ID A0A0M7BEC0_9RHOB Unreviewed; 371 AA.
AC A0A0M7BEC0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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 Name=gcvT_2 {ECO:0000313|EMBL:CUH40132.1};
GN ORFNames=JSE7799_02862 {ECO:0000313|EMBL:CUH40132.1};
OS Jannaschia seosinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH40132.1, ECO:0000313|Proteomes:UP000049455};
RN [1] {ECO:0000313|EMBL:CUH40132.1, ECO:0000313|Proteomes:UP000049455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH40132.1,
RC ECO:0000313|Proteomes:UP000049455};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-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}.
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DR EMBL; CYPR01000194; CUH40132.1; -; Genomic_DNA.
DR RefSeq; WP_055664216.1; NZ_CYPR01000194.1.
DR AlphaFoldDB; A0A0M7BEC0; -.
DR STRING; 313367.JSE7799_02862; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000049455; 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:CUH40132.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049455};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH40132.1}.
FT DOMAIN 12..255
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 288..364
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 371 AA; 39401 MW; 90BE0F566982AF08 CRC64;
MDDATQIPLP LAELHAELGG KMVPFAGYAM PVQYPAGVMA EHLHVRTRAG LFDVSHMGQV
IVAGDGAASA LERLMPVNVV GLAEGRQRYG LLTLPDGGVA DDLMVANRGD HLLLVVNGAM
KHLDMDILRA GLPDHSVELH DDRALLALQG PSAEAALEGL VPGTAAMRFM DVGGFEWQEA
DLWISRSGYT GEDGFEISVP IEVADAFARA LLSHEDVLPI GLGARDSLRL EAGMPLYGQD
LTPEISPVEA GLNWAIGKVR RPGGARAGGF TGEDRILHEL TEGPERIRVG LRPDGRAPMR
MGVMLYETED AVAPVGTVTS GGFGPSVGAP IAMGYVPAGT QAGVTLYGDV RGRRMPVTVA
DLPFHQPRYK R
//
