ID   GCST_BACFR              Reviewed;         361 AA.
AC   Q64WS3;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=BF1303;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; AP006841; BAD48053.1; -; Genomic_DNA.
DR   RefSeq; WP_005795559.1; NC_006347.1.
DR   RefSeq; YP_098587.1; NC_006347.1.
DR   AlphaFoldDB; Q64WS3; -.
DR   SMR; Q64WS3; -.
DR   STRING; 295405.BF1303; -.
DR   EnsemblBacteria; BAD48053; BAD48053; BF1303.
DR   KEGG; bfr:BF1303; -.
DR   PATRIC; fig|295405.11.peg.1286; -.
DR   HOGENOM; CLU_007884_10_2_10; -.
DR   OMA; MPVQYPA; -.
DR   Proteomes; UP000002197; 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; Transferase.
FT   CHAIN           1..361
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_0000122539"
SQ   SEQUENCE   361 AA;  39870 MW;  E5E9D8FE6A152D8C CRC64;
     MKTTPFTEKH IALGAKMHEF AGYNMPIEYS GIIDEHLTVC NGVGVFDVSH MGEFWVKGPH
     ALDFLQKVTS NNVAALVPGK IQYTCFPNED GGIVDDLLVY QYEPEKYLLV VNASNIEKDW
     NWCISHNTEG AELENSSDNM AQLAVQGPKA IQALQKLTDI NLADIPYYTF KVGEFAGEKN
     VIISNTGYTG AGGFELYFYP DAAMKIWDAV FEAGAEFGIK PIGLGARDTL RLEMGFCLYG
     NDLDDTTSPI EAGLGWITKF VDGKNFTNRS MLEKQKAEGT VRKLVGFEMI DRGIPRHGYE
     LTTAEGDKIG VVTSGTMSPI RKIGIGMGYV KPEYSKIGTE ICIDMRGRKL KAVVVKPPFR
     K