ID   GCST_SYNY3              Reviewed;         372 AA.
AC   P54261;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 145.
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=sll0171;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA10058.1; -; Genomic_DNA.
DR   PIR; S76080; S76080.
DR   AlphaFoldDB; P54261; -.
DR   SMR; P54261; -.
DR   FunCoup; P54261; 436.
DR   STRING; 1148.gene:10499550; -.
DR   PaxDb; 1148-gene:10499550; -.
DR   EnsemblBacteria; BAA10058; BAA10058; BAA10058.
DR   KEGG; syn:sll0171; -.
DR   eggNOG; COG0404; Bacteria.
DR   InParanoid; P54261; -.
DR   OMA; AACEMMF; -.
DR   PhylomeDB; P54261; -.
DR   BioCyc; MetaCyc:MONOMER-22026; -.
DR   BRENDA; 1.4.1.27; 6192.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IBA:GO_Central.
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; NF001567; gcvT; 1.
DR   NCBIfam; TIGR00528; gcvT; 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_0000122609"
SQ   SEQUENCE   372 AA;  41036 MW;  751D3E1BA65DE2DA CRC64;
     MANLFPALRT PLYNLITEQT TKLTTFGGWE MPVQFAGLKQ EHQAVREKVG MFDISHMGKF
     VLTGQKVLAA LQSLVPSDLD RLTPGKAQYT VLLNAQGGII DDIIVYDQGK NPEGQERVTL
     IVNAATTVKD KQWLLEHLPE EIDFQDLSRE KVLIALQGPE ALTILQPLVD QNLGELPAFG
     HLEAEFLREK AFIARTGYTG EDGFEIMVSP EVGKQLWQTF GSKGVTPCGL GARDTLRLEA
     GMGLYGQDMN DETTPLEAGL GWLVHLDSKG DFIGRAVLTE QKANGVEKRL VGLEMLAKQI
     ARHDYPILHN GEIMGIVTSG TLSPTLQKAI ALGYVPTELA KVGQELEVEV RGKTYGIKVV
     KKLFYRSEQK PR
//