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Database: UniProt
Entry: A0A059KQ87_9BURK
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Original site: A0A059KQ87_9BURK 
ID   A0A059KQ87_9BURK        Unreviewed;       328 AA.
AC   A0A059KQ87;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:KDB53652.1};
GN   ORFNames=X805_07340 {ECO:0000313|EMBL:KDB53652.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB53652.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB53652.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB53652.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037505-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505-2};
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:KDB53652.1}.
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DR   EMBL; AZRA01000019; KDB53652.1; -; Genomic_DNA.
DR   RefSeq; WP_051631556.1; NZ_AZRA01000019.1.
DR   AlphaFoldDB; A0A059KQ87; -.
DR   STRING; 34103.SAMN05421778_10963; -.
DR   PATRIC; fig|1286631.3.peg.724; -.
DR   eggNOG; COG2040; Bacteria.
DR   Proteomes; UP000026714; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
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   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   PANTHER; PTHR46015:SF1; ZGC:171603 PROTEIN; 1.
DR   PANTHER; PTHR46015; ZGC:172121; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037505; Betaine_HMT; 3.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}.
FT   DOMAIN          16..324
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   328 AA;  35428 MW;  D2D102BFA543D2BB CRC64;
     MTSPLTPTPP AAEPIDPIAE WLARRPHLIL DGALATELER RGADLRDALW SARLLIEQPE
     LIRAVHLDYF RAGADVATSA SYQATFEGFA RRGLDAEAAA ALMRRSVELA QEARAQWLRE
     RPGDDRRPAP LVAASVGPYG AMKADGSEYR GDYGLDEAAL MAFHRPRLEV LKAAGADLMA
     CETLPCLAEA RALARLMDEL GLRGWISFSC RDGGHTSQGE PIGDCAGALA PFASVVAIGV
     NCTAPQHIAS LVRAIRARTE RPVLVYPNAG EVWDAQAKVW RAGPECAHRA FDAQAMDWSE
     AGARLIGGCC RTSPADIAAL WRRWAQQG
//
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