ID   A0A117S4T9_9SPHN        Unreviewed;       348 AA.
AC   A0A117S4T9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:KUO51498.1};
GN   ORFNames=APF78_04025 {ECO:0000313|EMBL:KUO51498.1};
OS   Sphingomonadales bacterium BRH_c3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1734408 {ECO:0000313|EMBL:KUO51498.1, ECO:0000313|Proteomes:UP000061825};
RN   [1] {ECO:0000313|EMBL:KUO51498.1, ECO:0000313|Proteomes:UP000061825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c3 {ECO:0000313|EMBL:KUO51498.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
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:KUO51498.1}.
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DR   EMBL; LOET01000136; KUO51498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117S4T9; -.
DR   Proteomes; UP000061825; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          4..321
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   348 AA;  37296 MW;  EB784469C5CA613A CRC64;
     MNARERLNAA AAERILIKDG PYGTAIQNAK LSPEEYAGNT GLAQDQKGNN DLVNLTQPQV
     IRAICDRYIA AGATVLATNT FNANRISQAD YGAEGLVHEI NVAAARIIRQ ACDEATAKDG
     VPRFVCGAMG PTNKTLSLSP DVEDPGFREV TFDEVKDVYR EQASALLEGG AEFILIETVF
     DTLNCKAAIM AVKELEAERG QDIPLMISLT LTDLSGRNLS GHTVEAFWYA VRHARPATIG
     LNCSFGADQL RPHVQLLSQI ADTLLMAYPN AGLPNELGEY DELPETTARL VRQWAEGGRV
     NILGGCCGST PEHIAAVAEA VAGIAPREVP SLAHEMRLAG LEPFTIAA
//