GCST_CHICK
ID GCST_CHICK Reviewed; 392 AA.
AC P28337;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000305};
DE EC=2.1.2.10 {ECO:0000269|PubMed:1526969};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000303|PubMed:1526969};
DE Short=GCVT;
DE Flags: Precursor;
GN Name=AMT {ECO:0000250|UniProtKB:P48728};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TRANSIT PEPTIDE CLEAVAGE SITE, CATALYTIC
RP ACTIVITY, AND FUNCTION.
RX PubMed=1526969; DOI=10.1016/s0021-9258(19)36957-1;
RA Okamura-Ikeda K., Fujiwara K., Motokawa Y.;
RT "Molecular cloning of a cDNA encoding chicken T-protein of the glycine
RT cleavage system and expression of the functional protein in Escherichia
RT coli. Effect of mRNA secondary structure in the translational initiation
RT region on expression.";
RL J. Biol. Chem. 267:18284-18290(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 179-392.
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:0000269|PubMed:1526969}.
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:0000269|PubMed:1526969};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000305|PubMed:1526969}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:1526969}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D11162; BAA01937.1; -; mRNA.
DR PIR; A44167; A44167.
DR AlphaFoldDB; P28337; -.
DR SMR; P28337; -.
DR STRING; 9031.ENSGALP00000042238; -.
DR VEuPathDB; HostDB:geneid_395566; -.
DR eggNOG; KOG2770; Eukaryota.
DR InParanoid; P28337; -.
DR OrthoDB; 673132at2759; -.
DR PhylomeDB; P28337; -.
DR BioCyc; MetaCyc:MON-12927; -.
DR BRENDA; 1.4.1.27; 1306.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004047; F:aminomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IDA: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; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1526969"
FT CHAIN 17..392
FT /note="Aminomethyltransferase, mitochondrial"
FT /id="PRO_0000010757"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P48728"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P48728"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P48728"
SQ SEQUENCE 392 AA; 42058 MW; A022434038AF71E0 CRC64;
MLRAGCRAAL ARRHLSSAPE GLKQTPLDAL HRARGGRMVP FAGWSLPVQY GRGHLESHLH
TRRHCSLFDV SHMLQTRVYG RDRVRFLESL VVGDIAELRP GQGTLTLLTN ERGDIVDDLI
VTNTAEDHLY VVSNAGCADK DRAVMEGRAA ELRAAGGDVH LEVSGQRAAG VQGPSMAQVL
QAGLPDDLTK LTFMTSTATT VFGVPGCRVT RCGYTGEDGV EISVPAGRAV ELAERLLGCP
EVWPAGLAAR DSLRLEAGLC LYGNDIDEST TPVEAGLLWT LGKRRRTAMD FPGAAIIMEQ
VKEKPKRKRV GLTSVGPPLR PPAAILGPEG TPVGTVTSGC PSPSLGKNIA MGYVQAAHSR
PGTTLTVEVR KKQHPALVTK MPFVPTHYYM AK