ID A0A1I2MI87_9BACT Unreviewed; 361 AA.
AC A0A1I2MI87;
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=SAMN05216383_10252 {ECO:0000313|EMBL:SFF91225.1};
OS Prevotella sp. KH2C16.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFF91225.1, ECO:0000313|Proteomes:UP000198560};
RN [1] {ECO:0000313|Proteomes:UP000198560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA Varghese N., Submissions S.;
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; FOOW01000002; SFF91225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2MI87; -.
DR STRING; 1855325.SAMN05216383_10252; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000198560; 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:SFF91225.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFF91225.1}.
FT DOMAIN 8..254
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 279..355
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 361 AA; 40578 MW; 529B2A888F9AECE5 CRC64;
MENKRTCLYD KHVALGALIS PFGGFDMPIQ YSSIIEEHNV VRQHCGVFDV SHMGEVIVSG
REAEKFVNHI FTNDVTNMPV GKVMYGMMCY PDGGTVDDTC ICKLDQNLFL MTINASNIDK
DNEWIKENAE GFDAVICYKS DYYGQLAVQG PKAERVVETV LSIPCKELGF YEVKTLDRFD
ENIIISRTGY TGEDGFEIYG THDFIRNCWD KLMEAGVAPC GLGCRDTLRF EVGLPLYGDE
LSKEISPIMA GLSMFVKLDK LEFIGREALL DQKTNGVAKR LRGIELHDKA VPRHGYKVLK
GGKEVGEITT GYRLISIEKS CAVALVDSDI KLGDEVEIQI RKKTFPGTVV KKKFYEKHYK
K
//
