ID L0G0X5_ECHVK Unreviewed; 347 AA.
AC L0G0X5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:AGA79854.1};
GN OrderedLocusNames=Echvi_3639 {ECO:0000313|EMBL:AGA79854.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA79854.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-2012) 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; CP003346; AGA79854.1; -; Genomic_DNA.
DR RefSeq; WP_015267399.1; NC_019904.1.
DR AlphaFoldDB; L0G0X5; -.
DR STRING; 926556.Echvi_3639; -.
DR KEGG; evi:Echvi_3639; -.
DR PATRIC; fig|926556.3.peg.3831; -.
DR eggNOG; COG0646; Bacteria.
DR HOGENOM; CLU_004914_3_0_10; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000010796; 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:UP000010796};
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..332
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 347 AA; 38025 MW; 2CDC732526385F18 CRC64;
MNTRTDILLQ QVDKKILILD GAMGTMIQRY TLEEEDFRTP ELANHPKALK GNNDLLSLSR
PKIIRDIHDT YLEAGADIIE TNTFSSTSIA QEDYDLSQLA YELNVESARI AREAALSYSE
KTPDQPRFVA GAIGPTNRTA SISPDVNDPG YRAINFDQLS EAYAEQVRGL LDGGVDILLV
ETIFDTLNAK AALFAIQEVF EEKGLPLSPE EGGIPIMISG TITDASGRTL SGQTTEAFLI
SVSHVPLMSI GLNCALGAKE LRPYLKVLAE NAPFYVSAYP NAGLPNEFGQ YDQTAQEMAD
QVEEFLKDGL INILGGCCGT TPEHIRVIGD VSKKYKPRKL AYTLEEE
//
