ID   GCST_CHLCH              Reviewed;         366 AA.
AC   Q3AQ17;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=Cag_1656;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) 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; CP000108; ABB28908.1; -; Genomic_DNA.
DR   RefSeq; WP_011362670.1; NC_007514.1.
DR   AlphaFoldDB; Q3AQ17; -.
DR   SMR; Q3AQ17; -.
DR   STRING; 340177.Cag_1656; -.
DR   EnsemblBacteria; ABB28908; ABB28908; Cag_1656.
DR   KEGG; cch:Cag_1656; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_10; -.
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..366
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000047654"
SQ   SEQUENCE   366 AA;  39885 MW;  5E387192ED20C79B CRC64;
     MKKTALYPCH EQSGAKIIDF GGYLMPVQYA GIIAEHKAVR SAAGLFDVSH MGNFFVKGSR
     ALEFLQFVTT NDLAKVVDGQ AQYNLMLYPS GGIVDDLIIY RMSADTFFLI VNASNADKDF
     AWLQQHIDQF EGVTLEDHTE RLSLIALQGP LALSILNRLF PSIDGEALGS FHFCSASFNG
     FDVIIARTGY TGEKGVEMCV PNEAAIALWE ALMAAGAADG IQPIGLGARD TLRLEMGYSL
     YGHEINQDTN PLEARLKWVV KMDKGHFIGK EACEQAMQHP QRTVIGFSLE GRALPRQGFT
     LYNSDRQAIG VVCSGTLSPT LQEPVGTCSV LREYGKPGTP ILVEVRGAFH AGIIRSLPFV
     TNTSLA