ID A0A127MGW4_9SPHN Unreviewed; 871 AA.
AC A0A127MGW4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AMO72401.1};
GN ORFNames=AZE99_11535 {ECO:0000313|EMBL:AMO72401.1};
OS Sphingorhabdus sp. M41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO72401.1, ECO:0000313|Proteomes:UP000073959};
RN [1] {ECO:0000313|EMBL:AMO72401.1, ECO:0000313|Proteomes:UP000073959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:AMO72401.1,
RC ECO:0000313|Proteomes:UP000073959};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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; CP014545; AMO72401.1; -; Genomic_DNA.
DR RefSeq; WP_067201218.1; NZ_CP014545.1.
DR AlphaFoldDB; A0A127MGW4; -.
DR STRING; 1806885.AZE99_11535; -.
DR KEGG; sphg:AZE99_11535; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000073959; 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}; 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..398
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..871
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
FT BINDING 348
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 781
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 836..837
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
SQ SEQUENCE 871 AA; 96539 MW; 4FB3F3ED1694EA99 CRC64;
MTQSSSTNFV NIGERTNVTG SARFKKLILN DDYEAAVEVA RQQVENGAQV IDINMDEGLL
DAHHAMTTFL KLISAEPDIA RVPVMIDSSK WSVIEAGLKC VSGKPIVNSI SMKEGEEEFL
NHARKCMAYG AAVVVMAFDE TGQADTKDRK IEICERAYKL LTGIGFPPED IIFDPNVFAI
ATGIDEHRRY GLDFIEATRE IRKRCPHVHI SGGLSNLSFS FRGNEPVRKA MHSVFLYHAI
PAGMDMAIVN AGQLDIYDDI DPELRELCED VIFDRRDDAT DRLITLAEKF RGTDEVAEKA
AAEWRGYEVH KRLEHALVKG IDAHIVEDTE EMRLAVKNRS GRPIEVIEGP LMDGMNIVGD
LFGSGKMFLP QVVKSARVMK KAVAHLFPYI EAEKDEKAKG KGKIIMATVK GDVHDIGKNI
VGVVLQCNGF EVIDLGVMVS WTDILKAANE NNADIIGLSG LITPSLDEMV TVAEEMERAK
MQTPLLIGGA TTSKTHTALR IEPAYTGPTI HVLDASRAVG VASQLVSDTQ AVGFIAKTRE
DYEQVRIARA GKTGKKLATL EEARANAAKV DMSLKAAAPA KPGLHVYEDW DLAELRNYID
WTPFFRAWEL AGNYPAILTD KIVGESASDL FRDAQVMLDK IIEEKWLTAK GVAGIWRARR
EGDDILVSPE NEEFTLPMLR QQVVKRGGKP NNCLADFIDS ADDWIGGFAV TAGHGIDEHV
QRFEMDKDDY NSILLKALAD RLAEAFAERM HEHVRKDLWG YAADENLNNK DLVREKYKGI
RPAPGYPACP DHSLKPILFD MLNATENTGI ELTSGFAMTP TAAVSGFYFA HPEADYFGVA
RISEDQVEEY ATRRGVSVDQ ARQWLRPNLN E
//
