ID   A0A0S2K3A7_9GAMM        Unreviewed;       351 AA.
AC   A0A0S2K3A7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:ALO42548.1};
GN   ORFNames=PP2015_2050 {ECO:0000313|EMBL:ALO42548.1};
OS   Pseudoalteromonas phenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO42548.1, ECO:0000313|Proteomes:UP000061457};
RN   [1] {ECO:0000313|EMBL:ALO42548.1, ECO:0000313|Proteomes:UP000061457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO42548.1,
RC   ECO:0000313|Proteomes:UP000061457};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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}.
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DR   EMBL; CP013187; ALO42548.1; -; Genomic_DNA.
DR   RefSeq; WP_058030204.1; NZ_CP013187.1.
DR   AlphaFoldDB; A0A0S2K3A7; -.
DR   STRING; 161398.PP2015_2050; -.
DR   KEGG; pphe:PP2015_2050; -.
DR   PATRIC; fig|161398.10.peg.2085; -.
DR   OrthoDB; 8926130at2; -.
DR   Proteomes; UP000061457; Chromosome I.
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:UP000061457};
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          5..325
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   351 AA;  38559 MW;  3AF171DDDD66342B CRC64;
     MPNKSAALKE ALKQRILILD GAMGTMIQEY KFEEEDYRGE RFKDWHVLVK GNNDLLSLTQ
     PDVIADIHRK YLAAGADIIE TNTFNATTIS MEDYEMGSLS REINLESAKL ARKICDEFTK
     KEPHKPRYVA GVLGPTSKTC SISPDVNDPG YRNITFDALV EAYIESTLAL IEGGADLILI
     ETIFDTLNAK AASFAVEEAF EQAGITLPVM ISGTITDASG RTLSGQTTEA FYNSIRHIKP
     ISIGLNCALG PDLLRPYVEE LSRVCETFTS VHPNAGLPNE FGEYDLEADE MSVEIIDWGK
     EGFINIVGGC CGTTPEHIKA FANGLAQIKP RSLPELDVRM RLAGLEACNL N
//