ID GCST_BURM9 Reviewed; 372 AA.
AC A2S6F4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 02-NOV-2016, entry version 62.
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};
GN OrderedLocusNames=BMA10229_A1542;
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229;
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine
CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-
CC methylenetetrahydrofolate + NH(3). {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC P, T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
DR EMBL; CP000546; ABN02404.1; -; Genomic_DNA.
DR RefSeq; WP_004202927.1; NC_008836.1.
DR ProteinModelPortal; A2S6F4; -.
DR EnsemblBacteria; ABN02404; ABN02404; BMA10229_A1542.
DR KEGG; bml:BMA10229_A1542; -.
DR PATRIC; 19134040; VBIBurMal46188_3737.
DR HOGENOM; HOG000239381; -.
DR KO; K00605; -.
DR OMA; HSPILNM; -.
DR Proteomes; UP000002283; Chromosome I.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-HAMAP.
DR Gene3D; 2.40.30.110; -; 1.
DR Gene3D; 3.30.1360.120; -; 2.
DR HAMAP; MF_00259; GcvT; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR022903; GCS_T_bac.
DR InterPro; IPR028896; GCST/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; PTHR13847:SF5; PTHR13847:SF5; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PIRSF; PIRSF006487; GcvT; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Transferase.
FT CHAIN 1 372 Aminomethyltransferase.
FT /FTId=PRO_1000047649.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 3 366 ihamap:GcvT [T]
FT MYHIT 270 361 ipfam:GCV_T_C [T]
FT MYHIT 9 262 ipfam:GCV_T [T]
SQ SEQUENCE 372 AA; 40093 MW; 0EE9681AF1660350 CRC64;
MTVLKTTPLH AAHRALNARM VDFGGWDMPV NYGSQIEEHQ AVRTDAGMFD VSHMCVVDFT
GPRVRAFFEH AIANNVAKLQ TPGKALYSCL LNPQGGVIDD LIVYYFTEEF FRVVVNAGTA
EKDIAWFNQL NEQGGFGLTI APRRDFAIVA AQGPNARAKV WDTVPCARAA TSELKPFNAA
QVAGTPFGDL TVARTGYTGE DGFEIIVPAT HVEALWNALA ERGVRPCGLG ARDTLRLEAG
MNLYGQDMDE SVSPLDAGLA WTVDLSAPRA FVGRDALEAH GSRAAFVGLI LQKENGRAGG
VLRAHQKVAT PHGEGEITSG TFSPSMQESI AFARVPKDVA IGDTVHVQIR DKQLPARVVK
LPFVRNGKVL AA
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