ID A5ZUF2_9FIRM Unreviewed; 289 AA.
AC A5ZUF2;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDM86732.1};
GN ORFNames=RUMOBE_02637 {ECO:0000313|EMBL:EDM86732.1};
OS Blautia obeum ATCC 29174.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=411459 {ECO:0000313|EMBL:EDM86732.1, ECO:0000313|Proteomes:UP000006002};
RN [1] {ECO:0000313|EMBL:EDM86732.1, ECO:0000313|Proteomes:UP000006002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM86732.1,
RC ECO:0000313|Proteomes:UP000006002};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM86732.1, ECO:0000313|Proteomes:UP000006002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM86732.1,
RC ECO:0000313|Proteomes:UP000006002};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus obeum (ATCC 29174).";
RL Submitted (APR-2007) 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:EDM86732.1}.
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DR EMBL; AAVO02000012; EDM86732.1; -; Genomic_DNA.
DR RefSeq; WP_005422212.1; NZ_DS264297.1.
DR AlphaFoldDB; A5ZUF2; -.
DR GeneID; 79804507; -.
DR eggNOG; COG0646; Bacteria.
DR HOGENOM; CLU_004914_3_0_9; -.
DR Proteomes; UP000006002; 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; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR11103; SLR1189 PROTEIN; 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..288
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|PIRSR:PIRSR037505-2,
FT 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"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 289 AA; 30660 MW; 75F440942BCCA00E CRC64;
MTKEEFRKLT ENILILDGAT GSNLMASGMP RGICTETWVI DHKDIIQDLQ RAYIQAGSQV
IYAPTFGGNS INLEKHGLRD KIEEINRTLV GYSKELAGSG IYVAGDITTS GSFITADGDY
TYTEAYNMYQ EQIRILADAG IDLIAAETMI NIEETLAAVD AAASVCDLPI MCTMTVEADG
SIFSGGNAVE AAVSLEAAGA DAVGINCSVG PDQLVSVVRN IKENVSIPVI AKPNAGMPVI
DEKGNAVYSM NAEEFAHHMK VLIENGASVV GGCCGTTPSF IKALHDTIR
//
