ID E0SST1_IGNAA Unreviewed; 336 AA.
AC E0SST1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 OrderedLocusNames=Igag_0649 {ECO:0000313|EMBL:ADM27481.1};
OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignisphaera.
OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM27481.1, ECO:0000313|Proteomes:UP000001304};
RN [1] {ECO:0000313|EMBL:ADM27481.1, ECO:0000313|Proteomes:UP000001304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC {ECO:0000313|Proteomes:UP000001304};
RX PubMed=21304693; DOI=10.4056/sigs.1072907;
RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL Stand. Genomic Sci. 3:66-75(2010).
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}.
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DR EMBL; CP002098; ADM27481.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SST1; -.
DR STRING; 583356.Igag_0649; -.
DR KEGG; iag:Igag_0649; -.
DR HOGENOM; CLU_040013_3_0_2; -.
DR UniPathway; UPA00051; -.
DR Proteomes; UP000001304; Chromosome.
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 ECO:0000313|EMBL:ADM27481.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001304};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00288, ECO:0000313|EMBL:ADM27481.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00288}.
FT DOMAIN 7..313
FT /note="Cobalamin-independent methionine synthase MetE C-
FT terminal/archaeal"
FT /evidence="ECO:0000259|Pfam:PF01717"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
SQ SEQUENCE 336 AA; 38575 MW; CADDA21FCA5B3262 CRC64;
MMYLPVLPTT VIGSYPRPRW LREIIRGFRQ GRYDADTLRE ALDDAVITVV RDHEEAGIDI
PSDGEMRRDE MVEYFAERIG GFKFYGPVRV WGNNYFRKPA VVEPIKYLKP IVVEEFLFLK
SCTRKPIVKV TITGPYTIAD WSFNEYYRSK EDLAFDLAKV VNQELKKLEE AGALFVQIDE
PALTTHPDEI DWAVQAINKA VEGINIKIGL HVCYSNYELL QKYFDDINVT QFALEFANRG
FRDLHIVKKL GKELGLGVVD VHNKSVEAPE DIAKAITKAM SYIDPEYLYI NPDCGLKLLP
RSIAKKKLEA MVRGTEIVRR ELVKRGIESI PLRTKI
//
