ID L9XZB8_9EURY Unreviewed; 357 AA.
AC L9XZB8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Methionine synthase {ECO:0000256|HAMAP-Rule:MF_00288};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00288};
DE AltName: Full=Homocysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00288};
GN Name=metE {ECO:0000256|HAMAP-Rule:MF_00288};
GN ORFNames=C489_12307 {ECO:0000313|EMBL:ELY66827.1};
OS Natrinema versiforme JCM 10478.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY66827.1, ECO:0000313|Proteomes:UP000011632};
RN [1] {ECO:0000313|EMBL:ELY66827.1, ECO:0000313|Proteomes:UP000011632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY66827.1,
RC ECO:0000313|Proteomes:UP000011632};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group to L-homocysteine
CC resulting in methionine formation. The physiological methyl donor is
CC unknown. {ECO:0000256|HAMAP-Rule:MF_00288}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00288};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00288};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway. {ECO:0000256|HAMAP-Rule:MF_00288}.
CC -!- SIMILARITY: Belongs to the archaeal MetE family.
CC {ECO:0000256|ARBA:ARBA00007909, ECO:0000256|HAMAP-Rule:MF_00288}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY66827.1}.
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DR EMBL; AOID01000033; ELY66827.1; -; Genomic_DNA.
DR RefSeq; WP_006431556.1; NZ_AOID01000033.1.
DR AlphaFoldDB; L9XZB8; -.
DR STRING; 1227496.C489_12307; -.
DR PATRIC; fig|1227496.3.peg.2492; -.
DR OrthoDB; 17656at2157; -.
DR UniPathway; UPA00051; -.
DR Proteomes; UP000011632; Unassembled WGS sequence.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:InterPro.
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; -; 1.
DR HAMAP; MF_00288; MetE; 1.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR022921; MetE_arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR30519:SF0; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR SUPFAM; SSF51726; UROD/MetE-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00288};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00288}; Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00288};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00288};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00288};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00288}.
FT DOMAIN 21..334
FT /note="Cobalamin-independent methionine synthase MetE C-
FT terminal/archaeal"
FT /evidence="ECO:0000259|Pfam:PF01717"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
SQ SEQUENCE 357 AA; 40364 MW; A9459016476D20C0 CRC64;
MTNENKDQFR PPEHDSDHFL LTTVVGSYPK PKWLNRAKEL YEDDDHGFDA DDYQEAKDDA
SRLITNEHER AGLDVVVDGE MRRNEMVEFF AHRIDGYEFN GPVKVWGHNY FDKPSVVSEV
EYDDSWLVDE YEFTADASDR PVKVPITGPY TLANWSFNEA YEDDDELTLE LADLVNEEIE
KLVDAGARYI QIDEPALATT PDDHAIVGEA LERIVADLPE DVRIGLHVCY GDYSRIYPEI
LEFPVDEFDL ELANGDYDQL DVFKDPEFTK DLALGVCDAH VAEVESVEQI EENIKKGLEV
VPPEQLVVSP DCGVKLLPRE VAYGKMANMV QAARNVEDDL DAGTIDIERG APTPADD
//
