ID F6ET73_SPHCR Unreviewed; 867 AA.
AC F6ET73;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEG50447.1};
DE EC=2.1.1.13 {ECO:0000313|EMBL:AEG50447.1};
GN ORFNames=Sphch_2812 {ECO:0000313|EMBL:AEG50447.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG50447.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG50447.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG50447.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002798; AEG50447.1; -; Genomic_DNA.
DR RefSeq; WP_013848682.1; NC_015593.1.
DR AlphaFoldDB; F6ET73; -.
DR STRING; 690566.Sphch_2812; -.
DR KEGG; sch:Sphch_2812; -.
DR HOGENOM; CLU_004914_2_0_5; -.
DR Proteomes; UP000007150; Chromosome 1.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
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}; 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 10..270
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 301..395
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 398..533
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 548..867
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
FT BINDING 345
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 408..412
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 411
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 456
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 460
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 512
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 778
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 833..834
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
SQ SEQUENCE 867 AA; 95561 MW; 5B4BC30B04137FD2 CRC64;
MTQQTSTATF VNIGERTNVT GSAKFKKLIM AGDYAAAIDI ARDQVENGAQ IVDVNMDEGL
LDAVEAMTTF LKLMTSEPDI SRVPVMIDSS KWEVIEAGLK CVSGKPVVNS ISMKEGEEAF
LHHARLCMAY GAAVVVMAFD ETGQADTKDR KVEICERAYK LLLSIGFPPE DIIFDPNIFA
VATGIEEHNN YGLDFIEACR EIKKRCPHVH ISGGLSNFSF SFRGNEPVRR AMHSVFLYHA
IPAGLDMAIV NAGQLDVYDA IDPALRKACE DVLLNSDPEA GDRLVALAES YKGKDAASEK
AAQEWRGWPV AKRLEHALVK GIDMYVVEDT EEARLAAEKP IQVIEGPLMD GMNVVGDLFG
AGKMFLPQVV KSARVMKKAV AHLLPFIEAA KEPGAKGKGK VVMATVKGDV HDIGKNIVGV
VLQCNGFEVI DLGVMVPWQD IIKAANENDA DMIGLSGLIT PSLDEMVTVA AEMQRADMTM
PLLIGGATTS RVHTALRIDP AFKGPVVHVL DASRAVGVAT ALVSETQKDD FVARTKDDYE
HVRKAREGKG QSKLLSIEEA RANAFEIDES LKPGKPRLPG VHRFPDWDLK DLRNYIDWTP
FFRAWELAGN YPAILDDEVV GESATSLFND AQAMLDRVIN EKWLTARGVA GLWPCRREGD
DIIVHVEDEK HVTLPMLRQQ IAKREGRANM CLADFISHDG DWMGGFAVSI HGIEPHLARF
KNAIDDYSDI LLKALADRLA EAFAERLHHY VRTALWGYAE GEQLTNEALI KEQYRGIRPA
PGYPACPEHS LKPLLFDMLD AHHATGITLT ESFAMLPTAA VSGFYFGHPQ AEYFGVARVG
RDQLEDYAQR RGVDMETAER WLRPNLD
//
