ID   GCST_PEA                Reviewed;         408 AA.
AC   P49364;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   24-JAN-2024, entry version 109.
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; Synonyms=GDCT;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=8223576; DOI=10.1111/j.1432-1033.1993.tb18256.x;
RA   Bourguignon J., Vauclare P., Merand V., Forest E., Neuburger M., Douce R.;
RT   "Glycine decarboxylase complex from higher plants. Molecular cloning,
RT   tissue distribution and mass spectrometry analyses of the T protein.";
RL   Eur. J. Biochem. 217:377-386(1993).
RN   [2]
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9617803; DOI=10.1023/a:1005954200042;
RA   Vauclare P., Macherel D., Douce R., Bourguignon J.;
RT   "The gene encoding T protein of the glycine decarboxylase complex involved
RT   in the mitochondrial step of the photorespiratory pathway in plants
RT   exhibits features of light-induced genes.";
RL   Plant Mol. Biol. 37:309-318(1998).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-
CC         aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-
CC         methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC         lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC         Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57453, 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; X74793; CAA52800.1; -; mRNA.
DR   EMBL; Z25861; CAA81080.1; -; mRNA.
DR   EMBL; AJ222771; CAA10976.1; -; Genomic_DNA.
DR   PIR; S38370; S38370.
DR   PIR; S56661; S56661.
DR   AlphaFoldDB; P49364; -.
DR   SMR; P49364; -.
DR   IntAct; P49364; 1.
DR   BRENDA; 1.4.1.27; 4872.
DR   SABIO-RK; P49364; -.
DR   GO; GO:0005960; C:glycine cleavage complex; IDA:UniProtKB.
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; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 4.10.1250.10; Aminomethyltransferase fragment; 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   NCBIfam; TIGR00528; gcvT; 1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Mitochondrion; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT   CHAIN           31..408
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010763"
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"
FT   CONFLICT        98
FT                   /note="V -> I (in Ref. 1; CAA52800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="H -> N (in Ref. 1; CAA52800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="D -> E (in Ref. 1; CAA52800)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  44285 MW;  41BB4724AC910793 CRC64;
     MRGGLWQLGQ SITRRLANGG DKKAVARRCF ATESELKKTV LYDFHVAHGG KMVPFAGWSM
     PIQYKDSIMD STLNCRQNGS LFDVSHMCGL SLKGKDVVSF LEKLVIADVA ALAHGTGTLT
     VFTNEKGGAI DDSVITKVTD DHLYLVVNAG CRDKDLAHIE EHMKAFKAKG GDVSWHIHDE
     RSLLALQGPL AAPVLQHLTK EDLSKLYFGE FRVLDINGSQ CFLTRTGYTG EDGFEISVPS
     EHGVELAKAL LEKSEGKIRL TGLGARDSLR LEAGLCLYGN DLEQHITPIE AGLTWAIGKR
     RRAEGGFLGA DVILKQLADG PSIRRVGFIS SGPPPRSHSE IQDEGGNNIG EVTSGGFSPC
     LKKNIAIGYV KSGLHKAGTK VKIIIRGKQN EGVVTKMPFV PTKYYKPS
//