ID   GCST_BURP6              Reviewed;         372 AA.
AC   A3NEZ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=BURPS668_3926;
OS   Burkholderia pseudomallei (strain 668).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=668;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000570; ABN84729.1; -; Genomic_DNA.
DR   RefSeq; WP_004202927.1; NC_009074.1.
DR   AlphaFoldDB; A3NEZ8; -.
DR   SMR; A3NEZ8; -.
DR   EnsemblBacteria; ABN84729; ABN84729; BURPS668_3926.
DR   GeneID; 56594513; -.
DR   KEGG; bpd:BURPS668_3926; -.
DR   HOGENOM; CLU_007884_10_2_4; -.
DR   OMA; MPVQYPA; -.
DR   Proteomes; UP000002153; Chromosome I.
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..372
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000047651"
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