(data stored in SCRATCH zone)

SWISSPROT: D6XXG6_BACIE

ID   D6XXG6_BACIE            Unreviewed;      1158 AA.
AC   D6XXG6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 69.
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=Bsel_0486 {ECO:0000313|EMBL:ADH98023.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98023.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98023.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000381-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381-
CC       1};
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; CP001791; ADH98023.1; -; Genomic_DNA.
DR   RefSeq; WP_013171452.1; NC_014219.1.
DR   STRING; 439292.Bsel_0486; -.
DR   EnsemblBacteria; ADH98023; ADH98023; Bsel_0486.
DR   KEGG; bse:Bsel_0486; -.
DR   eggNOG; ENOG4105C3R; Bacteria.
DR   eggNOG; COG0646; LUCA.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251408; -.
DR   KO; K00548; -.
DR   OMA; ADCIAMS; -.
DR   OrthoDB; 118138at2; -.
DR   BioCyc; BSEL439292:G1GLR-516-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000000271; 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   Gene3D; 3.20.20.330; -; 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; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
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   Pfam; PF02574; S-methyl_trans; 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   SUPFAM; SSF82282; SSF82282; 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; PS50970; HCY; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   4: Predicted;
DR   PRODOM; D6XXG6.
DR   SWISS-2DPAGE; D6XXG6.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
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:PRU00333};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN        8    310       Hcy-binding. {ECO:0000259|PROSITE:
FT                                PS50970}.
FT   DOMAIN      340    595       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      621    715       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      717    852       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      873   1158       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      805    806       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1155   1156       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   COILED      620    640       {ECO:0000256|SAM:Coils}.
FT   METAL       232    232       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       295    295       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       296    296       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       730    730       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     775    775       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING    1101   1101       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1105   1105       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1158 AA;  127811 MW;  2E856EFB9A493A1E CRC64;
     MTVTTKQASA FRDALKERIL VLDGAMGTML QNANLTPEQF GGEAYEGCNE YLNITAPEVI
     RTIYHDYLEA GADIIETNTF GATDLVLDDY DLGHLAYELN KAAASIAVEE ARAFSTDSEP
     RFVAGAMGPT TKSLSVTGGT TFEELSSAYK EQVEGLLDGG VDLLLLETSQ DMRNVKAAYT
     AIEEVLSERD LDVPLIISGT IEPMGTTLAG QTIESFYISL EHMKPTVVGL NCATGPEFMQ
     DHLRSLSELS TGFVHCYPNA GLPDEEGHYH ETPSSLASKL RDFAEKGWLN VVGGCCGTTP
     EHIRAMKEAV RGFAPRQPAQ ETHHSISGIE PLIYDESLRP ILVGERTNVI GSKKFKRLIA
     DGKFEEASEI ARAQVKRGAM VVDVCLADPD RDEMADMEQF LHYVINKVKV PLMIDSTDEH
     VIEKALTYSQ GKAIINSINL EDGEERFEAV CPLIRRYGAA VVVGTIDEEG MGVSAERKLA
     IAKRSYELLT GKYGIAPEDI IFDPLVFPVG TGDEQYIGSA EATVEGIRLI KKAFPRTMTI
     LGVSNVSFGL PPLGREVLNA AFVYHCTKAG LDYAIVNTEK LERYGSVSED EKKLADELLF
     RTSDETLAEF TAFYRAKKPQ QKVEASKRTL EERLANYIIE GTKEGLYTDL DEALAKYPDP
     LDIINGPLMD GMDEVGKLFN NNELIVAEVL QSAEAMKAAV AHLEPHMEKK ESDDRGKGKI
     LLATVKGDVH DIGKNLVEII LSNNGFQVVN LGIKVASHEL IEAVEREDPD YIGLSGLLVK
     STQQMVITAN DLRERGIDIP ILVGGAALTR KFTETKITRQ YNGLVLYAKD AMNGLSLANK
     LAKPETRDEL VAVQHEKQLK LNEAEAAGDG MASKGKTNTA TADPAQSEVS RDHKVYQPED
     FEPHILRDFR LTHLQPYLNL QTLLGSHLGV NGNVRRKLES GDERTKELLD KVNALIQKGE
     QEKLLRADGM YQFFPAQSNG NDILIYDPND ESSVIERFTF PRQTQAPYMC LSDFLKSVDS
     GEMDRVGFLA VTAGKGIRKL AEAAKESGDY LDSYLVQAVA LELAEGFAER VHQQMRDKWG
     FSDPVDLTMQ DRFSARYQGV RVSYGYPACP NLEDQKKLFG LLKPEKIGIE LTDEYMMEPE
     ASVTAMVFSH PEGRYFNV
//

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