ID W4S1B4_9XANT Unreviewed; 379 AA.
AC W4S1B4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:GAE49918.1};
GN ORFNames=XPU_1450 {ECO:0000313|EMBL:GAE49918.1};
OS Xanthomonas arboricola pv. pruni str. MAFF 311562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1414836 {ECO:0000313|EMBL:GAE49918.1, ECO:0000313|Proteomes:UP000019143};
RN [1] {ECO:0000313|EMBL:GAE49918.1, ECO:0000313|Proteomes:UP000019143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311562 {ECO:0000313|Proteomes:UP000019143};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:GAE49918.1}.
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DR EMBL; BAVB01000230; GAE49918.1; -; Genomic_DNA.
DR AlphaFoldDB; W4S1B4; -.
DR Proteomes; UP000019143; Unassembled WGS sequence.
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}; 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 23..363
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 379 AA; 40686 MW; F6605D13C4441359 CRC64;
MTQVSNPQSP IRFALPWLHP ERAARLTAAL AERILIIDGA MGTMIQRHDL QEPDYRGTRF
ADGYDSAQVH VHGPGCDHVH APEGHDLKGN NDLLLLSRPE IIAGIHRAYL DAGADLLETN
TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDEVEALT PHKPRFVIGV LGPTSRTASI
SPDVNDPGYR NTSFDALRDT YREAIDGLID GGADTLMVET IFDTLNAKAA LYAIEEVFEA
RRGRLPVMIS GTITDASGRT LSGQTAEAFY ASVAHGRPLS VGLNCALGAK DLRPHVETLA
QIADAYVSAH PNAGLPNAFG EYDETPEEMA ETLREFAQAG LLNLVGGCCG TSPDHIRAIA
EAVADLPPRQ LPGAQELAA
//
