GCST_FLAAN
ID GCST_FLAAN Reviewed; 407 AA.
AC O49849;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 anomala (Yellowtops).
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=35877;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RA Nan Q., Chu C.-C., Bauwe H.;
RT "The GDCST gene encoding T-protein of the glycine cleavage system in the
RT C3-C4 intermediate plant Flaveria anomala.";
RL (er) Plant Gene Register PGR98-006(1998).
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; Z71184; CAA94902.1; -; Genomic_DNA.
DR AlphaFoldDB; O49849; -.
DR SMR; O49849; -.
DR PRIDE; O49849; -.
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 3: Inferred from homology;
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_0000010759"
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; 44279 MW; 7F1BE2896CDD1A59 CRC64;
MRGGLWQLGQ SITRRLGQSD KKTIVRRCYA SEADLKKTVL YDFHVAHGGK MVPFAGWSMP
IQYKDSIMDS TINCRENGSL FDVSHMCGLS LKGKDCVAFL EKLVVADVAG LAPGTGSLTV
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