ID A0A2A2SHL4_9SPHN Unreviewed; 861 AA.
AC A0A2A2SHL4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:PAX08757.1};
GN Name=metH {ECO:0000313|EMBL:PAX08757.1};
GN ORFNames=CKY28_05195 {ECO:0000313|EMBL:PAX08757.1};
OS Sphingomonas lenta.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1141887 {ECO:0000313|EMBL:PAX08757.1, ECO:0000313|Proteomes:UP000218151};
RN [1] {ECO:0000313|Proteomes:UP000218151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1PNM-20 {ECO:0000313|Proteomes:UP000218151};
RA Feng G., Zhu H.;
RL Submitted (SEP-2017) 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}.
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:PAX08757.1}.
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DR EMBL; NSLI01000002; PAX08757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2SHL4; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000218151; Unassembled WGS sequence.
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:UP000218151};
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 8..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 396..531
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 546..861
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 406..410
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 409
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 454
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 458
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 510
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 595
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 772
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 827..828
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
SQ SEQUENCE 861 AA; 93846 MW; AE887EB3BCF7B476 CRC64;
MTASTAQFVN IGERTNVTGS AKFKKLVMAG DYAQAVEVAR QQVEAGAQVI DVNMDEGLLD
AEAAMTTFLK LIAAEPDIAR VPVMVDSSKW SVIEAGLKCV SGKPIVNSIS MKEGEEPFLD
QARRCMAYGA AVVVMAFDEV GQADTRERKV EICTRAYKLL CGIGFPPEDI IFDPNIFAVA
TGIEEHNNYA VDFIEACRDI KAACPHVHIS GGLSNLSFSF RGNEPVRRAM HSVFLYHAIP
AGMDMAIVNA GQLDVYDTID PELRQGCEDV ILNRDLGATE RLIALAEKFK GGDAVAEKAA
QEWRGWDVRK RLEHALVKGI DAHIVDDTEE ARQAHARPIE VIEGPLMDGM NVVGDLFGSG
KMFLPQVVKS ARVMKKAVAH LLPYIEAEKS AGARSKGRIV MATVKGDVHD IGKNIVGVVL
QCNGFEVVDL GVMVPWAKIL EAANENDADM IGLSGLITPS LDEMVTVAEE MSRAKMTMPL
LIGGATTSKV HTALRIAPAY DGPVVHVLDA SRAVGVATTL VSETGRDAYV ANVAADYQAV
RDSRAGKGAN ELLPLAEARA RGFAADMALK APAAARPGVH RFDDWPLEDL RGHIDWTPFF
RAWELAGTYP AILQDEVVGE SATNLYADAQ GMLDRIVGEK WLTARGVAAL WPCRREGDDV
VLGSGERFPF LRQQINKREG RANMCLADFV DPAGDWMGGF AVGIHGIEPH LERYKANHDD
YNDILLKALA DRLAEAFAEA LHRHVRTTLW GYAPDEQLTN EALIREQYRG IRPAPGYPAC
PEHSLKRTLF ELLDAEGAAG LTLTDSFAML PTAAVSGFYF GHAQAEYFGV ARIGRDQVED
YAQRRGVSVE QAERWLRPNL D
//
