ID A0A0T2L2J0_9MICO Unreviewed; 345 AA.
AC A0A0T2L2J0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000313|EMBL:KRA26149.1};
DE EC=2.1.1.14 {ECO:0000313|EMBL:KRA26149.1};
GN ORFNames=ASD65_16200 {ECO:0000313|EMBL:KRA26149.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA26149.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA26149.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA26149.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA26149.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA26149.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00009553}.
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:KRA26149.1}.
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DR EMBL; LMGU01000001; KRA26149.1; -; Genomic_DNA.
DR RefSeq; WP_056225105.1; NZ_LMGU01000001.1.
DR AlphaFoldDB; A0A0T2L2J0; -.
DR STRING; 1736570.ASD65_16200; -.
DR OrthoDB; 244285at2; -.
DR Proteomes; UP000051216; Unassembled WGS sequence.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 1.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR016456; Met_Synthase_cat.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR30519:SF0; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF005632; Met_synth_catalytic_prd; 1.
DR SUPFAM; SSF51726; UROD/MetE-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KRA26149.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW Transferase {ECO:0000313|EMBL:KRA26149.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 5..328
FT /note="Cobalamin-independent methionine synthase MetE C-
FT terminal/archaeal"
FT /evidence="ECO:0000259|Pfam:PF01717"
SQ SEQUENCE 345 AA; 38690 MW; 088630759273BA46 CRC64;
MNSLLPTSIV GSLPKPSWLA EPETLWSPWK LEGDALVEGK QDALRIAVQE QRRRGIDIIS
DGEQTRQHFV TTFIEHLSGV DFEQRETVRI RNRYDASVPT VVGAVSREQS VFVEDAKFLR
QQTDQPIKWA LPGPMTMIDT LYDRHYKSRE KLAWEFATIL NEEAKELEAA GVDIIQFDEP
SFNVFFDEVQ DWGVATLERA AEGLRAETVV HICYGYGIKA NTDWKATLGA EWRQYEQTFP
LLQRSIIDTV SLESQHSHVP MDLIELIRGK KVMLGAIDVA SETIETPAEV ADTLRNALRF
VDADKLIPST NCGMAPLPRD VALGKLSALS AGADIVREEI AAAQR
//
