ID A0A2K2FZ34_9SPHN Unreviewed; 874 AA.
AC A0A2K2FZ34;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:PNU04043.1};
GN ORFNames=A8V01_05370 {ECO:0000313|EMBL:PNU04043.1};
OS Novosphingobium guangzhouense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1850347 {ECO:0000313|EMBL:PNU04043.1, ECO:0000313|Proteomes:UP000236327};
RN [1] {ECO:0000313|EMBL:PNU04043.1, ECO:0000313|Proteomes:UP000236327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA925 {ECO:0000313|EMBL:PNU04043.1,
RC ECO:0000313|Proteomes:UP000236327};
RA Sha S.;
RT "Complete genome sequence of Novosphingobium guangzhouense SA925(T).";
RL Submitted (MAY-2016) 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:PNU04043.1}.
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DR EMBL; LYMM01000040; PNU04043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2FZ34; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000236327; 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:UP000236327};
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 10..270
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 308..406
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 409..544
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 559..874
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
FT BINDING 356
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 419..423
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 422
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 467
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 471
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 523
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 608
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 785
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 840..841
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
SQ SEQUENCE 874 AA; 95665 MW; 51C7639ADE42E822 CRC64;
MTATSSGSRF VNIGERTNVT GSAKFKKLIM AGDYPAAIEV ARQQVENGAQ VIDVNMDEGL
LDAVEAMTTY LKLIAAEPDI ARVPVMVDSS KWEVIEAGLK CVSGKPIVNS ISMKEGEEQF
LDHARKCMAY GAAVVVMAFD ETGQADTKER KIEICERAYK LLVGIDFPPE DIIFDPNVFA
VATGIEEHDR YGLDFIEAVV EIRARCPHVH FSGGLSNLSF SFRGNETVRR AMHSVFLYHA
IPAGLDMAIV NAGQLDVYDQ IDPALREACE DVIMMRRPGV GEDGKTATER LIELAESYKG
VNKAEEKAAE EWRGWDVVKR IEHALVRGID AYVVEDTEEA RAAIAAAGGR PIEVIEGPLM
GGMNVVGDLF GSGKMFLPQV VKSARVMKKA VAHLIPFIEA EKDAKTKAKG RIIMATVKGD
VHDIGKNIVG VVLQCNGYEV IDLGVMVPWS KILESANENQ ADIIGLSGLI TPSLDEMVTV
AEEMQRAEMN IPLLIGGATT SKVHTALRID PAYTGTVVHV LDASRAVGVA SQLLSDTQAE
GFKSSVAIDY EKVREARAGK GQSDLLPLAD ARANAFPSDF AHKPAAPAQP GLHVFEDWDL
KDLVETFDWT PFFRAWELAG TYPAILTDDV VGESATSLFA DAQAMLAKII DEKWLTARGV
CAFWPAHSEG DDILLGDGTR LPFLRQQFKK SRGRANFCLS DFVAPQDDWL GGFAVGIHGI
EPHLERFKAA HDDYSDILLK ALADRFAEAF AERLHSHVRT TLWGYAPDEQ LTNEALIREE
YRGIRPAPGY PACPDHSLKP ILFDLLKAQH NAGIVLTESQ AMLPTAAVSG FYFAHPESQY
FGVARIGRDQ LEDYAGRRGV DLATAERWLR PNLD
//
