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Database: UniProt
Entry: I6Z827_MELRP
LinkDB: I6Z827_MELRP
Original site: I6Z827_MELRP 
ID   I6Z827_MELRP            Unreviewed;       293 AA.
AC   I6Z827;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Hcy-binding domain-containing protein {ECO:0000259|PROSITE:PS50970};
GN   OrderedLocusNames=MROS_2095 {ECO:0000313|EMBL:AFN75325.1};
OS   Melioribacter roseus (strain JCM 17771 / P3M-2).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Melioribacteraceae; Melioribacter.
OX   NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN75325.1, ECO:0000313|Proteomes:UP000009011};
RN   [1] {ECO:0000313|EMBL:AFN75325.1, ECO:0000313|Proteomes:UP000009011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX   PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA   Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA   Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT   "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT   organotrophic bacterium representing a novel deep lineage within
RT   Bacteriodetes/Chlorobi group.";
RL   PLoS ONE 8:E53047-E53047(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037505-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505-2};
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DR   EMBL; CP003557; AFN75325.1; -; Genomic_DNA.
DR   RefSeq; WP_014856757.1; NC_018178.1.
DR   AlphaFoldDB; I6Z827; -.
DR   STRING; 1191523.MROS_2095; -.
DR   GeneID; 78567022; -.
DR   KEGG; mro:MROS_2095; -.
DR   PATRIC; fig|1191523.3.peg.2215; -.
DR   eggNOG; COG0646; Bacteria.
DR   HOGENOM; CLU_004914_3_0_10; -.
DR   OMA; AQEDYKM; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000009011; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd00945; Aldolase_Class_I; 1.
DR   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   PANTHER; PTHR11103; SLR1189 PROTEIN; 1.
DR   PANTHER; PTHR11103:SF18; SLR1189 PROTEIN; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037505; Betaine_HMT; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000009011};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}.
FT   DOMAIN          2..291
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   293 AA;  31561 MW;  BC6638096942B2C3 CRC64;
     MRNFIEEVKS GKVLISDGAW GTFLYEKGLS SDECPELWNL THRDKVLEIA KSYIDAGSDM
     ILTNSFGASP YKLKRYGLDD RTYEINKTAA EISREAAGDD HFVLGSIGPT GAILMMGDIS
     EEELFNGFAI QAKALADGGA DAICVETMSD IAEAVSAVKA AKSACDLPVV CTFTFEKTVN
     NDYRTMMGVT PAQMAVELKN AGASVIGSNC GNGFDQMIEI VKEIRSVEKE LPVLVHANAG
     KPVFQEGKTV YLETPDSMAH KLNLLIESGA NIIGGCCGTT PRHIEAFVNT IKK
//
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