ID   GCST_COLP3              Reviewed;         362 AA.
AC   Q486J8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Aminomethyltransferase;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
GN   Name=gcvT; OrderedLocusNames=CPS_1274;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000083; AAZ28390.1; -; Genomic_DNA.
DR   RefSeq; YP_268017.1; -.
DR   GeneID; 3522650; -.
DR   GenomeReviews; CP000083_GR; CPS_1274.
DR   KEGG; cps:CPS_1274; -.
DR   NMPDR; fig|167879.3.peg.1235; -.
DR   TIGR; CPS_1274; -.
DR   HOGENOM; Q486J8; -.
DR   OMA; Q486J8; VEIRGKW.
DR   BioCyc; CPSY167879:CPS_1274-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    362       Aminomethyltransferase.
FT                                /FTId=PRO_1000047659.
SQ   SEQUENCE   362 AA;  39590 MW;  D74FA34F38C42F5A CRC64;
     MTNKTVLHAK HLASGAKMVD FFGWDMPINY GSQIEEHHAV RTDAGMFDVS HMTIVDVQGA
     DAKAFLRRLV INDVAKLATP GKALYTGMLN EEGGVIDDLI IYFFSDTDYR LVVNSATRVK
     DLAWMTKQST GFDITITERP EFGMLAVQGP EAKAKVAKLL TAEQIEAVEG MKPFFGVQVG
     DLFIATTGYT GEDGYEIIVP NNSAEDFWQK LLDEGVVPCG LGARDTLRLE AGMNLYGLDM
     DETVSPLAAN MAWTISWEPT DRDFIGRDVL TAQKAAGDQP KLVGLVLEAK GVLRSHQVVV
     TEFGNGEITS GTFSPTLGHS VALARVPRSV KVGDTIEVEM RKKLIKVQVT KPSFVRNGKK
     VF
//