ID A0A1N7KWG5_9RHOB Unreviewed; 369 AA.
AC A0A1N7KWG5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN05421580_10377 {ECO:0000313|EMBL:SIS65750.1};
OS Rhodobacter aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=453582 {ECO:0000313|EMBL:SIS65750.1, ECO:0000313|Proteomes:UP000186221};
RN [1] {ECO:0000313|Proteomes:UP000186221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19945 {ECO:0000313|Proteomes:UP000186221};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTOG01000003; SIS65750.1; -; Genomic_DNA.
DR RefSeq; WP_076484097.1; NZ_QAXT01000004.1.
DR AlphaFoldDB; A0A1N7KWG5; -.
DR STRING; 453582.SAMN05421580_10377; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000186221; 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:SIS65750.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186221};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SIS65750.1}.
FT DOMAIN 12..253
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 284..362
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 369 AA; 39025 MW; C9FF1AA7AB2991F7 CRC64;
MAGDTGCKRT SLYDLHVELG AKMVPFAGWE MPVQYPMGVL KEHLHTRVKA GLFDVSHMGQ
VILPIGAVAA LEALVPVDIA GLGLNRQRYA MLTNDAGGIL DDLMVTNRGD HLFLVVNAAC
AEADIAHLKA HIEGVTVVEG RGLLALQGPA AEGVLEAIVP GAAALRFMET ATFLWQGNDL
WVSRSGYTGE DGYEISVPDE VIDAFARALL ANEAVAPIGL GARDSLRLEA GLCLYGHDID
TTTSPVEAGL TWALQKARRA GGAREGGFPG AARILQELAN GPSRKRMGLR PEGRAPMREG
VEIYAAPEGG APIGTVTSGG FGPSIEGPMA MAYLPADLPE GSTVYGEMRG KRLPARITPL
PFHPTSYKR
//
