GCST_MYCLE
ID GCST_MYCLE Reviewed; 367 AA.
AC O32955;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
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}; OrderedLocusNames=ML0865;
GN ORFNames=MLCB22.13c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC 5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
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DR EMBL; Z98741; CAB11378.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31246.1; -; Genomic_DNA.
DR PIR; T44888; T44888.
DR RefSeq; NP_301653.1; NC_002677.1.
DR RefSeq; WP_010907977.1; NC_002677.1.
DR AlphaFoldDB; O32955; -.
DR SMR; O32955; -.
DR STRING; 272631.ML0865; -.
DR EnsemblBacteria; CAC31246; CAC31246; CAC31246.
DR KEGG; mle:ML0865; -.
DR PATRIC; fig|272631.5.peg.1592; -.
DR Leproma; ML0865; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_11; -.
DR OMA; YPLHGQD; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1360.120; -; 1.
DR HAMAP; MF_00259; GcvT; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR022903; GCS_T_bac.
DR InterPro; IPR028896; GCST/YgfZ/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; PTHR43757; PTHR43757; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122572"
SQ SEQUENCE 367 AA; 38879 MW; B0B40CEFF6A6A094 CRC64;
MTDAPELLKG PLEDRHRELG ANFAEFGGWL MPVSYAGTVS EHSATRNAVG LFDVSHLGKA
LVRGPGAAQF VNSVLTNDLG RIRPGKAQYT LCCSESGGVI DDLIAYYVDD DEIFLVSNAA
NTAAVVDALQ AVVPAGLTII NQHRSHAVLA VQGPRSTDVL GELGLPTGID YMGYVDASYA
GVPVRVCRTG YTGEQGYELL PPWESADVVF DALVAAVVDA RGEPAGLGAR DTLRTEMGYP
LYGHELSLDI SPLQARCGWA IGWKKDAFLG RDALLAEKAA GPRRLLRGLR MAGRGVLRPG
LTVCAGDIPI GVTTSGTFSP TLQVGVALAL IDSEAAVQDG QQIIVDVRGR AVECEVVRPP
FIEVKTR