GCST_LYSSC
ID GCST_LYSSC Reviewed; 367 AA.
AC B1HSN7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=Bsph_3609;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA41095.1; -; Genomic_DNA.
DR RefSeq; WP_012295154.1; NC_010382.1.
DR AlphaFoldDB; B1HSN7; -.
DR SMR; B1HSN7; -.
DR EnsemblBacteria; ACA41095; ACA41095; Bsph_3609.
DR KEGG; lsp:Bsph_3609; -.
DR HOGENOM; CLU_007884_10_2_9; -.
DR OMA; MPVQYPA; -.
DR Proteomes; UP000002164; 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; Transferase.
FT CHAIN 1..367
FT /note="Aminomethyltransferase"
FT /id="PRO_1000125642"
SQ SEQUENCE 367 AA; 40507 MW; 550B3946192B82EC CRC64;
MTNELKRTPL FEEYAKYGAK TVDFGGWELP VQFSSIKDEH DAVRNRAGLF DVSHMGEILV
TGPDALNFLQ NLLSNDVSKI ATGQAQYTAM CYENGGVVDD LLTYKLADDH YLLCVNAANI
EKDYDWMLEN QHQYDVTIDN QSDAYAQIAL QGPLAEEVLQ SLTSTDVSAI KFFRFQENVE
VTGHKVLVSR SGYTGEDGFE LYGAPEDIKA LWGKILDAGQ DKGVVPAGLG CRDTLRFEAG
LPLYGQELSA TISPLEAGIG FAVKLNKEDF IGHDALVAQK ENGLPRKLVG IEMIDKGIPR
HGYKVFKDGK EIGEVTTGTQ LPSSKRNVGH ALIDSQFATI GNEMEIEIRG KQLKVVTVET
PFYKRSK