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Database: UniProt
Entry: D3D371_9ACTN
LinkDB: D3D371_9ACTN
Original site: D3D371_9ACTN 
ID   D3D371_9ACTN            Unreviewed;       772 AA.
AC   D3D371;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFC82598.1};
DE            EC=2.1.1.13 {ECO:0000313|EMBL:EFC82598.1};
DE   Flags: Fragment;
GN   ORFNames=FrEUN1fDRAFT_4243 {ECO:0000313|EMBL:EFC82598.1};
OS   Parafrankia sp. EUN1f.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC82598.1, ECO:0000313|Proteomes:UP000004777};
RN   [1] {ECO:0000313|EMBL:EFC82598.1, ECO:0000313|Proteomes:UP000004777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1f {ECO:0000313|EMBL:EFC82598.1,
RC   ECO:0000313|Proteomes:UP000004777};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA   Fernandez M., Tisa L.;
RT   "The draft genome of Frankia sp. EUN1f.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFC82598.1}.
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DR   EMBL; ADGX01000069; EFC82598.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3D371; -.
DR   Proteomes; UP000004777; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd02069; methionine_synthase_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 1.10.288.10; Cobalamin-dependent Methionine Synthase, domain 2; 1.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR   Gene3D; 3.10.196.10; Vitamin B12-dependent methionine synthase, activation domain; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR033706; Met_synthase_B12-bd.
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   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
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   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   SUPFAM; SSF56507; Methionine synthase activation domain-like; 1.
DR   SUPFAM; SSF47644; Methionine synthase domain; 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   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00346}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00346}.
FT   DOMAIN          1..155
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
FT   DOMAIN          185..279
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51337"
FT   DOMAIN          294..429
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          442..772
FT                   /note="AdoMet activation"
FT                   /evidence="ECO:0000259|PROSITE:PS50974"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFC82598.1"
SQ   SEQUENCE   772 AA;  83433 MW;  15759CE31E9ADD28 CRC64;
     EEPFLAQARR IRDFGAGVVV MAFDEQGQAD TTERKVAICA RAYDLLTQKV GFPATDIIFD
     PNVLAVATGI AEHNGYAKAF VDALPLIKQR CPGVRISGGI SNLSFSFRGN DVVREAMHSA
     FLLHAVRAGL DMGIVNAGQL AVYADIPADL LELVEDVLFD RRDDATDRLV AFAETVSGSG
     TKRVVDLSWR EAPVAQRLSH ALVHGIVDFI EADTEEARAV AARPLDVIEG PLMDGMKIVG
     DLFGSGKMFL PQVVKSARVM KRSVAYLEPF MEAEKQALLA AGGSAEADSG RRGNGRVVMA
     TVKGDVHDIG KNIVGVVLGC NNYEVIDLGV MVPAKVILDT AVAEGADAVG LSGLITPSLD
     EMVAVAAEMQ RRGLKLPLLI GGATTSRQHT AVRIAPAYDG TTVHVLDASR VVGVVSDLLD
     DDRAAELAIR NRSEQQELRE AHEKRQQQPL LTLAQARANR EQVSFDDLPV PAFTGLRVVR
     PELAELRAMI DWQFFFLAWE LKGKYPAILE QPVARELYDD GNALLDQIIA DGGLRAEGVY
     GFWPAAADGD DILIDVAAAG TAATVEPTVS AADGRLRLAM LRQQTTKPTG RPNRSLADYV
     APAGDHLGAF AVAIHGADRL AAEYEARQDD YRAIMVKALA DRLAEAFAEY VHLEARRAWF
     EPGSEPALED LHAERFRGIR PAFGYPASPD HTEKRPLFDL VGAEQVGLGL TESFAMTPAS
     AVSGIIFASP AARYFTVGRI GRDQVEDYAA RRGMSVAEAE RWLRPNLAYD PE
//
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