ID   GCST_BURPS              Reviewed;         372 AA.
AC   Q63PL4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 107.
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=BPSL3360;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[protein] +
CC         (6S)-5,6,7,8-tetrahydrofolate = N(6)-[(R)-dihydrolipoyl]-L-lysyl-
CC         [protein] + (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NH4(+);
CC         Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10492,
CC         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; BX571965; CAH37373.1; -; Genomic_DNA.
DR   RefSeq; WP_004202927.1; NC_006350.1.
DR   AlphaFoldDB; Q63PL4; -.
DR   SMR; Q63PL4; -.
DR   STRING; 272560.BPSL3360; -.
DR   GeneID; 93061983; -.
DR   KEGG; bps:BPSL3360; -.
DR   PATRIC; fig|272560.51.peg.1840; -.
DR   eggNOG; COG0404; Bacteria.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   FunFam; 3.30.70.1400:FF:000001; Aminomethyltransferase; 1.
DR   FunFam; 4.10.1250.10:FF:000001; Aminomethyltransferase; 1.
DR   Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 4.10.1250.10; Aminomethyltransferase fragment; 1.
DR   Gene3D; 3.30.1360.120; Probable tRNA modification gtpase trme, domain 1; 1.
DR   HAMAP; MF_00259; GcvT; 1.
DR   InterPro; IPR006223; GcvT.
DR   InterPro; IPR028896; GcvT/YgfZ/DmdA.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR022903; GcvT_bac.
DR   InterPro; IPR013977; GcvT_C.
DR   InterPro; IPR006222; GCVT_N.
DR   InterPro; IPR027266; TrmE/GcvT-like.
DR   NCBIfam; TIGR00528; gcvT; 1.
DR   NCBIfam; NF001567; PRK00389.1; 1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Reference proteome; Transferase.
FT   CHAIN           1..372
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_0000122550"
SQ   SEQUENCE   372 AA;  40093 MW;  0EE9681AF1660350 CRC64;
     MTVLKTTPLH AAHRALNARM VDFGGWDMPV NYGSQIEEHQ AVRTDAGMFD VSHMCVVDFT
     GPRVRAFFEH AIANNVAKLQ TPGKALYSCL LNPQGGVIDD LIVYYFTEEF FRVVVNAGTA
     EKDIAWFNQL NEQGGFGLTI APRRDFAIVA AQGPNARAKV WDTVPCARAA TSELKPFNAA
     QVAGTPFGDL TVARTGYTGE DGFEIIVPAT HVEALWNALA ERGVRPCGLG ARDTLRLEAG
     MNLYGQDMDE SVSPLDAGLA WTVDLSAPRA FVGRDALEAH GSRAAFVGLI LQKENGRAGG
     VLRAHQKVAT PHGEGEITSG TFSPSMQESI AFARVPKDVA IGDTVHVQIR DKQLPARVVK
     LPFVRNGKVL AA
//