ID A0A1I5J3D1_9BRAD Unreviewed; 382 AA.
AC A0A1I5J3D1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05216330_10475 {ECO:0000313|EMBL:SFO66916.1};
OS Bradyrhizobium sp. Ghvi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855319 {ECO:0000313|EMBL:SFO66916.1, ECO:0000313|Proteomes:UP000198509};
RN [1] {ECO:0000313|EMBL:SFO66916.1, ECO:0000313|Proteomes:UP000198509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ghvi {ECO:0000313|EMBL:SFO66916.1,
RC ECO:0000313|Proteomes:UP000198509};
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; FOVU01000004; SFO66916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5J3D1; -.
DR STRING; 1855319.SAMN05216330_10475; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000198509; 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:SFO66916.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFO66916.1}.
FT DOMAIN 15..264
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 296..377
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 382 AA; 40498 MW; A32964A1FB12D750 CRC64;
MLAPDDQTSL KRTPLYDLHV SLGGKMVPFA GYDMPVQYPA GVLKEHLHTR SAAGLFDVSH
MGQLRLLPKS GKVEDAARAL ERLVPQDIVA IAQGRQRYAQ FTNADGGILD DLMVANFGDH
LFLVVNAACK DADEAHLRAN LADACEIESL ADRALIALQG PKAETALAKL CAAAPAMKFM
DAGPHEVAGI ECFVSRSGYT GEDGFEISVP GADAERLTQM LLQNPDVMPI GLGARDSLRL
EAGLCLYGHD IDTTTTPVEA ALEWSVQKSR RTGGARAGGF PGADKILAHF DQGASRRRVG
LRAEGRAPVR EGALLFADQA GGEPIGKVSS GGFGPSLNAP VAMGYVPTAL SALGTKLFAE
VRGQRLPLAV AAMPFVKNTY KR
//