ID   GCST_CHLTE              Reviewed;         365 AA.
AC   Q8KBJ9;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Aminomethyltransferase;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
GN   Name=gcvT; OrderedLocusNames=CT1788;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM73009.1; -; Genomic_DNA.
DR   RefSeq; NP_662667.1; -.
DR   GeneID; 1008275; -.
DR   GenomeReviews; AE006470_GR; CT1788.
DR   KEGG; cte:CT1788; -.
DR   NMPDR; fig|194439.1.peg.1761; -.
DR   TIGR; CT1788; -.
DR   HOGENOM; Q8KBJ9; -.
DR   OMA; Q8KBJ9; VEIRGKW.
DR   BioCyc; CTEP194439:CT_1788-MON; -.
DR   BRENDA; 2.1.2.10; 189605.
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_0000122551.
SQ   SEQUENCE   365 AA;  40139 MW;  5B627C302FF7C86A CRC64;
     MKKTALSAWH EAAGAKMIDF GGFLMPVQYT GIIAEHKAVR EAAGLFDVSH MGNFYVRGAR
     ALEFLQYMTT NDLAKIVDGQ AQYTLMLYPD GGIVDDLIIY RVSADTFFLI VNASNCEKDF
     DWLSSHIGQF EGVALENHTS ELSLIALQGP KSFDILARVF PGAGIDKLGS FHFIKLPFEG
     AEIMVARTGY TGEAGVEICL PNERAVALWS ALMEAGKSDG IQPIGLGARD TLRLEMGYSL
     YGHEIERDVN PLEARLKWVV KLNKPNFIGK QACEQVEINP RKSVVGFSLE GRAIPRQHFK
     VYNSDKQEIG EVCSGTVSPT LQEPIGTASL LLDYAQPGTP IFVEIRGTMQ PGAVRRLPFV
     HADRP
//