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
//