ID   GCST_CHLTE              Reviewed;         365 AA.
AC   Q8KBJ9;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   02-SEP-2026, entry version 116.
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=CT1788;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
OC   Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM73009.1; -; Genomic_DNA.
DR   RefSeq; WP_010933448.1; NC_002932.3.
DR   AlphaFoldDB; Q8KBJ9; -.
DR   SMR; Q8KBJ9; -.
DR   STRING; 194439.CT1788; -.
DR   EnsemblBacteria; AAM73009; AAM73009; CT1788.
DR   KEGG; cte:CT1788; -.
DR   PATRIC; fig|194439.7.peg.1622; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_10; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000001007; 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; 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..365
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_0000122551"
SQ   SEQUENCE   365 AA;  40139 MW;  5B627C302FF7C86A CRC64;
     MKKTALSAWH EAAGAKMIDF GGFLMPVQYT GIIAEHKAVR EAAGLFDVSH MGNFYVRGAR
     ALEFLQYMTT NDLAKIVDGQ AQYTLMLYPD GGIVDDLIIY RVSADTFFLI VNASNCEKDF
     DWLSSHIGQF EGVALENHTS ELSLIALQGP KSFDILARVF PGAGIDKLGS FHFIKLPFEG
     AEIMVARTGY TGEAGVEICL PNERAVALWS ALMEAGKSDG IQPIGLGARD TLRLEMGYSL
     YGHEIERDVN PLEARLKWVV KLNKPNFIGK QACEQVEINP RKSVVGFSLE GRAIPRQHFK
     VYNSDKQEIG EVCSGTVSPT LQEPIGTASL LLDYAQPGTP IFVEIRGTMQ PGAVRRLPFV
     HADRP
//