ID W0IUD2_9BACT Unreviewed; 363 AA.
AC W0IUD2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AHF89685.1};
GN ORFNames=OPIT5_05015 {ECO:0000313|EMBL:AHF89685.1};
OS Opitutaceae bacterium TAV5.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF89685.1, ECO:0000313|Proteomes:UP000003813};
RN [1] {ECO:0000313|EMBL:AHF89685.1, ECO:0000313|Proteomes:UP000003813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV5 {ECO:0000313|EMBL:AHF89685.1};
RX PubMed=25744998;
RA Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA Rodrigues J.L.;
RT "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT Potential Facultative Methylotroph of the Wood-Feeding Termite
RT Reticulitermes flavipes.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; CP007053; AHF89685.1; -; Genomic_DNA.
DR AlphaFoldDB; W0IUD2; -.
DR STRING; 794903.OPIT5_05015; -.
DR KEGG; obt:OPIT5_05015; -.
DR eggNOG; COG0646; Bacteria.
DR HOGENOM; CLU_004914_3_0_0; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000003813; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR PROSITE; PS50970; HCY; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000003813};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 17..337
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT REGION 342..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 363 AA; 38436 MW; 1542B81521E0A2E9 CRC64;
MSAASTSAAP PAGSPSFAAL RELFASRIAI LDGAMGSMVQ TWKLQEADFR GARFAGHPHD
LQGNNDLLVL TRPDVIEKIH ADYFAAGADI VETNTFNSTR ISQADYHLEP LVTELNTAAV
ALALRAARAA EAATPGRRCF VAGAIGPLNR TLSMSPDVNR PDYRAVTWAQ VVDAYTEQVR
ALVAAGVDAL LVETIFDTLN AKAALFAIEG VFDELGTRLP VMISVTITDA SGRTLSGQTP
EAFYNSIRHA RPFSVGINCA LGGAGMRPFV EELARLAECP VTCYPNAGLP NAFGGYDETP
ADMARILRQF AEAGLVNLVG GCCGSTPAHI KAIADAVRGL PPRPIPPRHT DLRLSGLEPL
TLS
//
