ID   GCST_PROM0              Reviewed;         370 AA.
AC   A3PFH6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=P9301_18781;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000576; ABO18501.1; -; Genomic_DNA.
DR   RefSeq; WP_011863783.1; NC_009091.1.
DR   AlphaFoldDB; A3PFH6; -.
DR   SMR; A3PFH6; -.
DR   STRING; 167546.P9301_18781; -.
DR   EnsemblBacteria; ABO18501; ABO18501; P9301_18781.
DR   KEGG; pmg:P9301_18781; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_3; -.
DR   OMA; MPVQYPA; -.
DR   Proteomes; UP000001430; 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..370
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000047686"
SQ   SEQUENCE   370 AA;  41870 MW;  26BCA9FE4FA98986 CRC64;
     MDLRKSPLYS KYIESNAKLV DFAGWEMPIS FSGLIKEHES VRSSAGLFDI SHMGVISVKG
     INPKDYIQKF FPTNLYSFSE GQGLYTVMLN DKGGIIDDLI IYDLGIQEND ITELLLIVNA
     SRYEEDFQWI KNNLNKDEIS ITNFKKAKVL LALQGKKSFD LFEEWIDSSI SHIPNFGCEY
     KIFEHISPKE KIFFSKTGYT GENGLEILLS KKAAINLWDF SISKNVAPCG LGARDTLRLE
     AGMHLYGQDI NEETSPYEAG LGWLVHLENN HEFFGRRFLE EQSRLGIQKK LVGLFIEGKA
     IGRKGCTVLK GEENIGTITS GSWSPTKQQA IAFAYINTSH ALINNEVQVL IRGKKFKGVI
     TKRAFYKKNY