ID G8NBD9_9DEIN Unreviewed; 349 AA.
AC G8NBD9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=TCCBUS3UF1_7810 {ECO:0000313|EMBL:AEV15829.1};
OS Thermus sp. CCB_US3_UF1.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=1111069 {ECO:0000313|EMBL:AEV15829.1, ECO:0000313|Proteomes:UP000005635};
RN [1] {ECO:0000313|EMBL:AEV15829.1, ECO:0000313|Proteomes:UP000005635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB_US3_UF1 {ECO:0000313|EMBL:AEV15829.1,
RC ECO:0000313|Proteomes:UP000005635};
RA Teh B.S., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT "Complete genome sequence of thermophilic Thermus sp. CCB_US3_UF1.";
RL Submitted (NOV-2011) 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; CP003126; AEV15829.1; -; Genomic_DNA.
DR RefSeq; WP_014515189.1; NC_017278.1.
DR AlphaFoldDB; G8NBD9; -.
DR STRING; 1111069.TCCBUS3UF1_7810; -.
DR KEGG; thc:TCCBUS3UF1_7810; -.
DR PATRIC; fig|1111069.3.peg.759; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_0; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000005635; Chromosome.
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 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:AEV15829.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEV15829.1}.
FT DOMAIN 6..252
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 275..346
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 349 AA; 37468 MW; F0F6BF5C9C081442 CRC64;
MKRTPLYEAH LRHGGRMVAF AGYALPLQYT SIVEEHLAVR RGAGVFDVSH MGEFLVRGEE
ALAFLQWATA NDASKLRVGR AQYSMLLNAQ GGVVDDIYLY RLEEAAYLLV VNAANIAKDW
AHLQGLAQGF RVELEDLSEG TALLALQGPK AAEILQGLTE ADLSKKRKND VFAAQVAGRP
ARLARTGYTG EDGFELFLAP EDAEAVFEAL LAAGAVPAGL GARDTLRLEA GFPLYGHELT
EATNPLCTPW AWVVKREKAF FGKEAALAQA CQEEVVGLVL EVGLPREGYP VLSGGRPVGR
VTSGGYSPLL GKGIALAWVE RGAQGPFFVE VRGKPVGASL SPLPFVPLK
//
