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METE_STRAW
ID   METE_STRAW              Reviewed;         772 AA.
AC   Q82LG4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=SAV_2046;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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}.
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DR   EMBL; BA000030; BAC69757.1; -; Genomic_DNA.
DR   RefSeq; WP_010983486.1; NZ_JZJK01000086.1.
DR   AlphaFoldDB; Q82LG4; -.
DR   SMR; Q82LG4; -.
DR   STRING; 227882.SAV_2046; -.
DR   PRIDE; Q82LG4; -.
DR   EnsemblBacteria; BAC69757; BAC69757; SAVERM_2046.
DR   KEGG; sma:SAVERM_2046; -.
DR   eggNOG; COG0620; Bacteria.
DR   HOGENOM; CLU_013175_0_0_11; -.
DR   OMA; KVMKGML; -.
DR   OrthoDB; 577156at2; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000000428; 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   CHAIN           1..772
FT                   /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT                   methyltransferase"
FT                   /id="PRO_0000098668"
FT   REGION          404..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        709
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         24..27
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         120
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         446..448
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         446..448
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         499
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         499
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         576
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         614
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         614
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         620
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         656
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         658
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         680
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         741
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ   SEQUENCE   772 AA;  83151 MW;  14251874DD7723EC CRC64;
     MTAKSAAAAA RATVYGYPRQ GRGRELKKAI EGYWKGRLDA DALRTTATGL RRDTWQQLAE
     AGIHEVPTGD FSYYDHVLDT SVMVGAIPAR HRAAVEADAL DGYFAMARGT QDVAPLEMTK
     WFDTNYHYLV PELGPDTVFS TDSAKQVAEL GEALALGLTA RPVLVGPVTY LLLAKPAPGV
     AADFDPLTLL DRLLPVYAEV LADLRAAGAE WVQLDEPALV QDRTPAELNA AERAYRVLGG
     LTDRPKLLVA SYFDRLGDAL PVLAEAPVEG LALDFAEGAA ANLDALAAVG GLPGKRLVAG
     VVDGRNIWVN DLEKSLALLG TLLGLADRVD VAASCSLLHV PLDAAAERDI APQVLRWLAF
     ARQKTAEIVT LAKGLGHGTD AIAAQLAANR ADLVSRADSA LTRDPAVRSR TAATTDADAR
     RSGPYPERAA AQRARLGLPL LPTTTIGSFP QTAELRTARA DLRAGRIDSA GYEERIRAEI
     GEVISFQEKA GLDVLVHGEA ERNDMVQYFA ERLTGYLTTQ HGWVQSYGTR YVRPPVLAGD
     ISRPEPMTVP WTTYAQSLTD RPVKGMLTGP VTMLAWSFVR DDQPLGETAR QVALALRDEV
     GDLEAAGTSV IQVDEPALRE TLPLRAADRP AYLAWATEAF RLTTGGVRPD TQIHTHMCYA
     EFGDIVQAID DLDADVISLE AARSHMQVAR ELAEHAYPRE AGPGVYDIHS PRVPGVDETA
     ALLRKGLEAI PAERLWVNPD CGLKTRGWPE TRASLENLVA AARTVRAEHA GS
 
 
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