GCST_SYMTH
ID GCST_SYMTH Reviewed; 375 AA.
AC Q67N36;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000255|HAMAP-Rule:MF_00259}; OrderedLocusNames=STH1922;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
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:0000255|HAMAP-Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
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DR EMBL; AP006840; BAD40907.1; -; Genomic_DNA.
DR AlphaFoldDB; Q67N36; -.
DR SMR; Q67N36; -.
DR STRING; 292459.STH1922; -.
DR EnsemblBacteria; BAD40907; BAD40907; STH1922.
DR KEGG; sth:STH1922; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_9; -.
DR OMA; MPVQYPA; -.
DR Proteomes; UP000000417; Chromosome.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1360.120; -; 1.
DR HAMAP; MF_00259; GcvT; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR022903; GCS_T_bac.
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; Reference proteome; Transferase.
FT CHAIN 1..375
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122605"
SQ SEQUENCE 375 AA; 41243 MW; EC3FF63B4CDC73DD CRC64;
MNESLKRTPL YELHLKLGAR MVPFGGWEMP VQYSSVIEEH RAVREAAGLF DVSHMGEFEV
RGPQALDLIQ LVSTNDAAKL AVGRVQYALM CYENGTVVDD ILIYRLDEHR YWLVVNAGNT
QKDWEWINTA RERAGLHNLE LIDRSAEIAL LALQGPKAEE ILQPLATGVV LSQLEPFSLA
KNVTVSGVPT LVLSRTGYTG EDGFEIYVKA EDVAALWEAL LEAGDEQGLL PCGLGARDTL
RFEAKLPLYG HEISDQHNPL EAGLGFAVKL KKGVDFIGRD ALARIKEQGP TRKLVGIEMI
DRGVPRQGYP VAVGGEVVGE VTTGSFSPTL EKNIALAYVP VAHSAVGTEV EVIIRGRALK
ARVVETPFYR SPHRR
