METE_DICDI
ID METE_DICDI Reviewed; 825 AA.
AC Q54X49;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase;
DE EC=2.1.1.14;
DE AltName: Full=Cobalamin-independent methionine synthase;
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme;
GN Name=metE; ORFNames=DDB_G0279211;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-11; 82-99; 113-129; 164-183; 312-323; 432-440;
RP 461-471; 678-686; 724-735; 747-764 AND 805-812, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000030; EAL67754.1; -; Genomic_DNA.
DR RefSeq; XP_641728.1; XM_636636.1.
DR AlphaFoldDB; Q54X49; -.
DR SMR; Q54X49; -.
DR STRING; 44689.DDB0230069; -.
DR PaxDb; Q54X49; -.
DR PRIDE; Q54X49; -.
DR EnsemblProtists; EAL67754; EAL67754; DDB_G0279211.
DR GeneID; 8621924; -.
DR KEGG; ddi:DDB_G0279211; -.
DR dictyBase; DDB_G0279211; -.
DR eggNOG; KOG2263; Eukaryota.
DR HOGENOM; CLU_013175_0_0_1; -.
DR InParanoid; Q54X49; -.
DR OMA; KVMKGML; -.
DR PhylomeDB; Q54X49; -.
DR UniPathway; UPA00051; UER00082.
DR PRO; PR:Q54X49; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; ISS:dictyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; ISS:dictyBase.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_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 Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Direct protein sequencing; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Reference proteome;
KW Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..825
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000342368"
FT ACT_SITE 761
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 19
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 148
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 498..500
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 498..500
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 551
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 551
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 556
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 579
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 582..583
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 628
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 666
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 666
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 793
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
SQ SEQUENCE 825 AA; 94518 MW; 0AD6B7B9F57F5E67 CRC64;
MVSSSNLGFP RMGENRELKK LVENYWQGKV EETQFQKELK EIRINHWKLQ KEAGIEIIPS
NDFSLYDQVL DHIHLFGAIP KRYTPVVESE IEDGSNGLRT YFAMGRGYQT SKAATQVSET
NTQGAFASKV EKSIDVGSME MKKWFDTNYH YIVPEFEDSQ QFKLTNYGGY SEPKPIHEFL
EAKSIDIETR PVVLGPISFL LLGKSSDSSK PYSSKFDSLV HLNALLGVYE ELFKQFEKIG
VKSVQIDEPV LCFDLFETEL IKNAYTTAFN VIHKAAPNIN ILIATYFGEI RENIDLITSL
PVNGIHIDTI RSSSSEVESV LTKIPTSWTI SIGIIDGRNV WKNDLTKSLV TLKNIIAKTG
SDRILLAPSC SLLHCPHSLT REIGRVESQV LDWLAFSLEK LKEISFLTYA LNKCTFTTEN
TITFPEDTCS KIKEYYQLNK ESNQKRRESK LIHNDIVKKR VTEITPSMLK RENPFPVRRE
AQRKRLTTLP ALFPTTTIGS FPQTKEVRLA RSNFKSKKIT PEAYDQFIRD EIRKCIKVQE
ECELDVLVHG EFERTDMVEY FGEYLAGFVF TQNGWVQSYG SRCVKPPIIY GDVNRPVPMT
LEYTTFAQTL TTKPMKGMLT GPVTILQWSF VRDDQPRSET CFQIGLAIRD EVTDLENKGI
ACIQIDEPAI REGLPLRLSD WNQYLKWAID SFLLSSTGVK DSTQIHSHMC YSDFNDIFES
IQRMDTDVLT IENSKSDLKL LKAFEKYGYT NEIGPGLYDI HSPRIPSVED MKDRVEQMLK
YLSTNLLWIN PDCGLKTREP ETTRLALINM VKVAKQFREI YANKE
