ID D2B6D6_STRRD Unreviewed; 287 AA.
AC D2B6D6;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ACZ85700.1};
GN OrderedLocusNames=Sros_2740 {ECO:0000313|EMBL:ACZ85700.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ85700.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ85700.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
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DR EMBL; CP001814; ACZ85700.1; -; Genomic_DNA.
DR RefSeq; WP_012889445.1; NC_013595.1.
DR AlphaFoldDB; D2B6D6; -.
DR STRING; 479432.Sros_2740; -.
DR KEGG; sro:Sros_2740; -.
DR eggNOG; COG2040; Bacteria.
DR HOGENOM; CLU_004914_3_2_11; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000002029; Chromosome.
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|PROSITE-ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000002029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 1..284
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 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 287 AA; 30343 MW; 3634D037570DD973 CRC64;
MVILDGGLAT HLEALGADLR DELWSAKLLL ENPSVIRQAH LDYFTAGAEV ATTASYQASI
PAFVRRGLSA REAEELIVLS VRLAAEARDS HGTGTVAASV GPYGAYLANG AEYTGDYDLD
EDGLADWHRD RWHILAGSGA DLLACETIPS YAEARALGRL LAETPGTRAW VSFSCRDGEH
ISDGTPLKDA AALFAGNPQV IAVGVNCTAP RHITSLIGRI EGKPVMVYPN SGETWDAANR
RWLGLADPAE FGAAAAGWHA AGSAFVGGCC RTTPEHIRQI GEHLKAG
//