METE_SALTY
ID METE_SALTY Reviewed; 754 AA.
AC Q9L6N1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00172};
DE EC=2.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00172};
DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000255|HAMAP-Rule:MF_00172};
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172};
GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00172}; OrderedLocusNames=STM3965;
GN ORFNames=STMD1.25;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000255|HAMAP-Rule:MF_00172}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00172};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00172};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00172};
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:0000255|HAMAP-Rule:MF_00172}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000305}.
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DR EMBL; AF233324; AAF33427.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22809.1; -; Genomic_DNA.
DR RefSeq; NP_462850.1; NC_003197.2.
DR RefSeq; WP_000154192.1; NC_003197.2.
DR AlphaFoldDB; Q9L6N1; -.
DR SMR; Q9L6N1; -.
DR STRING; 99287.STM3965; -.
DR PaxDb; Q9L6N1; -.
DR EnsemblBacteria; AAL22809; AAL22809; STM3965.
DR GeneID; 1255491; -.
DR KEGG; stm:STM3965; -.
DR PATRIC; fig|99287.12.peg.4183; -.
DR HOGENOM; CLU_013175_0_0_6; -.
DR OMA; KVMKGML; -.
DR PhylomeDB; Q9L6N1; -.
DR BioCyc; SENT99287:STM3965-MON; -.
DR UniPathway; UPA00051; UER00082.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
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 PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Reference proteome; Repeat; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..754
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098655"
FT ACT_SITE 694
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 17..20
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 117
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 431..433
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 431..433
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 484
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 484
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 515..516
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 561
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 599
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 599
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 605
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 641
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 643
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 726
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ SEQUENCE 754 AA; 84668 MW; 8C8163AABF181BBF CRC64;
MTILTHTLGF PRVGLRRELK KAQESYWAGN TTREALLAVG RELRARHWEQ QKQAGIDLLP
VGDFAWYDHV LTTSLLLGNV PARHQNNDGS VDIDTLFRIG RGRAPTGEPA AAAEMTKWFN
TNYHYIVPEF SKGQQFRLTW TQLLEEVDEA LALGHKIKPV LLGPVTYLWL GKVKGEPFDR
LTLLKDILPV YQHVLAELAK RGIEWVQIDE PALVLELPQA WLDAFKPAYD ALAGQVKLLL
TTYFEGVTPN LDTIIALPVQ GLHVDLIHGK DDVAELHQRL PVDWLLSAGL INGRNVWRAD
LTEKYAQINA IVGKRALWVA SSCSLLHSPI DLSVETRLDT EVKSWFAFAL QKCGELALLR
DALNSGETAA LEEWSAPIQA RRHSRRVHNA AVEKRLAAIT AQDSQRENPY EVRAEAQRAR
FKLPAWPTTT IGSFPQTTEI RGLRLDFKKG NLDANHYRTG IAEHIKQAII EQERLGLDVL
VHGEAERNDM VEYFGEHLDG FVFTQNGWVQ SYGSRCVKPP VVIGDISRPA PITVEWAKYA
QSLTDKPVKG MLTGPVTILC WSFPREDVTR ETIAKQIALA LRDEVADLEA AGIGIIQIDE
PALREGLPLR RSDWDAYLEW GVEAFRINAA VAKDETQIHT HMCYCEFNDI MDSIAALDAD
VITIETSRSD MELLESFEAF DYPNEIGPGV YDIHSPNVPS VEWIEALLKK AAQRIPAQRL
WVNPDCGLKT RGWPETRAAL ANMVKAAHNL RQAK
