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Database: UniProt/TrEMBL
Entry: A1UIA7_MYCSK
LinkDB: A1UIA7_MYCSK
Original site: A1UIA7_MYCSK 
ID   A1UIA7_MYCSK            Unreviewed;       364 AA.
AC   A1UIA7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   29-OCT-2014, entry version 57.
DE   RecName: Full=Aminomethyltransferase {ECO:0000256|HAMAP-Rule:MF_00259, ECO:0000256|RuleBase:RU003981};
DE            EC=2.1.2.10 {ECO:0000256|HAMAP-Rule:MF_00259, ECO:0000256|RuleBase:RU003981};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000256|HAMAP-Rule:MF_00259};
GN   Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN   OrderedLocusNames=Mkms_3371 {ECO:0000313|EMBL:ABL92565.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92565.1, ECO:0000313|Proteomes:UP000000638};
RN   [1] {ECO:0000313|EMBL:ABL92565.1, ECO:0000313|Proteomes:UP000000638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL92565.1,
RC   ECO:0000313|Proteomes:UP000000638};
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. {ECO:0000256|HAMAP-Rule:MF_00259,
CC       ECO:0000256|RuleBase:RU003981, ECO:0000256|SAAS:SAAS00001700}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine
CC       + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-
CC       methylenetetrahydrofolate + NH(3). {ECO:0000256|HAMAP-
CC       Rule:MF_00259, ECO:0000256|RuleBase:RU003981,
CC       ECO:0000256|SAAS:SAAS00001695}.
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259,
CC       ECO:0000256|RuleBase:RU003981, ECO:0000256|SAAS:SAAS00001706}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|HAMAP-
CC       Rule:MF_00259, ECO:0000256|RuleBase:RU003980}.
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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; PFVEINT; -.
DR   OrthoDB; EOG6T1WS5; -.
DR   BioCyc; MSP189918:GH4X-3396-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 {ECO:0000256|HAMAP-Rule:MF_00259,
KW   ECO:0000256|RuleBase:RU003981};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000638};
KW   Methyltransferase {ECO:0000313|EMBL:ABL92565.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000638};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00259,
KW   ECO:0000256|RuleBase:RU003981}.
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
//
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