ID A0A1X1Q2Q3_9FIRM Unreviewed; 791 AA.
AC A0A1X1Q2Q3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=D081_2352 {ECO:0000313|EMBL:ORT98849.1};
OS Anaerovibrio sp. JC8.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=1240085 {ECO:0000313|EMBL:ORT98849.1, ECO:0000313|Proteomes:UP000192538};
RN [1] {ECO:0000313|EMBL:ORT98849.1, ECO:0000313|Proteomes:UP000192538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC8 {ECO:0000313|EMBL:ORT98849.1,
RC ECO:0000313|Proteomes:UP000192538};
RA Evans P.N., Cheung J.L., Rosewarne C.P., Morrison M.;
RT "Genomic and phenotypic data suggests Anaerovibrio species JC8 from the
RT bovine rumen reduces fumarate and sulphite to decrease the inhibitory
RT effect of hydrogen.";
RL Submitted (OCT-2012) 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:ORT98849.1}.
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DR EMBL; ANBM01000019; ORT98849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1Q2Q3; -.
DR STRING; 1240085.D081_2352; -.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00051; UER00081.
DR Proteomes; UP000192538; 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}; 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..277
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT DOMAIN 309..553
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 576..670
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 670..791
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 791 AA; 84402 MW; CBACA2B15A44E492 CRC64;
MIHIFDGAMG TILQQKGLLP AGYCPELLNV DKPEEITAVH QQYIDAGSTI IETNTFGGSP
LKLAHYNLSD RAREINIAAV KAARAAAGDK VKIAGSMGPT GKFIKPLGDL DFEDAFENYK
VQAAALAEGG ADYILIETSI DIQEMRAALL AAKEVTSLPI ICQLSYSEDG RTVTGTDPQT
AAITLDAMGA DIIGINCSLG PEQLVPIVKI LSENTEKPIS VQPNAGLPQL VNGKTTFPMG
PEDFGKWAPK LIQAGATYIG GCCGTSPAHI AAIKDALKDF EEPKFKPLRR RLMVASRSKT
VVIDKELPTV LIGERINPTG RKKLAAEIKD GSFLSVKKEA MDQVKAGAKL LDVNMGVGGI
DQAQAMKKAI TEISQLTDAP LVIDTSDPEV LEAGLRAYPG RALINSVSAE KERLRTFIPL
AIKYGAAILC LPLTDDGIPK TAEERIEVMN IIIDEAKKAG LKDGDFLLDG LVMTVAADQD
ACNHVLNTLR LYREKYGYPA TMGLSNISFG LPNRPLINST FFSMCLAAGL DAPIMNPYDE
QMQNALMASM ALLGKDPNGR DFSTNEKNLA VPKKAAVAKH EELTPVEAIK QAVISGDADS
MPELLERALA ENIDPNELTE KALTAAMNEI GVDFGAGRVF LPQVLLSAEA MRSAFNILKE
RFPAQEGEGK GTVVLATVKG DVHDLGKNIV GALLENSGFN LIDLGKDVPA EEIVATAIKN
DADIVGLCAL MTTTMTEIDE VIRQLKESGN TSKVIVGGAA LTQDYADEAG ADYYAQDAVI
ALNIANDIIS K
//
