ID A0A1Y3W8P3_9FIRM Unreviewed; 820 AA.
AC A0A1Y3W8P3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Methionine synthase {ECO:0000256|ARBA:ARBA00013998};
DE EC=2.1.1.13 {ECO:0000256|ARBA:ARBA00012032};
DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|ARBA:ARBA00031040};
GN ORFNames=B5G11_08660 {ECO:0000313|EMBL:OUN69532.1};
OS Drancourtella sp. An57.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Drancourtella.
OX NCBI_TaxID=1965647 {ECO:0000313|EMBL:OUN69532.1, ECO:0000313|Proteomes:UP000196207};
RN [1] {ECO:0000313|Proteomes:UP000196207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An57 {ECO:0000313|Proteomes:UP000196207};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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|ARBA:ARBA00025552}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172,
CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58199; EC=2.1.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001700};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|PROSITE-ProRule:PRU00333};
CC -!- COFACTOR:
CC Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC Evidence={ECO:0000256|ARBA:ARBA00001956};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005178}.
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:OUN69532.1}.
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DR EMBL; NFHY01000009; OUN69532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3W8P3; -.
DR UniPathway; UPA00051; UER00081.
DR Proteomes; UP000196207; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; cd02070; corrinoid_protein_B12-BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR Gene3D; 1.10.1240.10; Methionine synthase 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; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR InterPro; IPR017215; MetH_bac.
DR InterPro; IPR036594; Meth_synthase_dom.
DR InterPro; IPR000489; Pterin-binding_dom.
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; PF00809; Pterin_bind; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037472; DHPS_mtfrase; 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; SSF82282; Homocysteine S-methyltransferase; 1.
DR SUPFAM; SSF47644; Methionine synthase domain; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000196207};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 1..287
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT DOMAIN 316..570
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 599..692
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 694..820
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 581..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 820 AA; 89190 MW; 32744D2E940D0BAD CRC64;
MRERLGKELL FLDGGMGTLL QERGLKPGEL PETWNLKRKE EIIEIHRQYY EAGSDIVLSN
TFGANALKFH DEDCSLREII FAAVDNVKTA RALAGKDDGR HYAALDIGPT GKLLEPMGDL
SFDEAYEAFA QAARYGAEAG ADLIHIETMS DTYEVKAAVL AAKEQTGIPV FATLIFDERG
KLLTGGDVTG TVAMLEGLGV DALGINCGLG PEQMLPILKE ICRHASVPVI VKPNAGLPKQ
RDGKTCYDVT PEIFAGWMKQ LVETGACIIG GCCGTTPAHI RAMTKACRGM QIQVPTEKTE
TIVSSYGQAV VLGDCPVIIG ERINPTGKKR FKQALKEHDI DYILKEGIRQ QEQGAHILDV
NVGLPDIDEP AMMEEVVKEL QGITSLPLQI DTVDQRAMER AMRIYNGKPM VNSVSGKQES
MDMVFPLVKK YGGVVIGLAL DENGIPKTAE GRVEVAGKII REAAKYGIRP KDIVIDVLTM
TISSEPEGAI TVLQALEMVR KKYHVRTVLG VSNISFGLPY RPAVNSVFYA LAMQKGLTAG
IINPGSEEMM KAYRSYLALM NFDKNCEAYI AAYADYKPAG PARTGSPASG KTDSAGGASG
TGKDRKTGEM DLRYTIERGL KEEAGRLAKA LAETEEPLSI INQHLIPALD TVGKRFEQGT
LFLPQLLMSA DAAKEAFAVL KDTMEQSGIV QEKNGKIILA TVKGDIHDIG KNIVKVLLEN
YGFDVIDLGK DVDPERIVET AVEEDIRLVG LSALMTTTVV NMEETIRLLR KEKPDCQVMV
GGAVLNQEYA DMIGADFYGK DAMQSVHFAQ KVLHSGEKES
//
