ID   GCST_CANLF              Reviewed;         403 AA.
AC   Q9TSZ7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, 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:0000250|UniProtKB:P48728};
DE            Short=GCVT;
DE   Flags: Precursor;
GN   Name=AMT {ECO:0000303|PubMed:10894947};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10894947; DOI=10.1159/000015573;
RA   Leeb T., Breen M., Brenig B.;
RT   "Genomic structures and sequences of two closely linked genes (AMT,TCTA) on
RT   dog chromosome 20q15.1-q15.2.";
RL   Cytogenet. Cell Genet. 89:98-100(2000).
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; AJ012166; CAB62567.1; -; Genomic_DNA.
DR   RefSeq; NP_001029165.1; NM_001033993.1.
DR   RefSeq; XP_005632381.1; XM_005632324.2.
DR   AlphaFoldDB; Q9TSZ7; -.
DR   SMR; Q9TSZ7; -.
DR   STRING; 9612.ENSCAFP00000030953; -.
DR   PaxDb; Q9TSZ7; -.
DR   Ensembl; ENSCAFT00030026179; ENSCAFP00030022862; ENSCAFG00030013895.
DR   Ensembl; ENSCAFT00040035671; ENSCAFP00040031062; ENSCAFG00040018932.
DR   Ensembl; ENSCAFT00845046773; ENSCAFP00845036693; ENSCAFG00845026162.
DR   GeneID; 484770; -.
DR   KEGG; cfa:484770; -.
DR   CTD; 275; -.
DR   VEuPathDB; HostDB:ENSCAFG00845026162; -.
DR   eggNOG; KOG2770; Eukaryota.
DR   GeneTree; ENSGT00940000157524; -.
DR   HOGENOM; CLU_007884_10_0_1; -.
DR   InParanoid; Q9TSZ7; -.
DR   OMA; MPVQYPA; -.
DR   OrthoDB; 673132at2759; -.
DR   TreeFam; TF313026; -.
DR   Reactome; R-CFA-6783984; Glycine degradation.
DR   SABIO-RK; Q9TSZ7; -.
DR   Proteomes; UP000002254; Chromosome 20.
DR   Bgee; ENSCAFG00000011489; Expressed in liver and 48 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004047; F:aminomethyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Aminotransferase; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P25285"
FT   CHAIN           29..403
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010754"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
FT   BINDING         399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P48728"
SQ   SEQUENCE   403 AA;  43652 MW;  F12B8B9AE79FB8B8 CRC64;
     MQRAMTVVPH LGLRLQALPL ALGRPLSRAQ DVLRRTPLYD FHLAHGGKMV AFAGWSLPVQ
     YRDSHVDSHL HTRRHCSLFD VSHMLQTKIL GCDRVKLMES LVVGDIAELR PNQGTLSLFT
     NEAGGIEDDL IVTSTSEGYL YVVSNAGCWD KDLALMQGKV RELQNMGSDV SLEVVDNALL
     ALQGPTATQV LQAGVADDLR KLPFMTSAVM EVFGVSGCRV TRCGYTGEDG VEISVPAAAA
     VRLAAALLEN PEVKLAGLAA RDSLRLEAGL CLYGSDIDEH TTPVEGSLSW TLGKRRRAAM
     DFPGASVIIA QLKGKVQRRR VGLTCEGAPV RAHSPILNME GTVIGTVTSG CPSPCLKKNV
     AMGYVPSEYS RPGTPLLVEV RRKQQMAVVS KMPFVTTNYY TLK