ID   GCST_FRAAA              Reviewed;         365 AA.
AC   Q0RFF6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Aminomethyltransferase;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
GN   Name=gcvT; OrderedLocusNames=FRAAL5148;
OS   Frankia alni (strain ACN14a).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CT573213; CAJ63788.1; -; Genomic_DNA.
DR   RefSeq; YP_715325.1; -.
DR   GeneID; 4233028; -.
DR   GenomeReviews; CT573213_GR; FRAAL5148.
DR   KEGG; fal:FRAAL5148; -.
DR   OMA; Q0RFF6; ARCGWAI.
DR   BioCyc; FALN326424:FRAAL5148-MON; -.
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    365       Aminomethyltransferase.
FT                                /FTId=PRO_1000047665.
SQ   SEQUENCE   365 AA;  38064 MW;  DD60D9675E66BA1F CRC64;
     MADLRRSPLY GRHVDLGAKM AGFGGWEMPI EYAGRGVLAE HQAVRGAVGI FDVSHLGKAE
     VTGAGAAEFV NACLSNDLGR IAPGQAQYTL CCNDEGGVVD DLIAYLFSGE RVLLVPNAAN
     NAEVVARLAA AAPAGVSVTD RHTGFGVLAV QGPAAPTLVA ALGLPTDGAY MSFVEAAWKG
     RPVIVCRSGY TGERGYELLP RWDDTPALWD ALFAAGEGLG ASPVGLGARD TLRTEMGYPL
     HGQDLSPTIT PVQARSGWAV GWGKERFWGR EALLAERAAG PARLLWGLAS TGRAIPRPHM
     PVTAADGAPV GEVTSGTFSP TLRQGIGLAL LDRGVAEGDT VNVDVRGRPG PMTVVRPPFV
     PSTPR
//