(data stored in SCRATCH zone)

SWISSPROT: A4ATQ9_MARSH

ID   A4ATQ9_MARSH            Unreviewed;       896 AA.
AC   A4ATQ9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=FB2170_17131 {ECO:0000313|EMBL:EAR00829.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00829.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00829.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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; CP002157; EAR00829.1; -; Genomic_DNA.
DR   STRING; 313603.FB2170_17131; -.
DR   PRIDE; A4ATQ9; -.
DR   EnsemblBacteria; EAR00829; EAR00829; FB2170_17131.
DR   KEGG; fbc:FB2170_17131; -.
DR   eggNOG; ENOG4108H4F; Bacteria.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251409; -.
DR   KO; K00548; -.
DR   OMA; ADCIAMS; -.
DR   BioCyc; MSP313603:G1GNS-203-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000001602; 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; A4ATQ9.
DR   SWISS-2DPAGE; A4ATQ9.
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:UP000001602};
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:EAR00829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
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:EAR00829.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381}.
FT   DOMAIN       25    286       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      316    410       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      418    553       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      569    896       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      506    507       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION      860    861       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   METAL       431    431       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     476    476       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     619    619       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING     805    805       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING     809    809       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   896 AA;  100659 MW;  CDCD01D1FF42B1CF CRC64;
     MSTISQKYLK LSGLEPLVVT PESNFINVGE RTNVAGSKRF LRLIKEEKFE EALDVARHQV
     EGGAQIIDIN MDDGLINGKA AMVKYLNLII AEPDIARVPI MIDSSKWEII EAGLQVVQGK
     CVVNSISLKE GKEQFVQQAK LIKRYGAAVI VMAFDEVGQA DNYERRLEIS KRSYSILVNE
     VGFAPEDIIF DLNVFPVATG MEEHRRNALD FIDATKWVKT NLPYCSVSGG VSNVSFSFRG
     NNPVREAMHS VFLYHAIQAG MNMGIVNPTM LEVYDDIPKD LLKHVEDVIL DRRDDATERL
     LDFAESVVGK AKESKVDLSW REDSLQDRIT RALVKGIDQY IVEDVEEART NVNRPIEVIE
     GHLMTGMNVV GDLFGSGKMF LPQVVKSARV MKKAVAHLLP FIEEEKKNNP DAIAGGAAGK
     ILMATVKGDV HDIGKNIVSV VLACNNYEIV DLGVMVPPEK IINAAKDENV DIIGLSGLIT
     PSLDEMVFLA KEMERQNFNV PLLIGGATTS KAHTAVKIDP QYKNAVVHVN DASRAVTVVG
     DLLQKENSDN YKKEIKLNYE EFRDKFLKRS KQKEYRTINE ARANKFKIDW KTEEVIKPNE
     LGIQVIEDFD LQKLVQFIDW SPFFRSWDLH GKYPDILKDN VVGQQARELF EDAKAMLKTI
     VDKSQLKAKA IFGLFLANSV DSDDIKVLIN DETKKFRTLR QQLKKREGVP NFALADFIAP
     QETGIQDYIG CFCVSTGFGT ADLAAKFEED HDDYSSIMIK ALADRLAEAF AEYLHKEVRT
     KYWGYSSNEH LSNEELIKET YKGIRPAPGY PACPDHLEKL TIWEILGVKE KIDVELTESL
     AMWPAASVSG YYFANPEARY FGLGKIKEDQ VLDYAKRKGI PLEDANKWLA PNIAED
//

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