ID   GCST_FRATO              Reviewed;         358 AA.
AC   Q0BN73;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Aminomethyltransferase;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
GN   Name=gcvT; OrderedLocusNames=FTH_0475;
OS   Francisella tularensis subsp. holarctica (strain OSU18).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980500; DOI=10.1128/JB.00506-06;
RA   Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S.,
RA   Liu Y., Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A.,
RA   Fox G.E., Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D.,
RA   Weinstock G.M.;
RT   "Chromosome rearrangement and diversification of Francisella
RT   tularensis revealed by the type B (OSU18) genome sequence.";
RL   J. Bacteriol. 188:6977-6985(2006).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine (By similarity).
CC   -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine
CC       + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-
CC       methylenetetrahydrofolate + NH(3).
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H (By similarity).
CC   -!- SIMILARITY: Belongs to the gcvT family.
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DR   EMBL; CP000437; ABI82461.1; -; Genomic_DNA.
DR   RefSeq; YP_763098.1; -.
DR   GeneID; 4306531; -.
DR   GenomeReviews; CP000437_GR; FTH_0475.
DR   KEGG; fth:FTH_0475; -.
DR   HOGENOM; Q0BN73; -.
DR   OMA; Q0BN73; VEIRGKW.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP.
DR   HAMAP; MF_00259; -; 1.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR006223; GcvT.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Transferase.
FT   CHAIN         1    358       Aminomethyltransferase.
FT                                /FTId=PRO_1000047670.
SQ   SEQUENCE   358 AA;  39516 MW;  52C8DD19F908945E CRC64;
     MLKTPLYESH IAANAKMIDF SGWSMPINYG SQIQEHNNVR EDCGIFDVSH MLAVDIQGSE
     AEKFLRYLLA NDVAKLQENK AQYGCMLNHD AGIVDDLITY KVTDEHFRIV VNAGNRESDV
     AWFNQNAQNF DVAITPQTDL AIVAVQGPKA VAVIKRVVTK EIAAEIEALL PFSFKFFSKW
     MVARTGYTGE DGFEVILPAT QVKKFWDSLL ENGAQPAGLG ARDTLRLEAG MHLYGADMDT
     STTPLERGLG WSVDLSDEHR DFIGKKAYLA KKAQGVDTKW VGVVLKTKGV LRAGQEIDFD
     NGEKGYITSG SFSPTLKVAI GLAYVPKQAD NPVVNIRGKE LEVELVKPKF VKNGKSLI
//