ID A0A1H6FLR4_9SPHN Unreviewed; 374 AA.
AC A0A1H6FLR4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395};
GN ORFNames=SAMN05428974_0320 {ECO:0000313|EMBL:SEH11819.1};
OS Sphingopyxis sp. YR583.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1881047 {ECO:0000313|EMBL:SEH11819.1, ECO:0000313|Proteomes:UP000198829};
RN [1] {ECO:0000313|EMBL:SEH11819.1, ECO:0000313|Proteomes:UP000198829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR583 {ECO:0000313|EMBL:SEH11819.1,
RC ECO:0000313|Proteomes:UP000198829};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FNWK01000001; SEH11819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6FLR4; -.
DR STRING; 1881047.SAMN05428974_0320; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000198829; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 InterPro; IPR006223; GCS_T.
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};
KW Methyltransferase {ECO:0000313|EMBL:SEH11819.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEH11819.1}.
FT DOMAIN 16..260
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 287..364
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 374 AA; 40300 MW; 323A283735D51F86 CRC64;
MREDDEVPIE TATLPLDAWH RAKGGRMVEF AGYWMPIQYE GIMAEHLWTR ENAGLFDVSH
MGQLSLSGEK VAEALEALVP GDISALKPGR MRYSLLLDED GGILDDLMIT NEGDQYGIVV
NGAVKWEDIG HLRENLPDDI TLNHNEDYGL LALQGPKAVD ALARLVPEAA SLVFMQAVRA
TWNGHAISLS RSGYTGEDGF EISLPNEALT AFADALCAME EVKPIGLGAR DSLRLEAGLP
LYGHDLTPAI DPAEADLGFA VSKRRREEEN FPGAARILGH LEDGPPRKRV GLLVDGKLPV
REGAKLFDGE DEIGVVTSGG FAPSVGAPIA MGYVPRDHAV PGTAIAAEVR GKLVHCTVAA
MPFVPHRYVR KTGG
//
