ID   GCST_GEOSW              Reviewed;         364 AA.
AC   C5D4A2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=GWCH70_2361;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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; CP001638; ACS25058.1; -; Genomic_DNA.
DR   RefSeq; WP_015864474.1; NC_012793.1.
DR   AlphaFoldDB; C5D4A2; -.
DR   SMR; C5D4A2; -.
DR   STRING; 471223.GWCH70_2361; -.
DR   EnsemblBacteria; ACS25058; ACS25058; GWCH70_2361.
DR   KEGG; gwc:GWCH70_2361; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_9; -.
DR   OMA; MPVQYPA; -.
DR   OrthoDB; 282830at2; -.
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..364
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000204637"
SQ   SEQUENCE   364 AA;  40551 MW;  485DE70BA4105D43 CRC64;
     MLKRTPLFAV YERYGAKTID FGGWELPVQF SSIKEEHEAV RTRAGLFDVS HMGEFVVKGD
     DSLAFLQKMM TNDVSKLTDG RVQYSLMCYE DGGTVDDLLI YKKADGHYLL VVNAANIEKD
     FEWLHGHLFG DVELVNISQE IAQLALQGPL AEQVLQKLTN TDLSAIKFFS FQDDININGV
     KALVSRTGYT GEDGFEIYCR REDAVALWES ILEAGKEEGV LPCGLGARDT LRFEATLPLY
     GQELSKDITP IEAGLGFAVK TNKDADFIGK DVLKKQKEEG TARKLVGIEM IDKGIPRHGY
     KVFANGEEIG FVTTGTQSPT LKKNIGLALI KTEFTEMDTE VEVEIRGKRL KAKVIATPFY
     KRAK