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Database: UniProt
Entry: A0A0T5ZRC3_9BACT
LinkDB: A0A0T5ZRC3_9BACT
Original site: A0A0T5ZRC3_9BACT 
ID   A0A0T5ZRC3_9BACT        Unreviewed;       318 AA.
AC   A0A0T5ZRC3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000313|EMBL:KRT65345.1};
DE            EC=2.1.1.14 {ECO:0000313|EMBL:KRT65345.1};
GN   ORFNames=XU13_C0135G0002 {ECO:0000313|EMBL:KRT65345.1};
OS   Candidatus Rokubacteria bacterium CSP1-6.
OC   Bacteria; Candidatus Rokubacteria.
OX   NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT65345.1, ECO:0000313|Proteomes:UP000051916};
RN   [1] {ECO:0000313|EMBL:KRT65345.1, ECO:0000313|Proteomes:UP000051916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT65345.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-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:KRT65345.1}.
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DR   EMBL; LDXP01000135; KRT65345.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T5ZRC3; -.
DR   STRING; 1640509.XU13_C0135G0002; -.
DR   Proteomes; UP000051916; 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; 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   SUPFAM; SSF51726; UROD/MetE-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:KRT65345.1};
KW   Transferase {ECO:0000313|EMBL:KRT65345.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          7..308
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
SQ   SEQUENCE   318 AA;  36571 MW;  CE404B625B6AB5B4 CRC64;
     MPGWLERLKT DYFLRRISRH DLEEIHDTAV KAAIKDQEMA GIDIVTDGEL RRDNMIDYFA
     GRLPGVQIDH ASKKFYYDFF DSVVRGKLPT APLGLVDDFK FLRRFTERPT KFSITGPHSL
     VRRIRNEYYP SEEAFALDIA RVMNLELREL VKAGATYLQI DEPYYSGFPE DVRWGVKVLN
     VLTEGVDAKI GLHICYGNRY GKPTWEGSYR YLFPAILDAR VQQLTLEFAR RGEEDVALFR
     EFKAPFELGL GVIDVKNPTV ETPDMVAERI RKALEIVPAE RLYVNPDCGC LHLPRDVAFA
     KLCAMVEGTR LVRKELET
//
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