ID A0A0M3AMZ7_9SPHN Unreviewed; 383 AA.
AC A0A0M3AMZ7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=YP76_16680 {ECO:0000313|EMBL:KKW91205.1};
OS Sphingobium chungbukense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW91205.1, ECO:0000313|Proteomes:UP000033874};
RN [1] {ECO:0000313|EMBL:KKW91205.1, ECO:0000313|Proteomes:UP000033874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ77 {ECO:0000313|EMBL:KKW91205.1,
RC ECO:0000313|Proteomes:UP000033874};
RA Kim Y.-C., Chae J.-C.;
RT "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT chungbukense DJ77.";
RL Submitted (APR-2015) 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}.
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:KKW91205.1}.
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DR EMBL; LBIC01000007; KKW91205.1; -; Genomic_DNA.
DR RefSeq; WP_046764720.1; NZ_LBIC01000007.1.
DR AlphaFoldDB; A0A0M3AMZ7; -.
DR STRING; 56193.YP76_16680; -.
DR PATRIC; fig|56193.3.peg.3494; -.
DR Proteomes; UP000033874; 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:KKW91205.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKW91205.1}.
FT DOMAIN 21..270
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 299..375
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 383 AA; 41299 MW; 94BD65036C73B470 CRC64;
MSGNDDIAHI EEELPLQDLP LDAWHRAKGA RMVGFAGYHM PIQYEGIMAE HGWTREHAGL
FDVSHMGQLT FSGEGVDEAL EHLLPSDIKG LKPFRQRYSM LLDEEGGILD DLMVSRIGGD
AFDGADIYMV VNGATKYDDI GWMIEHLPDE VVMNHMDEQA LLALQGPEAG EALATLIPET
AALVFMQSGP FVWRGVPLWI SRSGYTGEDG FEISVPAGDV VLLADALCAL PQVKPIGLGA
RDSLRLEAGL PLYGHDLTPA VSTIGADLGF AIQKRRREEG GFIGHARVMK ELADGPGSRR
VGLKIEGRLP AREGAAIYAG DVLVGEVTSG GFAPTVGAPI AMGWVSLPHA GLDEALEIEV
RGKRIAATVA PMPFVPHRYR RKA
//
