ID Q8W0Q7_SORBI Unreviewed; 760 AA.
AC Q8W0Q7;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 08-NOV-2023, entry version 98.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000256|ARBA:ARBA00012034};
DE EC=2.1.1.14 {ECO:0000256|ARBA:ARBA00012034};
GN Name=SB32H17.13 {ECO:0000313|EMBL:AAL73979.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:AAL73979.1};
RN [1] {ECO:0000313|EMBL:AAL73979.1}
RP NUCLEOTIDE SEQUENCE.
RA Park Y.-J., Ramakrishna W., SanMiguel P., Emberton J., Bennetzen J.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAL73979.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15466289; DOI=10.1101/gr.2332504;
RA Swigonova Z., Lai J., Ma J., Ramakrishna W., Llaca V., Bennetzen J.L.,
RA Messing J.;
RT "Close split of sorghum and maize genome progenitors.";
RL Genome Res. 14:1916-1923(2004).
RN [3] {ECO:0000313|EMBL:AAL73979.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15466290; DOI=10.1101/gr.2701104;
RA Lai J., Ma J., Swigonova Z., Ramakrishna W., Linton E., Llaca V.,
RA Tanyolac B., Park Y.J., Jeong O.Y., Bennetzen J.L., Messing J.;
RT "Gene loss and movement in the maize genome.";
RL Genome Res. 14:1924-1931(2004).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001757};
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; AF466201; AAL73979.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8W0Q7; -.
DR HOGENOM; CLU_013175_0_0_1; -.
DR UniPathway; UPA00051; UER00082.
DR ExpressionAtlas; Q8W0Q7; baseline and differential.
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:SF22; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE 1; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000382-2}.
FT DOMAIN 3..311
FT /note="Cobalamin-independent methionine synthase MetE N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08267"
FT DOMAIN 427..750
FT /note="Cobalamin-independent methionine synthase MetE C-
FT terminal/archaeal"
FT /evidence="ECO:0000259|Pfam:PF01717"
FT ACT_SITE 696
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-3"
FT BINDING 18
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 432..434
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 432..434
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 485
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 516..517
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 562
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 600
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 600
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 642
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 644
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 653
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 657
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 666
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 728
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 760 AA; 83789 MW; F652B0B72EB96260 CRC64;
MASHIVGYPR MGPKRELKFA LESFWDGKSS AEDLEKVATD LRSSIWKQMS EAGIKYIPSN
TFSYYDQVLD TTAMLGAVPE RYSWTGGEIG LSTYFSMARG NATVPAMEMT KCHFIVPELG
PSTKFTYASH KAVSEYKEAK ALGIDTVPVL VGPVSYLLLS KPAKGVEKSF SLLSLLGSIL
PIYKEVVAEL KAAGASWIQF DEPTLVKDLD AHELAAFSSA YAELESAFSG LNVLIETYFA
DIPAESYKTL TSLSGVTAYG FDLIRGAKTL DLIRSSFPSG KYLFAGVVDG RNIWADDLAA
SLSTLQSLEA VAGKDKLVVS TSCSLMHTAV DLVNETKLDD EIKSWLAFAA QKVVEVNALA
KALAGQKDEA YFAANAAAQA SRRSSPRVTN EEVQKAAAAL KGSDHRRATT VSSRLDAQQK
KLNLPVLPTT TIGSFPQTPE LRRVRREYKA KKISEEEYIS AIKEEISKVV KIQEELDIDV
LVHGEPERND MVEYFGEQLS GFAFTANGWV QSYGSRCVKP PIIYGDVSRP NPMTVFWSKT
AQSMTARPMK GMLTGPVTIL NWSFVRNDQP RFETCYQIAL AIKKEVEDLE AAGIQVIQID
EAALREGLPL RKSEHAFYLD WAVHSFRITN CGVQDTTQIH THMCYSNFND IIHSIIDMDA
DVITIENSRS DEKLLSVFRE GVKYGAGIGP GVYDIHSPRI PTTEEIADRV NKMLAVLDTN
ILWVNPDCGL KTRKYTEVKP ALTNMVSATK LIRTQLASAK
//
