLSKMYFGDF RIIDISGSKC FLTRTGYTGE DGFEISVPSE
     NAVDLAKAIL EKSEGKVRLT GLGARDSLRL EAGLCLYGND MEQHITPVEA GLTWAIGKRR
     RAEGGFLGAE VILKQIADGP AIRRVGLFST GPPARSHSEI QNEQGENIGE VTSGGFSPCL
     KKNIGMGYVK SGLHKPGTKL KIVIRGKTYE GSVTKMPFVP TKYYKPA