GCST_THET8
ID GCST_THET8 Reviewed; 349 AA.
AC Q5SKX0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=TTHA0523;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; AP008226; BAD70346.1; -; Genomic_DNA.
DR RefSeq; WP_011228001.1; NC_006461.1.
DR RefSeq; YP_143789.1; NC_006461.1.
DR AlphaFoldDB; Q5SKX0; -.
DR SMR; Q5SKX0; -.
DR STRING; 300852.55771905; -.
DR EnsemblBacteria; BAD70346; BAD70346; BAD70346.
DR GeneID; 3169106; -.
DR KEGG; ttj:TTHA0523; -.
DR PATRIC; fig|300852.9.peg.521; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_0; -.
DR OMA; MPVQYPA; -.
DR PhylomeDB; Q5SKX0; -.
DR Proteomes; UP000000532; 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..349
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122612"
SQ SEQUENCE 349 AA; 37938 MW; B949E27D90AD76FD CRC64;
MKKTPLYEAH LRLGARMVDF AGYLLPLQYT SIVEEHLAVR RAVGVFDVSH MGEFLVRGKE
ALAFLQWATA NDAGKLKVGR AQYSMLPNER GGVVDDIYLY RLGEEEYLMV VNAANIAKDL
AHLQALAKGF RVELEDASER TALLALQGPK AASLLQGLTD LDLSQKRKND VFPARVAGRP
ARLARTGYTG EDGFELFLAP EDAEPVFLAL VEAGAKPAGL GARDSLRLEA GFPLYGHELT
EETNPLCTPW AWVVKKEKAF LGKEAMLAQA CRERLVGLVL EGGIPREGYR VLSGGRPVGR
VTSGGYSPLL QRGIALAYVE EGAEGPFQVE VRGRAVPAAL SPLPFVPLK
