ID A0A109MYT4_9BACI Unreviewed; 368 AA.
AC A0A109MYT4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN ORFNames=AS888_18600 {ECO:0000313|EMBL:KWW20379.1};
OS Peribacillus simplex.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1478 {ECO:0000313|EMBL:KWW20379.1, ECO:0000313|Proteomes:UP000064189};
RN [1] {ECO:0000313|EMBL:KWW20379.1, ECO:0000313|Proteomes:UP000064189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VanAntwerpen02 {ECO:0000313|EMBL:KWW20379.1,
RC ECO:0000313|Proteomes:UP000064189};
RA Couger M.B.;
RT "Genome Sequence of Bacillus simplex strain VanAntwerpen2.";
RL Submitted (NOV-2015) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-
CC aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00043710, ECO:0000256|HAMAP-
CC Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|HAMAP-Rule:MF_00259}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KWW20379.1}.
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DR EMBL; LNNH01000017; KWW20379.1; -; Genomic_DNA.
DR RefSeq; WP_061142006.1; NZ_LNNH01000017.1.
DR AlphaFoldDB; A0A109MYT4; -.
DR Proteomes; UP000064189; Unassembled WGS sequence.
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; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 4.10.1250.10; Aminomethyltransferase fragment; 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 NCBIfam; TIGR00528; gcvT; 1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PIRSF; PIRSF006487; GcvT; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00259};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 11..261
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 286..364
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 368 AA; 40434 MW; 660CDE6A4F279260 CRC64;
MTNLKRTPLF EVYQESGGKT IDFGGWELPV QFSGIKDEHE AVRAKAGLFD VSHMGEVDVK
GPGSLPFLQK MLTNDVSKLQ QGGALYTAMC YENGGTIDDL IVYKMAEDDY LLVVNAANTE
KDFNWLQANC PEDVQLTNVS SDYTQLALQG PAAEKILQKL SGDTDLSEIG FFKFKENVMI
NGIATIVSRT GYTGEDGFEI YSRSENGPSL WKAILEAGKE EGIQPIGLGA RDTLRFEAKL
PLYGQELSAD ITPIEAGIGF AVKVDKEADF FGKAVLAEQK EKGAPRKLVG IEMIDRGIPR
HGYKVYSGDQ IIGEVTTGTQ SPTLKKNVGL VLIDKEFSAL DATVEVEIRS KRLKATIIQT
PFYKKPRK
//
