ID   GCST_KORVE              Reviewed;         380 AA.
AC   Q1INT8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, 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=Acid345_2461;
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Terriglobales;
OC   Candidatus Korobacteraceae; Candidatus Korobacter.
OX   NCBI_TaxID=204669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF41462.1; -; Genomic_DNA.
DR   RefSeq; WP_011523263.1; NC_008009.1.
DR   AlphaFoldDB; Q1INT8; -.
DR   SMR; Q1INT8; -.
DR   STRING; 204669.Acid345_2461; -.
DR   EnsemblBacteria; ABF41462; ABF41462; Acid345_2461.
DR   KEGG; aba:Acid345_2461; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_0; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000002432; 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   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..380
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000125627"
SQ   SEQUENCE   380 AA;  42105 MW;  87513DF46CE93217 CRC64;
     MNPPVEANIR KTALNATHRQ SGAKMVDYSG WDMPVEYPSV GGLMKEHLAV RAGVGLFDVS
     HMGDIRVHGP EALKAVQYLT MNDASKLNTG QAQYSAMLYP NGTFVDDVIV HKFADDDYLL
     VINAGTREKD VNWVKDNTRQ FKVTVEDLSD QFTQIAIQGP KGVDTLQKLT DVDLSKVKFY
     WFTRGTVAGL KNVLIARTGY TAEDGFEIYI PSDAATSDRV WNELLQAGKE FGVVPAGLGS
     RNTLRLEGKL PLYGHEISDE INVWEAGLDR FLKMDKGDFI GRAALEKAKN DGVKRALVGL
     ETIERGIPRD GYKVLDLEGK EIGYVTSGSY MPFLKRNLAL AYVPVEQSAL DNIVAVEIRN
     QPVKAKVVPS QFYKRPKKSS
//