ID C2EGM1_9LACO Unreviewed; 307 AA.
AC C2EGM1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEJ74293.1};
DE EC=2.1.1.10 {ECO:0000313|EMBL:EEJ74293.1};
GN Name=mmuM {ECO:0000313|EMBL:EEJ74293.1};
GN ORFNames=HMPREF0545_0793 {ECO:0000313|EMBL:EEJ74293.1};
OS Ligilactobacillus salivarius DSM 20555 = ATCC 11741.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423799 {ECO:0000313|EMBL:EEJ74293.1, ECO:0000313|Proteomes:UP000003531};
RN [1] {ECO:0000313|EMBL:EEJ74293.1, ECO:0000313|Proteomes:UP000003531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11741 {ECO:0000313|EMBL:EEJ74293.1,
RC ECO:0000313|Proteomes:UP000003531};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:EEJ74293.1}.
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DR EMBL; ACGT01000005; EEJ74293.1; -; Genomic_DNA.
DR RefSeq; WP_003700965.1; NZ_GG693225.1.
DR AlphaFoldDB; C2EGM1; -.
DR PATRIC; fig|1423799.3.peg.1911; -.
DR HOGENOM; CLU_004914_3_2_9; -.
DR Proteomes; UP000003531; 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; 1.
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 1..303
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 223
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 288
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 289
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 307 AA; 34497 MW; 4ECCFECCD25BA185 CRC64;
MDFTEFLTNN PVVLDGAMST PLERLGADTN NDLWTAKALI DNEELVYEVH KMYFEAGADL
IITDTYQANV QAFEKVGYSE KEARNLIKKA VKIAQKARDD YENRTGKHNY IAGTIGPYGA
YLANGSEYRG DYELSVEEYQ QFHLPRIEEL VNAGVDILAI ETQPKLDEVL AILELLKKKY
PQQKVYVSYT LSDDDTISDG TPLPRAIHAL EDYSQVIAVG INCVKLELVE PALKNMKEIT
DKHLIVYPNS SAVYDPKSKT WSQPKTSATF EELIPNWYEA GARIIGGCCT TGPKEIKAVA
DFIKRNR
//