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Database: UniProt
Entry: A0A0B4E2S2_9RHOB
LinkDB: A0A0B4E2S2_9RHOB
Original site: A0A0B4E2S2_9RHOB 
ID   A0A0B4E2S2_9RHOB        Unreviewed;       349 AA.
AC   A0A0B4E2S2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:KID12439.1};
GN   ORFNames=P279_28160 {ECO:0000313|EMBL:KID12439.1};
OS   Rhodobacteraceae bacterium PD-2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1169855 {ECO:0000313|EMBL:KID12439.1, ECO:0000313|Proteomes:UP000023196};
RN   [1] {ECO:0000313|EMBL:KID12439.1, ECO:0000313|Proteomes:UP000023196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD-2 {ECO:0000313|EMBL:KID12439.1,
RC   ECO:0000313|Proteomes:UP000023196};
RX   PubMed=25700405;
RA   Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT   "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT   Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT   Prorocentrum donghaiense.";
RL   Genome Announc. Announc.3:e01549-14(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}.
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:KID12439.1}.
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DR   EMBL; AWRV02000010; KID12439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B4E2S2; -.
DR   HOGENOM; CLU_004914_3_0_5; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000023196; 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   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000023196};
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          12..339
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   349 AA;  36518 MW;  26187981ABD5C635 CRC64;
     MLPFALPDAP ALATLRAVAE HRILILDGAM GTMIQTLGLS EEDFTDGGHV HGPGCRHHPT
     DHPQKGNNDL LSLTRPKAIE DIHFAFAMAG ADILETNTFS STTIAQADYG LESAVHDLNV
     AGAQVARRAA DRATAEDGRP RFVAGAVGPT NRTASISPDV NDPGYRAVSF DDLRTAYGQQ
     IDGLIEGGSD LILIETIFDT LNAKAAIFAA FESFARAGRR LPIMISGTIT DASGRTLSGQ
     TPTAFWHSVA HARPFSVGLN CALGAAAMRP HIAELSGVAP TLICAYPNAG LPNAFGQYDE
     TAEQTAEQVA GFAQEGLVNI VGGCCGTTPD HIRAIAEAVA PFAPRTVPA
//
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