GCST_SOLTU
ID GCST_SOLTU Reviewed; 406 AA.
AC P54260;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, 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;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=8165246; DOI=10.1104/pp.104.3.1079;
RA Kopriva S., Bauwe H.;
RT "T-protein of glycine decarboxylase from Solanum tuberosum.";
RL Plant Physiol. 104:1079-1080(1994).
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; Z25862; CAA81081.1; -; mRNA.
DR PIR; S59948; S59948.
DR RefSeq; NP_001275291.1; NM_001288362.1.
DR AlphaFoldDB; P54260; -.
DR SMR; P54260; -.
DR IntAct; P54260; 1.
DR STRING; 4113.PGSC0003DMT400042406; -.
DR PRIDE; P54260; -.
DR ProMEX; P54260; -.
DR GeneID; 102602939; -.
DR KEGG; sot:102602939; -.
DR eggNOG; KOG2770; Eukaryota.
DR InParanoid; P54260; -.
DR OrthoDB; 673132at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P54260; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004047; F:aminomethyltransferase activity; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Aminotransferase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..406
FT /note="Aminomethyltransferase, mitochondrial"
FT /id="PRO_0000010764"
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 406 AA; 44277 MW; F52F4A13D70E33AD CRC64;
MRGGLWQLGQ SITRRLAQAD KKTIGRRCFA SDADLKKTVL YDFHVVNGGK MVPFAGWSMP
IQYKDSIMDS TVNCRENGSL FDVSHMCGLS LKGKDTIPFL EKLVIADVAG LAPGTGSLTV
FTNEKGGAID DSVVTKVTND HIYLVVNAGC RDKDLAHIEE HMKSFKSKGG DVSWHIHDER
SLLALQGPLA APVLQYLTKD DLSKMYFGEF RVLDINGAPC FLTRTGYTGE DGFEISVPSE
NALDLAKALL EKSEGKIRLT GLGARDSLRL EAGLCLYGND MEQHTTPVEA GLTWAIGKRR
RAEGGFLGAE VILKQIEEGP KIRRVGFFSS GPPPRSHSEI QDSNGQNIGE ITSGGFSPCL
KKNIAMGYVK TGNHKAGTNV KIVIRGKSYD GVVTKMPFVP TKYYKP