ID   A0A0K1NGG6_9BURK        Unreviewed;       348 AA.
AC   A0A0K1NGG6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AKU67973.1};
GN   ORFNames=ADJ79_03170 {ECO:0000313|EMBL:AKU67973.1};
OS   Ottowia sp. oral taxon 894.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ottowia.
OX   NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU67973.1, ECO:0000313|Proteomes:UP000056623};
RN   [1] {ECO:0000313|Proteomes:UP000056623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (JUL-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}.
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DR   EMBL; CP012073; AKU67973.1; -; Genomic_DNA.
DR   RefSeq; WP_050716366.1; NZ_CP012073.1.
DR   AlphaFoldDB; A0A0K1NGG6; -.
DR   STRING; 1658672.ADJ79_03170; -.
DR   KEGG; oto:ADJ79_03170; -.
DR   PATRIC; fig|1658672.3.peg.865; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000056623; Chromosome.
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          9..330
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   348 AA;  37259 MW;  C0D285FFC1F7804D CRC64;
     MNLPAYTRAQ DLPATLSKRL VILDGAMGTM IQRFKLDEAQ YRGERFKDFA RDVKGNNELL
     SLTRPDVIAD IHDKYLAAGA DLIETNTFGA TSIAQEDYGM ADLAREMNLA SARLARAACD
     RHATPERPRY VAGALGPTPR TASISPDVND PGARNITFEQ LRAAYLEQAL ALIEGGADVL
     LVETIFDTLN AKAALFAIEQ AFDATGERLP VIISGTVTDA SGRVLSGQTV TAFWHSVRHA
     RPLAVGLNCA LGAALMRPYI QELAKAAADT FISCYPNAGL PNPMSETGFD ETPEVTSRLV
     HEFAAEGLVN IVGGCCGTTP DHINAIARAV MPLAPRGVQA ARFYAAQA
//