ID A0A0U4X9Q7_9GAMM Unreviewed; 875 AA.
AC A0A0U4X9Q7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Methionine synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATY27_15855 {ECO:0000313|EMBL:ALZ77081.1};
OS Rheinheimera sp. F8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ77081.1, ECO:0000313|Proteomes:UP000059499};
RN [1] {ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA Schuster A.K., Szewzyk U.;
RT "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming strain
RT which produces large amounts of extracellular DNA.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALZ77081.1, ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|EMBL:ALZ77081.1,
RC ECO:0000313|Proteomes:UP000059499};
RX PubMed=26966195;
RA Schuster A.K., Szewzyk U.;
RT "Draft Genome Sequence of Rheinheimera sp. F8, a Biofilm-Forming Strain
RT Which Produces Large Amounts of Extracellular DNA.";
RL Genome Announc. 4:0-0(2016).
CC -!- COFACTOR:
CC Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1};
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; CP013656; ALZ77081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4X9Q7; -.
DR Proteomes; UP000059499; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 CDD; cd00740; MeTr; 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; IPR011822; MetH.
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 NCBIfam; TIGR02082; metH; 1.
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 PIRSF; PIRSF000381; MetH; 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 Cobalamin {ECO:0000256|PIRSR:PIRSR000381-1};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000381-1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00346}; Reference proteome {ECO:0000313|Proteomes:UP000059499};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR000381-2};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00346}.
FT DOMAIN 7..268
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 299..393
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 397..532
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 548..875
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
FT BINDING 343
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 407..411
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 410
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-1"
FT BINDING 455
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 459
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 511
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 597
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 786
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 841..842
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
SQ SEQUENCE 875 AA; 97127 MW; 18B59A915A8D1764 CRC64;
MQQQARFINI GERTNVTGSA RFKKLIMDGK YEAALDVARQ QVVSGAQIID INMDEAMLDS
KAAMVRYLNL LASEPDIARV PIMVDSSKWE VIEAALKCIQ GKAVVNSISL KEGEAPFIQQ
AKLLRRYGAA VVVMAFDEVG QADTKARKVE ICQRAYKILV EQIGFPPQDI IFDPNIFAVA
TGIEEHNNYA VDFIEATREI KRLCPHAKIS GGVSNVSFSF RGNDPVREAI HSVFLYHAIK
AGMDMGIVNA GQLAVYDDIP ELLKERVEDV VLNRRDDATE RLLEVAAQFH GKGTVAVKED
NAWRSWPVTK RLEHALVKGI TDFIDEDTEE ARQSVERPLH VIEGPLMDGM NVVGDLFGEG
KMFLPQVVKS ARVMKKAVAY LQPYIEAEKA GTGATTQGKV LMATVKGDVH DIGKNIVGVV
LQCNNYEVID LGVMVPCATL LQKAKELNVD VIGLSGLITP SLDEMVHVAK EMTRLGFTVP
LLIGGATTSK AHTAIKIAPH YAHGVVYVPN ASRSVSVVQS LISAEHKPDY LARVQDEYVR
VIEQHQRSRK HEEMLSLEQA RANRFSLDLN KVAAAPQQPG VHVWHDVDLQ VLRDYIDWTP
FFLTWQLSGK FPAILNHAEV GLEARRVYQD ANALLDRMIA ERRISGKAVF GLFPANSDGD
DIIVWTDESR STERCRLYNL RQQVALRNNA PNCCMADFVA PADSGIADYI GAFAVSTGYG
ADEYAAEFAH AHDDYNSIMV KALADRLAEA LAEYLHMKVR KEYWGYAANE QLDNEQLIRE
AYQGIRPAPG YPACPEHTEK GTLFSLLDAE AQIGMLLTES YAMWPGAAVS GWYLSHPDSK
YFAVSKIGED QLEQYAAKKG WNRQEAESWL APNLR
//
