ID A3LQC9_PICST Unreviewed; 337 AA.
AC A3LQC9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=AdoMet-homocysteine methyltransferase {ECO:0000313|EMBL:ABN65186.2};
DE EC=2.1.1.10 {ECO:0000313|EMBL:ABN65186.2};
GN Name=SAM4 {ECO:0000313|EMBL:ABN65186.2};
GN ORFNames=PICST_30270 {ECO:0000313|EMBL:ABN65186.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65186.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN65186.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000496; ABN65186.2; -; Genomic_DNA.
DR RefSeq; XP_001383215.2; XM_001383178.1.
DR AlphaFoldDB; A3LQC9; -.
DR STRING; 322104.A3LQC9; -.
DR GeneID; 4837518; -.
DR KEGG; pic:PICST_30270; -.
DR eggNOG; KOG1579; Eukaryota.
DR HOGENOM; CLU_004914_3_2_1; -.
DR InParanoid; A3LQC9; -.
DR OMA; TAVINTH; -.
DR OrthoDB; 66796at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
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 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:UP000002258};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 1..335
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 337 AA; 38610 MW; 98894FBDCF017C41 CRC64;
MLSLKEALSK NRLVLDGAMG TELEACIPKD SKIQPRKHPL WSGLVLLNEP NLIKNVHYNY
LEQADVDALI SSTYQISYPS LKEHTDLDDE QIRGIWKKSI DVVEDAILQY RSKNSNSKKK
IYIIGSIGPY ATYLADGSEY TGDYKNASDS DIESYHQPLL EYFLGDDRVD TIGFETIPSF
QEVKVVLKLL SHLFAEQEKR KYYYISFNFD EATITDGTPT EVVISYIDSF LDKYPFLRKY
MVGLGLNCID YHKIGSIVAK INDSQTSAQK PLFPLIVYPN FTIKYVPEED DYRAYKDIEK
WKELVSEWVT IPNVRMIGGC CSTSPKEIKE VRRIIGT
//
