ID   GCST_THEM4              Reviewed;         363 AA.
AC   A6LP67;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   02-SEP-2026, entry version 111.
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=Tmel_1885;
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
OC   Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=391009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-2007) 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=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; CP000716; ABR31718.1; -; Genomic_DNA.
DR   RefSeq; WP_012058076.1; NC_009616.1.
DR   AlphaFoldDB; A6LP67; -.
DR   SMR; A6LP67; -.
DR   STRING; 391009.Tmel_1885; -.
DR   KEGG; tme:Tmel_1885; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_0; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000001110; Chromosome.
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; 2.40.30.110:FF:000003; Aminomethyltransferase; 1.
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..363
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000047724"
SQ   SEQUENCE   363 AA;  40855 MW;  93B118746EFFAD7A CRC64;
     MKYTPLYEEH VKLGAKMVDF AGFNMPIQYT SIKDEVLAVR KNVGMFDVSH MGEVIVEGKD
     STKFVDFLIT NDFKNLKPGE IVYTAMCNEN GGFVDDLLAY KISEEKAMLV INASNIEKDF
     SWMKKISESF DVTLENKSDE YVLIAVQGPN AQKTLQKITN VDLEQIGYYT FTEGNVLDIK
     AIISRTGYTG EDGFEIYTTD KDGIIKIWKK LLNLNVIPAG LGARDCLRLE ASLLLYGNDM
     DETITPLEVG IKWAVKFEKD FMGKEALKRQ LEEGTSRRLK GFKIIDKGIA RHGYKVFKDG
     KEIGYVTSGT FSPTLNQAIG MALIEKGYKS GEIIEIEIRN KLVKAEIVKM PFYRGSVKSK
     KKG
//