(data stored in ACNUC1104 zone)

SWISSPROT: E6V0A8_VARPE

ID   E6V0A8_VARPE            Unreviewed;       915 AA.
AC   E6V0A8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Methionine synthase {ECO:0000256|PIRNR:PIRNR000381};
DE            EC=2.1.1.13 {ECO:0000256|PIRNR:PIRNR000381};
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|PIRNR:PIRNR000381};
GN   OrderedLocusNames=Varpa_0200 {ECO:0000313|EMBL:ADU34422.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34422.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34422.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34422.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
CC       cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
CC       methionine. Subsequently, remethylates the cofactor using
CC       methyltetrahydrofolate. {ECO:0000256|PIRNR:PIRNR000381}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-methionine;
CC         Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381,
CC         ECO:0000256|PIRSR:PIRSR000381-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1. {ECO:0000256|PIRNR:PIRNR000381}.
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DR   EMBL; CP002417; ADU34422.1; -; Genomic_DNA.
DR   STRING; 595537.Varpa_0200; -.
DR   EnsemblBacteria; ADU34422; ADU34422; Varpa_0200.
DR   KEGG; vpe:Varpa_0200; -.
DR   eggNOG; ENOG4108EW3; Bacteria.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251409; -.
DR   KO; K00548; -.
DR   OMA; ADCIAMS; -.
DR   BioCyc; VPAR595537:G1GQO-201-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd02069; methionine_synthase_B12_BD; 1.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   Gene3D; 3.10.196.10; -; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR033706; Met_synthase_B12-bd.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR   InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   Pfam; PF02965; Met_synt_B12; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   PIRSF; PIRSF000381; MetH; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   SUPFAM; SSF56507; SSF56507; 1.
DR   TIGRFAMs; TIGR02082; metH; 1.
DR   PROSITE; PS50974; ADOMET_ACTIVATION; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   4: Predicted;
DR   PRODOM; E6V0A8.
DR   SWISS-2DPAGE; E6V0A8.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Cobalamin {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-
KW   1}; Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-1};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00346, ECO:0000313|EMBL:ADU34422.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00346, ECO:0000313|EMBL:ADU34422.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381}.
FT   DOMAIN       28    289       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      324    422       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      431    570       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      584    915       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      523    524       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION      882    883       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   METAL       444    444       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     489    489       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     634    634       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING     828    828       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING     832    832       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   915 AA;  101217 MW;  F41AE28DA568F3E0 CRC64;
     MAQTPQISVP PMKLSGLEPV AIGEGTLFVN IGERTNVTGS KAFARMILNG QFEEALAVAR
     QQVENGAQVI DINMDEAMLD SKVAMVRFLN LIASEPDIAR VPVMVDSSKW DVIEAGLRCI
     QGKGIVNSIS MKEGVDKFKH EAKLVKRYGA AAVVMAFDEK GQADTYERKV EICERAYRIL
     VDEVGFPPED IIFDPNIFAI ATGIEEHDNY AVDFINAVRW IKENLPGAKV SGGVSNVSFS
     FRGNDPMREA IHTVFLYHAI KAGMDMGIVN AGMVGVYDDL EPELRERVED VVLNRRPDAG
     ERLVEVAETA KSGAKDESKR LEWRGTPESP VHVNQRLSHA MVHGITDFIV EDTEEAYQQI
     LAKGGRPLHV IEGPLMDGMN IVGDLFGAGK MFLPQVVKSA RVMKSAVAHL LPYIEEEKLR
     DEAAGRDVRT KGKIIIATVK GDVHDIGKNI VTVVLQCNNF EVVNMGVMVP CHEILARAKV
     EGADIVGLSG LITPSLEEMQ YVAGEMQRDD HFRIKKIPLM IGGATTSRVH TAVKIAPHYE
     GPVVYVPDAS RSVSVAQSLL SDQATAYIDE INADYEKVRT QHANKKQVPM WPLAKARANK
     TPIDWTNYVP PVPKFIGRRV FKNFDLTELA KYIDWGPFFQ TWDLAGPFPA ILKDEVVGTE
     AVRVYADGQR MLKRLIEGRW LSASGIVGFW PANTVNDDDI ELYTDETRSE VALTWYGMRQ
     QTEKQMIDGV MRPSRCLADF VAPKDSGLKD YVGVFAVTAG LGVEKKEKYF IDDLDDYSAI
     MLKALADRLA EAFAESLHHR SRTDLWGYAP DEGLSNEDMI GEKYRGIRPA PGYPACPDHS
     VKGPMFDLLA CADIGMTLTE SLAMMPAASV SGFYLSHPDA TYFNVGKIGH DQLQDQAARR
     KESESDLERL LAPNL
//

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