ID   GCST_BACC7              Reviewed;         366 AA.
AC   B7HNZ1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 74.
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};
GN   OrderedLocusNames=BCAH187_A4358;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001177; ACJ79177.1; -; Genomic_DNA.
DR   RefSeq; WP_000631772.1; NC_011658.1.
DR   AlphaFoldDB; B7HNZ1; -.
DR   SMR; B7HNZ1; -.
DR   EnsemblBacteria; ACJ79177; ACJ79177; BCAH187_A4358.
DR   GeneID; 59155197; -.
DR   KEGG; bcr:BCAH187_A4358; -.
DR   HOGENOM; CLU_007884_10_2_9; -.
DR   OMA; MPVQYPA; -.
DR   OrthoDB; 282830at2; -.
DR   Proteomes; UP000002214; 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..366
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000119196"
SQ   SEQUENCE   366 AA;  40233 MW;  4F3F63E43AB94F09 CRC64;
     MITLQRTPLF DVYAKYGGKT IDFGGWELPV QFSSIKEEHE AVRTAAGLFD VSHMGEVEVK
     GVDSLAFLQR VVTNDVSTLK VGGAQYTAMC YENGGTVDDL LIYKRGEEDY LLVINASNIE
     KDYEWLASHV IGDATVVNVS SEVAQLAIQG PKAEGILQKV VSEDLKEIKF FKFKNDILVD
     GIPALVSRTG YTGEDGFEIY CKSEDAAKLW EKLLEVGAEE GLKPCGLGAR DTLRFEATLP
     LYGQELSKDI TPVEAGIGFA VKPNKEADFF GKATLKEQKE NGAPRKLVGI EVIERGIPRT
     HYPVFIGEEK IGEVTSGTQS PTLKKSIGLA LIDVKYAAVD TEVEIEIRNK RVKAVVVPTP
     FYKRSK