ID   GCST_FLAPR              Reviewed;         407 AA.
AC   P49363;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
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 pringlei.
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=4226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=7766903; DOI=10.1007/bf00020895;
RA   Kopriva S., Turner S.R., Rawsthorne S., Bauwe H.;
RT   "T-protein of the glycine decarboxylase multienzyme complex: evidence for
RT   partial similarity to formyltetrahydrofolate synthetase.";
RL   Plant Mol. Biol. 27:1215-1220(1995).
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; Z25858; CAA81077.1; -; mRNA.
DR   PIR; S56660; S56660.
DR   AlphaFoldDB; P49363; -.
DR   SMR; P49363; -.
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..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..407
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010760"
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;  44353 MW;  8B87F7EBE679F7C0 CRC64;
     MRGGLWQLGQ SITRRLGQSD KKTIARRCYA SEADLKKTVL YDFHVANGGK MVPFAGWSMP
     IQYKDSIMES TINCRENGSL FDVSHMCGLS LKGKDCVPFL EKLVVADVAG LRPGTGSLTV
     FTNEKGGAID DSVITKVTDD HIYLVVNAGC RDKDLAHIEE HMKAFKAKGG DVSWHIYDER
     SLLALQGPLA GSTLQHLTKE DLSKMYFGDF RIIDINGSKC FLTRTGYTGE DGFEISVPSE
     NAVDLAKAIL EKSEGKVRLT GLGARDSLRL EAGLCLYGND MEQHITPVEA GLTWAIGKRR
     RAEGGFLGAD VILKQIADGP AIRRVGLFST GPPARSHSEI QNEKGENIGE VTSGGFSPCL
     KKNIGMGYVK SGLHKPGTKL KIVIRGKTYE GSVTKMPFVP TKYYKPA