ID A0A1M6EG53_9CLOT Unreviewed; 794 AA.
AC A0A1M6EG53;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN02745176_01548 {ECO:0000313|EMBL:SHI84466.1};
OS Lutispora thermophila DSM 19022.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Lutispora.
OX NCBI_TaxID=1122184 {ECO:0000313|EMBL:SHI84466.1, ECO:0000313|Proteomes:UP000184442};
RN [1] {ECO:0000313|EMBL:SHI84466.1, ECO:0000313|Proteomes:UP000184442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19022 {ECO:0000313|EMBL:SHI84466.1,
RC ECO:0000313|Proteomes:UP000184442};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQZS01000009; SHI84466.1; -; Genomic_DNA.
DR RefSeq; WP_073025646.1; NZ_FQZS01000009.1.
DR AlphaFoldDB; A0A1M6EG53; -.
DR STRING; 1122184.SAMN02745176_01548; -.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00051; UER00081.
DR Proteomes; UP000184442; 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:UP000184442};
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..281
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT DOMAIN 310..554
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 572..665
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 669..794
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 794 AA; 86811 MW; 8A8424ADE6F865F3 CRC64;
MSRNVDFNKF LVFDGAMGTM LQACGMKAGE LSERYNIEKP EVIEKIHRAY IDAGADVITT
NTFGANRYKL NDTGLNLNDV ITRAVEVATK AAKDKLVALD VGPLGQLMEP YGSLSFEEAY
EAFKEQVLAG ALAGADIIII ETMSDIYEAK AAILAARENS NLPIICTMTF QEDGRTLTGT
DPLTMVNILQ NLGIAALGIN CSLGPKEMMP LVHEVLKYSR IPVIVQPNAG LPKMAGSETI
FEITPEMFAA YGRQMAEAGV RILGGCCGTT PEHIRELKNA LIGLKPVKTH IERITAASSS
TCTVTLGGEV KIIGERINPT GKKKLKEALM KDDMDYILRE AVDQKDNGAH ILDVNVGIPE
MDEETVMVRA IKEIQGIVNL PLQIDSVKPK VIEAGVRVCN GRPIINSVNG EDKVMETIFP
IVKKYGCLVV ALTLDDGGIP KTAEERLKIA EKIIKRAGEY GIPKEDIIVD CLVLTASAQQ
KEVKETIRAV RLVKEKLGVM TTLGVSNVSF GLPARSLLNR TFLAAALSAG LDAPIMNPMD
ADMRDTVRAF NVLWNHDKDS KEYINAYADS KAKPENNDNK TNKDLKKIII DGLKEEVKET
VREFLKEFKA LEIVDNYLIP ALDIVGEKYE KGEIFLPQLI LSAETVKNAF EVIKEDIMKN
SSHDRAINKG NIVIATVKGD IHDIGKNIAK ILLENYGFQV YDLGKDVPTE KIVGKVKEVK
APLVGLSALM TTTVQSMEET IKALKLHCPD CVVMAGGAVL NENYANMIGA DFYVKDARDS
VKVAEMVING VKKN
//
