ID T0G8V6_9SPHN Unreviewed; 872 AA.
AC T0G8V6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EQA97081.1};
GN ORFNames=L485_23695 {ECO:0000313|EMBL:EQA97081.1};
OS Sphingobium baderi LL03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQA97081.1, ECO:0000313|Proteomes:UP000015524};
RN [1] {ECO:0000313|EMBL:EQA97081.1, ECO:0000313|Proteomes:UP000015524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL03 {ECO:0000313|EMBL:EQA97081.1,
RC ECO:0000313|Proteomes:UP000015524};
RX PubMed=24051322;
RA Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT Sphingobium baderi Strain LL03T.";
RL Genome Announc. 1:e00751-13(2013).
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:EQA97081.1}.
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DR EMBL; ATIB01000088; EQA97081.1; -; Genomic_DNA.
DR RefSeq; WP_021247254.1; NZ_KQ130471.1.
DR AlphaFoldDB; T0G8V6; -.
DR PATRIC; fig|1114964.3.peg.4654; -.
DR eggNOG; COG1410; Bacteria.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000015524; 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:UP000015524};
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 306..400
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 403..538
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 553..872
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
FT BINDING 350
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 413..417
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 416
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 461
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 465
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 517
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 602
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 783
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 838..839
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
SQ SEQUENCE 872 AA; 96097 MW; 98A0C877A1A94474 CRC64;
MTTQPSATNF VNIGERTNVT GSAKFKKLIM AGDYATAIDI AREQVENGAQ VVDVNMDEGL
LDAVEAMTTF LKLMTSEPDI SRVPVMIDSS KWEVIEAGLK CVSGKPIVNS ISMKEGEEAF
LVHARKVMAY GAAVVVMAFD ETGQADTKER KVEICARAYD LLVGIGFPPE DIIFDPNIFA
VATGIEEHNN YGVDFIEACK EIKARCPHVH ISGGLSNLSF SFRGNEPVRR AMHSIFLYHA
IPAGMDMGIV NAGQLDVYDA IDPELREACE DVILNRPQRD PSVTPTERLV ELAEKFRGTG
GEVDKAAEEW RGWPVAKRLE HALVKGIDMY VVEDTEEARL SADKPIEVIE GPLMDGMNVV
GDLFGAGKMF LPQVVKSARV MKKAVAHLLP YIEAAKEPGA KGKGKVVMAT VKGDVHDIGK
NIVGVVLQCN GFEVIDLGVM VPWQDILKAA NENDADMIGL SGLITPSLDE MVTVAQEMQR
ADMSMPLLIG GATTSRVHTA LRIDPAFTGP VVHVLDASRA VGVATALVSQ TQKTDFVQKT
KDDYEHVRVA RANKGQSALL SLEDARANAF EIDENLKPPR PRLPGVHRFP DWDLKDLRDY
IDWTPFFRAW ELAGNYPAIL TDDIVGESAA SLFADAQKML DRIIDEKWLT ARGVAGLWPC
AREGDDIIVH VEDERHVHLP MLRQQIAKRE GRANMCLADF ISPDGDWIGG FAVSLHGIEP
HLARFKNAID DYSDILLKAL ADRLAEAFAE RLHHYVRTAL WGYAEGEQLT NEALIKEQYR
GIRPAPGYPA CPEHSLKPLL FDMLDAHHAT GITLTESFAM LPTAAVSGFY FGHPQAEYFG
VARIGRDQLE DYAQRRGVDV ETAERWLRPN LD
//
