ID A0A1M6GZ41_9RHOB Unreviewed; 374 AA.
AC A0A1M6GZ41;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=SAMN05444000_105170 {ECO:0000313|EMBL:SHJ15203.1};
OS Shimia gijangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1470563 {ECO:0000313|EMBL:SHJ15203.1, ECO:0000313|Proteomes:UP000183982};
RN [1] {ECO:0000313|Proteomes:UP000183982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100564 {ECO:0000313|Proteomes:UP000183982};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQZQ01000005; SHJ15203.1; -; Genomic_DNA.
DR RefSeq; WP_073250836.1; NZ_FQZQ01000005.1.
DR AlphaFoldDB; A0A1M6GZ41; -.
DR STRING; 1470563.SAMN05444000_105170; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000183982; 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:SHJ15203.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183982};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SHJ15203.1}.
FT DOMAIN 9..257
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 288..368
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 374 AA; 39345 MW; AD4EB1D229E63737 CRC64;
MGELLRTPLF DLHVELGAKM VPFAGYEMSV QYPLGVMKEH LHTRASAGLF DVSHMGQVIL
RGESYEAVAT AFETLVPMDV LGLGAERQRY GLFTNDAGGI DDDLMFANRG DHLFVVVNAA
CKDADIARMK TALEPDVSVE VIEDRALVAL QGPAAETALA RLNPVVAEMS FMDVATVTLN
GAECWVSRSG YTGEDGYEIS VPAAEADALC RALLGMDEVE AIGLGARDSL RLEGGLCLYG
NDIDATTSPI EAGLIWAIQK VRRAGGDRAG GFPGASRVFG DLAEGVARKR VGLAPQGRAP
MRAGTQLFAA AEGGDPIGEV TSGGFGPTLE GPVAMGYVGS AQAAVGTEVF GEVRGKRLPV
MVAKMPLVPA NFKR
//
