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Database: UniProt
Entry: L5NDB2_9BACI
LinkDB: L5NDB2_9BACI
Original site: L5NDB2_9BACI 
ID   L5NDB2_9BACI            Unreviewed;       290 AA.
AC   L5NDB2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ELK48068.1};
DE            EC=2.1.1.10 {ECO:0000313|EMBL:ELK48068.1};
GN   Name=mmuM {ECO:0000313|EMBL:ELK48068.1};
GN   ORFNames=D479_04113 {ECO:0000313|EMBL:ELK48068.1};
OS   Halobacillus sp. BAB-2008.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK48068.1, ECO:0000313|Proteomes:UP000010769};
RN   [1] {ECO:0000313|EMBL:ELK48068.1, ECO:0000313|Proteomes:UP000010769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK48068.1,
RC   ECO:0000313|Proteomes:UP000010769};
RX   PubMed=23469348;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT   BAB-2008.";
RL   Genome Announc. 1:E00222-12(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
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:ELK48068.1}.
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DR   EMBL; ANPF01000013; ELK48068.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5NDB2; -.
DR   PATRIC; fig|1246484.3.peg.863; -.
DR   eggNOG; COG2040; Bacteria.
DR   Proteomes; UP000010769; Unassembled WGS sequence.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061627; F:S-methylmethionine-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   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; 2.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000010769};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          1..287
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   290 AA;  32295 MW;  A3678A94A1A2FADE CRC64;
     MATELETYGF DLDDPLWSAR VLLENPDAIR KVHADYFRNG ADIAITASYQ ATIDGFKQRG
     IDEDKARTLI KDTVRLAQEA RSDVWREADD RAYPVVAGSV GPYGAYLADG SEYIGNYGVT
     DERLKEFHRP RIEALIEAGA DVLAFETIPS LQEAEVLTEL LGEYPGASAW LSFSLKNGSQ
     ISDGTEWRRC IDVIEGREQV VAVGVNCAPI PDATEAVGHI RALTDKPIIL YPNSGETYDP
     DTNDWYGERS CQRFDEQSDR WVEAGATIIG GCCRTTPDHI QSLARRWQNR
//
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