ID   GCST_BOVIN              Reviewed;         397 AA.
AC   P25285;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000305};
DE            EC=2.1.2.10 {ECO:0000250|UniProtKB:P28337, ECO:0000250|UniProtKB:P48728};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000303|PubMed:2002038};
DE            Short=GCVT;
DE   Flags: Precursor;
GN   Name=AMT {ECO:0000250|UniProtKB:P48728};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-55.
RC   TISSUE=Liver;
RX   PubMed=2002038; DOI=10.1016/s0021-9258(19)67736-7;
RA   Okamura-Ikeda K., Fujiwara K., Yamamoto M., Hiraga K., Motokawa Y.;
RT   "Isolation and sequence determination of cDNA encoding T-protein of the
RT   glycine cleavage system.";
RL   J. Biol. Chem. 266:4917-4921(1991).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000250|UniProtKB:P48728}.
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         Evidence={ECO:0000250|UniProtKB:P48728};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000250|UniProtKB:P48728}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P48728}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR   EMBL; M59799; AAA30786.1; -; mRNA.
DR   PIR; A23707; A23707.
DR   RefSeq; NP_803451.1; NM_177485.2.
DR   AlphaFoldDB; P25285; -.
DR   SMR; P25285; -.
DR   STRING; 9913.ENSBTAP00000002992; -.
DR   PaxDb; P25285; -.
DR   PRIDE; P25285; -.
DR   Ensembl; ENSBTAT00000002992; ENSBTAP00000002992; ENSBTAG00000002321.
DR   GeneID; 280719; -.
DR   KEGG; bta:280719; -.
DR   CTD; 275; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002321; -.
DR   eggNOG; KOG2770; Eukaryota.
DR   GeneTree; ENSGT00940000157524; -.
DR   HOGENOM; CLU_007884_10_0_1; -.
DR   InParanoid; P25285; -.
DR   OMA; MPVQYPA; -.
DR   OrthoDB; 673132at2759; -.
DR   TreeFam; TF313026; -.
DR   Reactome; R-BTA-6783984; Glycine degradation.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000002321; Expressed in retina and 107 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:AgBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:AgBase.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0004047; F:aminomethyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0031405; F:lipoic acid binding; IDA:AgBase.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006546; P:glycine catabolic process; TAS:AgBase.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Mitochondrion;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2002038"
FT   CHAIN           23..397
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010753"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
FT   BINDING         393
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
SQ   SEQUENCE   397 AA;  42869 MW;  3FE5D598B78AB6FD CRC64;
     MVSRLSSRLQ ALASAPCRSL SCAQDVLHRT PLYDFHLAHG GKMVAFAGWS LPVQYRDSHV
     NSHLHTRQHC SLFDVSHMLQ TKIFGCDRVK LMESLVVGDI AELKPNQGTL SLFTNEAGGI
     LDDLIVTSAS EGHLYVVSNA GCREKDLTLM QDKVRELQNK GSDVALEVMD NALLALQGPT
     AAQVLQAGVA DDLRKLPFMT SAVMEVFGVS GCRVTRCGYT GEDGVEISVP AAEAVHLAAA
     LLKNPEVKLA GLAARDSLRL EAGLCLYGND IDEHTTPVEG SLSWTLGKRR RAAMDFPGAS
     VIVPQLKSKA QRRRVGLMCD GAPVRAQSPI LSPEGTVIGA VTSGCPSPCL KKNVAMGYVP
     YEYSRPGTPL LVEVRRKQQP AVVSKMPFVS TNYYILK