ID   GCST_SHEPC              Reviewed;         364 AA.
AC   A4YAE0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Sputcn32_3211;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
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., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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; CP000681; ABP76923.1; -; Genomic_DNA.
DR   RefSeq; WP_011788111.1; NC_009438.1.
DR   AlphaFoldDB; A4YAE0; -.
DR   SMR; A4YAE0; -.
DR   STRING; 319224.Sputcn32_3211; -.
DR   GeneID; 45043703; -.
DR   KEGG; spc:Sputcn32_3211; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_6; -.
DR   OMA; MPVQYPA; -.
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..364
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000047703"
SQ   SEQUENCE   364 AA;  39796 MW;  D465ED97E2BE4B6F CRC64;
     MANKTILFNK HLESNAKMVD FHGWDMPLNY GSQIEEHHAV RQDAGMFDVS HMTVVDVIGT
     DACAFLRKLL ANDVARLKVP GKALYSGMLD ENAGIIDDLI TYYLTDTFYR VVVNSATREK
     DLAWIAKQSQ GFDITVTERP ELAMIAVQGP NAKAKAAAVF SADQNAAIEG MKPFFGKQAG
     SLFIATTGYT GEAGYEIIVP EDEAQALWQA LLDQGVKPCG LGARDTLRLE AGMNLYGLDM
     DETINPLAAN MGWTIAWEPT DRDFIGRKAL EALRDAGTDK LVGLVMEEKG VLRHDMPVFF
     TDAAGVEHQG VITSGTFSPT LGYSIAMARV PNQIGDTAEV EMRKKRVAVR VVAPNFVRNG
     KQAF