ID   GCST_CHLPD              Reviewed;         365 AA.
AC   A1BI02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Cpha266_2017;
OS   Chlorobium phaeobacteroides (strain DSM 266).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 266;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL   Submitted (DEC-2006) 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; CP000492; ABL66029.1; -; Genomic_DNA.
DR   RefSeq; WP_011745833.1; NC_008639.1.
DR   AlphaFoldDB; A1BI02; -.
DR   SMR; A1BI02; -.
DR   STRING; 290317.Cpha266_2017; -.
DR   EnsemblBacteria; ABL66029; ABL66029; Cpha266_2017.
DR   KEGG; cph:Cpha266_2017; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_10; -.
DR   OMA; MPVQYPA; -.
DR   OrthoDB; 282830at2; -.
DR   Proteomes; UP000008701; Chromosome.
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; Reference proteome; Transferase.
FT   CHAIN           1..365
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000047655"
SQ   SEQUENCE   365 AA;  40686 MW;  510331E5B8A9AE4A CRC64;
     MKKTALYHWH EQAGARIIDF GGYLMPVQYS GIIAEHRAVR SAAGLFDVSH MGNFYVTGER
     SEAFLQYMVT NDLSKVRDGE AQYNLMLYPN GGVVDDLIIY RLDSKTFFLI VNASNTEKDY
     AWLQQHIGAF DGVCLEDHTD RLSLIALQGP VAIDIVKTVF PSVDFDALLQ FQFCRTLYGD
     APVMIARTGY TGEKGVEICL PNEAALPLWE ALYDAGRACG ISPVGLGARD TLRLEMGYSL
     YGHEIDQDIN PLEARLKWAV KMDKGSFIGR EACQQVELHL TRGVAGFSIE SRVLPRQHCK
     VYNTDRQEIG WVCSGTLSPT LQEPIGTCNI VRKYITSGDS VFVDVRGTLH KGEIRRLPFV
     KTSLG