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Database: UniProt
Entry: A0A101TAG1_9ACTN
LinkDB: A0A101TAG1_9ACTN
Original site: A0A101TAG1_9ACTN 
ID   A0A101TAG1_9ACTN        Unreviewed;       312 AA.
AC   A0A101TAG1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:KUN88719.1};
GN   ORFNames=AQJ64_01805 {ECO:0000313|EMBL:KUN88719.1};
OS   Streptomyces griseoruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN88719.1, ECO:0000313|Proteomes:UP000052982};
RN   [1] {ECO:0000313|EMBL:KUN88719.1, ECO:0000313|Proteomes:UP000052982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN88719.1,
RC   ECO:0000313|Proteomes:UP000052982};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT   for the species Streptomyces griseoruber.";
RL   Submitted (OCT-2015) 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:KUN88719.1}.
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DR   EMBL; LMWW01000002; KUN88719.1; -; Genomic_DNA.
DR   RefSeq; WP_059202348.1; NZ_KQ948763.1.
DR   AlphaFoldDB; A0A101TAG1; -.
DR   STRING; 1943.AQJ64_01805; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000052982; 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          10..309
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         231
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|PROSITE-ProRule:PRU00333"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   312 AA;  32581 MW;  C7B3A784475E0F87 CRC64;
     MTSDTSSPYG APLAEALATG TVVLDGGMSN QLESAGHDLS DELWSARLLA ERPGAITEAH
     LAYFEAGANV AITSSYQATF EGFAKRGISP EEAARLLALS VELAREAARQ ARDKGITQPL
     WVAASVGPYG AMLADGSEYR GRYGLSVAEL ERFHRPRLEV LAAAAPDVLA LETVPDAEEA
     EALLRAVRGL GVPAWLSYTV DGVRTRAGQP LDEAFALAAE ADEVIAVGVN CCAPEDVDAA
     VATAARVTGK PVVVYPNSGE SWDAQARAWN GRSSFAPEQV LGWRDSGARL IGGCCRVGPE
     AVASIARTLG TA
//
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