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Database: UniProt
Entry: V4K1W1_9CREN
LinkDB: V4K1W1_9CREN
Original site: V4K1W1_9CREN 
ID   V4K1W1_9CREN            Unreviewed;       330 AA.
AC   V4K1W1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=MGAcid_02870 {ECO:0000313|EMBL:ESQ23517.1};
OS   uncultured Acidilobus sp. MG.
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus; environmental samples.
OX   NCBI_TaxID=1410573 {ECO:0000313|EMBL:ESQ23517.1, ECO:0000313|Proteomes:UP000017902};
RN   [1] {ECO:0000313|EMBL:ESQ23517.1, ECO:0000313|Proteomes:UP000017902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT   "Predominant Acidilobus-like populations from geothermal environments of
RT   Yellowstone National Park exhibit similar metabolic potential in different
RT   hypoxic microbial communities.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:ESQ23517.1}.
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DR   EMBL; AYMA01000001; ESQ23517.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4K1W1; -.
DR   STRING; 1410573.MGAcid_02870; -.
DR   PATRIC; fig|1410573.3.peg.270; -.
DR   UniPathway; UPA00051; -.
DR   Proteomes; UP000017902; 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          9..324
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00288"
SQ   SEQUENCE   330 AA;  38238 MW;  412558D75575D5A3 CRC64;
     MSYQVPSKFP TTVIGSYPKI AGASEIIKRR DRGEISEEEF HRLIRVPISE VVKDYLEAGV
     DIISDGEQSR EDMVVYFAQR VKGYAEGEWV RIFDNMYFRK PIIVGELRRE RSLAIEDWTY
     TSSISQGRPV KFIITGPYTM MEWSFNVFYR DRAELIMALA KIIREEVMDA VKAGAKYVQV
     DEPALSTRPW PEEAQLAGEA LRYVFAGVEA KRVVHICYGR LERLLPYILD YPVDQFALEF
     KNSDFRLLPY LKEYGYNKEL GYGVIDVHSL QVETVEEVKR DIDRLMKLGI LAPERVYINP
     DCGLKRLPRE VAKAKLINMV KAARLAREEW
//
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