ID I2HM40_9BACI Unreviewed; 315 AA.
AC I2HM40;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EIF11799.1};
GN ORFNames=MY7_0086 {ECO:0000313|EMBL:EIF11799.1};
OS Bacillus sp. 5B6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1127743 {ECO:0000313|EMBL:EIF11799.1, ECO:0000313|Proteomes:UP000005799};
RN [1] {ECO:0000313|EMBL:EIF11799.1, ECO:0000313|Proteomes:UP000005799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5B6 {ECO:0000313|EMBL:EIF11799.1,
RC ECO:0000313|Proteomes:UP000005799};
RX PubMed=22740678; DOI=10.1128/JB.00682-12;
RA Kim B.K., Chung J.H., Kim S.Y., Jeong H., Kang S.G., Kwon S.K., Lee C.H.,
RA Song J.Y., Yu D.S., Ryu C.M., Kim J.F.;
RT "Genome Sequence of the Leaf-Colonizing Bacterium Bacillus sp. Strain 5B6,
RT Isolated from a Cherry Tree.";
RL J. Bacteriol. 194:3758-3759(2012).
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:EIF11799.1}.
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DR EMBL; AJST01000001; EIF11799.1; -; Genomic_DNA.
DR RefSeq; WP_007609171.1; NZ_AJST01000001.1.
DR AlphaFoldDB; I2HM40; -.
DR PATRIC; fig|1127743.3.peg.75; -.
DR Proteomes; UP000005799; 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; 2.
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 2..309
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 229
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 294
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 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 315 AA; 34482 MW; E2D896A74A687E45 CRC64;
MNPISQILNE YPVMIIDGAM ATELERMGCD LHDDLWSAKI LLERPELIKQ VHAEYFAAGA
DCAITASYQS TIEGFAARGI LETDAIRLIQ TSVELAAQAR DEFWAHEENR LHRPKPLVAA
SIGPYGASLA DGSEYRGHYG LTEDELISFH RPRMKALIES GADLLACETI PCLSEAKAIT
RLLEEFPGTY AWISFSAKDG RHISEGTPIS ECAALLDSCS QIAAIGINCT PIEHIPQLVQ
EIKRATSKPI IAYPNSGEQY DPVTKTWKGA ACENHFGKSA QSWYENGVSL IGGCCRTKPA
DIQAIADWAK TLKTT
//
