ID A1UIA7_MYCSK Unreviewed; 364 AA.
AC A1UIA7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Aminomethyltransferase;
DE EC=2.1.2.10;
DE AltName: Full=Glycine cleavage system T protein;
GN Name=gcvT; OrderedLocusNames=Mkms_3371;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Miller C.D., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; CP000518; ABL92565.1; -; Genomic_DNA.
DR RefSeq; YP_939355.1; NC_008705.1.
DR ProteinModelPortal; A1UIA7; -.
DR STRING; 189918.Mkms_3371; -.
DR EnsemblBacteria; ABL92565; ABL92565; Mkms_3371.
DR GeneID; 4611297; -.
DR KEGG; mkm:Mkms_3371; -.
DR PATRIC; 18105720; VBIMycSp70743_3890.
DR eggNOG; COG0404; -.
DR HOGENOM; HOG000239381; -.
DR KO; K00605; -.
DR OMA; KPAFWGR; -.
DR ProtClustDB; PRK00389; -.
DR BioCyc; MSP189918:GH4X-3428-MONOMER; -.
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 cleavage system; IEA:HAMAP.
DR Gene3D; 3.30.1360.120; -; 2.
DR HAMAP; MF_00259; GcvT; 1; -.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR006223; GcvT.
DR InterPro; IPR022903; NH2_Me_Trfase.
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 TIGRFAMs; TIGR00528; gcvT; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Methyltransferase; Transferase.
SQ SEQUENCE 364 AA; 38544 MW; 566FF014CCF8042C CRC64;
MSEPLHGPLE DRHRELGATF AEFGGWLMPV SYAGTVTEHT ATRTTVGLFD VSHLGKALVR
GPGAAAYVNS ALTNDLNRIG PGKAQYTLCC NDSGGVIDDL IAYYVSDDEI FLVPNAANTA
AVVAALAERA PDGVTVTDEH RSYAVLAVQG PKSAEVLGGL GLPTDMDYMG YVDAELNGTA
VRVCRTGYTG EQGYELLPAW DDAPAVFDAL VSAVRDAAGE LAGLGARDTL RTEMGYPLHG
HELSPEISPL QARCGWAVGW RKDAFWGRDA LLAEKEAGPK RLLRGLRAVG RGVLRPDLTV
FDGDTAVGVT TSGTFSPSLK VGIALALVDT AHDIADGSRV EVDVRGRRIE CEVVPPPFVT
AKTR
//
