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Database: UniProt
Entry: A0A0P9EL42_RHOGW
LinkDB: A0A0P9EL42_RHOGW
Original site: A0A0P9EL42_RHOGW 
ID   A0A0P9EL42_RHOGW        Unreviewed;       770 AA.
AC   A0A0P9EL42;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000256|ARBA:ARBA00012034};
DE            EC=2.1.1.14 {ECO:0000256|ARBA:ARBA00012034};
GN   ORFNames=RHOBADRAFT_55893 {ECO:0000313|EMBL:KPV72427.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV72427.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV72427.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV72427.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC       methyltetrahydrofolate to homocysteine resulting in methionine
CC       formation. {ECO:0000256|ARBA:ARBA00002777}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000382-2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR000382-
CC       2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004681}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00009553}.
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DR   EMBL; KQ474087; KPV72427.1; -; Genomic_DNA.
DR   RefSeq; XP_018268476.1; XM_018418071.1.
DR   AlphaFoldDB; A0A0P9EL42; -.
DR   STRING; 578459.A0A0P9EL42; -.
DR   GeneID; 28978519; -.
DR   OMA; KVMKGML; -.
DR   OrthoDB; 1326895at2759; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-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:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd03311; CIMS_C_terminal_like; 1.
DR   CDD; cd03312; CIMS_N_terminal_like; 1.
DR   Gene3D; 3.20.20.210; -; 2.
DR   HAMAP; MF_00172; Meth_synth; 1.
DR   InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR   InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR   InterPro; IPR002629; Met_Synth_C/arc.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   NCBIfam; TIGR01371; met_syn_B12ind; 1.
DR   PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR30519:SF0; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR   Pfam; PF08267; Meth_synt_1; 1.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR   SUPFAM; SSF51726; UROD/MetE-like; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000382-2};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000382-2}.
FT   DOMAIN          5..320
FT                   /note="Cobalamin-independent methionine synthase MetE N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08267"
FT   DOMAIN          439..762
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
FT   ACT_SITE        707
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-3"
FT   BINDING         20
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         121
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         444..446
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         444..446
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         497
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         574
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         612
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         612
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         654
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT   BINDING         656
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT   BINDING         678
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT   BINDING         740
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
SQ   SEQUENCE   770 AA;  85593 MW;  FE33BFC284FAA9F8 CRC64;
     MSIQSAVLGF PRIGAKREVK KATEAYWAGK IQAAELQKVA KEQRLARWQT LKDQGVDVIP
     SGDFTLYDHV LDFNATFNII PSRFAQANLS DLDRYFAMGR GHQKDGVDLE AQEMQKWFDS
     NYHYIKSEVS SKTEFKLNNL KPVDEFNEAK EAGITTRPVL VGPITALLLG KAGRDEGAGA
     ASFEPLSLLD KLVPVYGELL KKLEEAGATE VQIDEPSLVM DSTADLGAKY QSTFEAFAKA
     APGLKITLAT YFGRLDKNVE FVAKLPVAAL HIDLDRASEQ LDQVIAAVKP TSLKLSLGLV
     SGRNIWKNDF EASLATAKKA VDALGADRVV VATSSSLLHT PVTLANESRL KPEQKDWFSF
     ATEKAAEVAT LAKALSGADV QAALDANKQS IKARRDFEKN SDAAVRERLA AVTPEQYNRK
     SPFPERLAAQ SKVYKLPQFP TTTIGSFPQT KEIRLARSKH TKGELSTEEY EKFLENEIKH
     AVDFQEAIDI DVLVHGEPER NDMSQYFGEQ LTGFVFTENA WVQSYGSRYV RPPIVVSDVS
     RPHPMTVRWS SYAQSLTKRP MKGMLTGPVT ILNWSFPRAD VSKEVQCKQL ALALRDEVID
     LANAGIFAIQ VDEPAIREGL PLRQVDWDGY LTWAVDSFKL ATAGVEDKTS VHSHFCYSDF
     SLIFEHIKRL DCDVISVEQS KAGGRDLVAF HEKGYENEIG PGLYDIHSPR VPSVEEMKGR
     LDAYLKALPA QKHIWVNPDC GLKTRAWPET EQSLKNMVEV AKLARAERPE
//
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