ID A0A419RR41_9SPHN Unreviewed; 866 AA.
AC A0A419RR41;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:RJY08251.1};
DE EC=2.1.1.13 {ECO:0000313|EMBL:RJY08251.1};
GN Name=metH {ECO:0000313|EMBL:RJY08251.1};
GN ORFNames=D6201_01755 {ECO:0000313|EMBL:RJY08251.1};
OS Aurantiacibacter aquimixticola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1958945 {ECO:0000313|EMBL:RJY08251.1, ECO:0000313|Proteomes:UP000285232};
RN [1] {ECO:0000313|EMBL:RJY08251.1, ECO:0000313|Proteomes:UP000285232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSSK-14 {ECO:0000313|EMBL:RJY08251.1,
RC ECO:0000313|Proteomes:UP000285232};
RX PubMed=28820100; DOI=10.1099/ijsem.0.002055;
RA Park S., Jung Y.T., Choi S.J., Yoon J.H.;
RT "Erythrobacter aquimixticola sp. nov., isolated from the junction between
RT the ocean and a freshwater spring.";
RL Int. J. Syst. Evol. Microbiol. 67:2964-2969(2017).
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:RJY08251.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RAHX01000001; RJY08251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419RR41; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000285232; Unassembled WGS sequence.
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 9..269
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 300..394
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 401..536
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 551..866
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
FT BINDING 344
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 411..415
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 414
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 459
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 463
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 515
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 600
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 777
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 832..833
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
SQ SEQUENCE 866 AA; 94974 MW; B4B0EAC993B94101 CRC64;
MTNLSTARFV NIGERTNVTG SAAFKKLIMA GDYPTAVEVA RQQVENGAQI IDVNMDEGLL
DAVEAMTTFL KLIAAEPDIA RVPVMIDSSK FEVIEAGLKC VSGKPIVNSI SMKEGEAQFL
EQAGICRDYG AAVVVMAFDE TGQADTKERK VEICSRAYDL LVRNGFPPED IIFDPNIFAV
ATGIAEHDRY GLDFIEAVAE IKQRCPYAKT SGGLSNLSFS FRGNETVRRA MHSVFLYHAI
PAGLDMAIVN AGQLDVYDTI DPQLREACED VILARRPDAS ERLVDLAESY KGKSKEDEKA
EAEWRSLEVT KRLEYALVKG IDAHIVADTE EARQSAKRPI EVIEGPLMDG MNVVGDLFGS
GKMFLPQVVK SARVMKKAVA HLIPFIEAEK DKLAPEERKA KGKVIMATVK GDVHDIGKNI
VGVVLQCNGY EVIDLGVMVP WSTILETARE QDADIIGLSG LITPSLDEMV TVAEEMQRAD
MTLPLLIGGA TTSRLHTALR IDPAYKGPVL HVLDASRAVG VASRLLSDTQ RDGLVNDTAG
EYQVMRDKRA GKEASKLLTL GEARENGFAA DFSRKSPAPA QPGLHVFGDW DLADLVSCFD
WTPFFRSWEL AGTYPAILDD EVVGESARAL KADADAMLQL IVGEKWLMAK AVCGFWPCRR
DGDDIRLDSG ELIPMLRQQV AKSRDRANYC LADFIDPAGD WIGGFGVAIH GIDPHIARFK
AETDDYSDIL LKALADRFAE ALAERLHQHV RTDLWGYAPD ERLSNADLIR ERYDGIRPAP
GYPACPDHSL KPILFDLLDA TKNAGLTLTD SNAMLPTSAV SGMYFSHPDS SYFGVARIGG
DQLTDYAERR GMPIEDATRW LRPNLD
//
