(data stored in SCRATCH zone)

SWISSPROT: C5BC96_EDWI9

ID   C5BC96_EDWI9            Unreviewed;       758 AA.
AC   C5BC96;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172, ECO:0000256|SAAS:SAAS00101669};
DE            EC=2.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00172};
DE   AltName: Full=Cobalamin-independent methionine synthase {ECO:0000256|HAMAP-Rule:MF_00172};
DE   AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000256|HAMAP-Rule:MF_00172};
GN   Name=metE {ECO:0000256|HAMAP-Rule:MF_00172};
GN   OrderedLocusNames=NT01EI_0132 {ECO:0000313|EMBL:ACR67387.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67387.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC       methyltetrahydrofolate to homocysteine resulting in methionine
CC       formation. {ECO:0000256|HAMAP-Rule:MF_00172,
CC       ECO:0000256|SAAS:SAAS00101695}.
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L-
CC       homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_00172, ECO:0000256|SAAS:SAAS00101678}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetE route): step
CC       1/1. {ECO:0000256|SAAS:SAAS00363622}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine
CC       synthase family. {ECO:0000256|HAMAP-Rule:MF_00172,
CC       ECO:0000256|SAAS:SAAS00577555}.
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DR   EMBL; CP001600; ACR67387.1; -; Genomic_DNA.
DR   RefSeq; WP_015869606.1; NC_012779.2.
DR   ProteinModelPortal; C5BC96; -.
DR   STRING; 634503.NT01EI_0132; -.
DR   EnsemblBacteria; ACR67387; ACR67387; NT01EI_0132.
DR   GeneID; 7959846; -.
DR   KEGG; eic:NT01EI_0132; -.
DR   PATRIC; fig|634503.3.peg.123; -.
DR   eggNOG; ENOG4105DSS; Bacteria.
DR   eggNOG; COG0620; LUCA.
DR   HOGENOM; HOG000246221; -.
DR   KO; K00549; -.
DR   OMA; GRNIWKN; -.
DR   OrthoDB; POG091H0282; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-HAMAP.
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   Pfam; PF08267; Meth_synt_1; 1.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR   TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BC96.
DR   SWISS-2DPAGE; C5BC96.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00172,
KW   ECO:0000256|SAAS:SAAS00050074};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00172,
KW   ECO:0000256|SAAS:SAAS00468534};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00172,
KW   ECO:0000256|SAAS:SAAS00050076};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172,
KW   ECO:0000256|SAAS:SAAS00050078, ECO:0000313|EMBL:ACR67387.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00172};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00172,
KW   ECO:0000256|SAAS:SAAS00050075, ECO:0000313|EMBL:ACR67387.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00172, ECO:0000256|SAAS:SAAS00101720}.
FT   DOMAIN        5    312       Meth_synt_1. {ECO:0000259|Pfam:PF08267}.
FT   DOMAIN      428    750       Meth_synt_2. {ECO:0000259|Pfam:PF01717}.
FT   METAL       643    643       Zinc. {ECO:0000256|HAMAP-Rule:MF_00172}.
FT   METAL       645    645       Zinc. {ECO:0000256|HAMAP-Rule:MF_00172}.
FT   METAL       728    728       Zinc. {ECO:0000256|HAMAP-Rule:MF_00172}.
SQ   SEQUENCE   758 AA;  84732 MW;  262B6A22A4ED4151 CRC64;
     MQAISHTLGF PRIGLQRELK KALEAYWSGS APQSALLACG AELRARHWRQ QHKAGIDLLP
     VGDFAWYDHV LATSLMLGNV PARHRRADGV IDLDTLFGIA RGQAPGGKPA AAAEMTKWFN
     TNYHYIVPEF TRGQRFSLGW HQLLDEVDEA LAQGYRVKPV LLGPLTYLWL GKVKGAPFDR
     LSLLEEILAV YRQVLAALAE RGVEWVQVDE PALVLTLPPA WRDAYQNAYQ ALQGPVKLLL
     TTYFGDIGHH LPTICALPVQ GLHVDLVQGA GDALALHRQL PADWVLSLGA ISGRNVWRAD
     LADWQTRLQP LVGQRPIWLG SSCSLLHTPI DLSAETQLDE EVKSWFAFAL QKCDELALLT
     QALNDPVPRR EALLSYSTPL YLRRRSGRVH NPAVAGRLAA LTDADTQRPS GYPQRAQRQR
     QRFALPLWPT TTIGSFPQTQ AIRALRLDFR RGQLTPEHYR QGIADHIRQA IGEQELLGLD
     VLVHGEAERN DMVEYFGEQL EGFVFTRNGW VQSYGSRCVK PPVIVGDISR PAPLTVEWTT
     FAQAQTARPV KGMLTGPITM LCWSFAREDV PREVIARQLA LALRDEVDDL QRAGIGIIQI
     DEPALREGLP LRQDEWQAYL AWAVAAFRLT AAVAYDDTQI HTHMCYCEFN DIMAAIAALD
     ADVITIETAR SDMELLEAFS RFDYPNEIGP GVYDIHSPNV PTQAAMVELL RRAAQHIPAE
     RLWVNPDCGL KTRGWEETRR ALSNMVAAAR LLRAQTQE
//

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