ID A0A136NJD0_9BACT Unreviewed; 764 AA.
AC A0A136NJD0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:KXK46156.1};
GN ORFNames=UZ10_BCD003001362 {ECO:0000313|EMBL:KXK46156.1};
OS Bacteroidetes bacterium OLB10.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617421 {ECO:0000313|EMBL:KXK46156.1, ECO:0000313|Proteomes:UP000070480};
RN [1] {ECO:0000313|EMBL:KXK46156.1, ECO:0000313|Proteomes:UP000070480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB10 {ECO:0000313|EMBL:KXK46156.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK46156.1}.
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; LNBX01000030; KXK46156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136NJD0; -.
DR STRING; 1617421.UZ10_BCD003001362; -.
DR PATRIC; fig|1617421.3.peg.1419; -.
DR Proteomes; UP000070480; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008705; F:methionine synthase activity; 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 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; 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 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 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 Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00346}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00346}.
FT DOMAIN 1..135
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 166..260
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 262..397
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 430..764
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
SQ SEQUENCE 764 AA; 85947 MW; 4D59DBFCE7059F64 CRC64;
MLFDEQGQAD TTPRRIEIAK RAYDILVNKV HFTPQDIIFD PNIFPIATGL EEHRKNAVSY
FEATKWIKEN LPLAKVSGGL SNVSFSFRGN DHVREAIHAA FLYHGIHAGM DMGIVNPSQL
IVYDEIEKEL LKKVEDVLLD RTDDATEQLV DFAEAFKGKG KEKTESEEEW RKQPLQDRIT
HSLVKGITDY IEQDTEEARQ QYDKALEVIE GPLMVGMSVV GDLFGSGKMF LPQVVKSARV
MKKAVAYLTP YIEAEKTKGQ SKGKIVLATV KGDVHDIGKS IVGVVLACNN YEIVDLGVMV
PSEKILATAR EQHADMIGVS GLITPSLDEM VHVAKEMERE KFSIPLLIGG ATTSKVHTAV
KIEPHYSGTV VYVNDASRSV PVVSNLLSEE LKENFVAEIK AENERTRTYF KADRAKGNYL
TLDKARANRF EASEQPSTVP NIRDKKYVAG YLQSDDAKRN GAFAIDGNKG IGWSHYSLEE
IAPYIDWTPF FVAWEMKGSY PKIFDNKERG AEAKKLFDEA QDMLQKIIKE KWLTAKAVIG
IFPAAANQDD INLYDEQGNK THTFFTIRQQ SQKAEGQKNA ALADFIRPKG TASAGDSLGL
FALSTGFGIE EKVKEFQKIH DDYSVIMLKA LADRLAEAFA ELLHKRVRKE FWGYDTDENL
SNDELIKEKY HGIRPAPGYP AQPDHTEKFT LWEILDVEKN TGIQLTEHLA MYPTAAVSGL
YFAHPDSYYF AVGKIQRDQV EDYARRKNMS VEDVERWLGS ILAY
//
