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Database: UniProt
Entry: A0A1I6M874_9BACT
LinkDB: A0A1I6M874_9BACT
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ID   A0A1I6M874_9BACT        Unreviewed;       640 AA.
AC   A0A1I6M874;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:SFS11916.1};
GN   ORFNames=SAMN05421771_2033 {ECO:0000313|EMBL:SFS11916.1};
OS   Granulicella pectinivorans.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=474950 {ECO:0000313|EMBL:SFS11916.1, ECO:0000313|Proteomes:UP000199024};
RN   [1] {ECO:0000313|EMBL:SFS11916.1, ECO:0000313|Proteomes:UP000199024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21001 {ECO:0000313|EMBL:SFS11916.1,
RC   ECO:0000313|Proteomes:UP000199024};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777}.
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DR   EMBL; FOZL01000001; SFS11916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6M874; -.
DR   STRING; 474950.SAMN05421771_2033; -.
DR   OrthoDB; 9803687at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000199024; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006555; P:methionine metabolic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00537; MTHFR; 1.
DR   Gene3D; 3.20.20.220; -; 1.
DR   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   PANTHER; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR   PANTHER; PTHR11103; SLR1189 PROTEIN; 1.
DR   Pfam; PF02219; MTHFR; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          17..314
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   640 AA;  68768 MW;  5E0A0F78EEB9067C CRC64;
     MTGTAVETTN KALDELFRAP DGETARRTVL CDGAMGTMLY DRGVFINRSY DELNISQPEL
     VRAVHAEYLQ AGAEIIETNT FGANAFRLER YGLRDSVRKL NLAGMRLARE CVTQMREKQA
     SEAYVAGALG PLGVRLVPHG PVSREDARET FREQVRALAE GGPGVGADLF VIETMMSMAE
     TEEAMAAVKE EAPGLKLIVM LTVDDKGNSL DGTSAEEATR LMQLWGADAI GCNCSDGPQT
     VLDVIQRMRA VTKLPLAAMP NAGIPREVDG RHMYMTTPEY MAGFARKAVK AGATFLGGCC
     GTTPAHIRAM RHALRALGAM QEGVHAEAAV VIESTVKPPA LKERSKVGAM IAAGDWITMV
     EIVPPKGIDC TKEIEGARML YKLGVDVINV PDSPRASARM AAQSLCVQIQ QQVGIETIIH
     YTCRDRNVLS IQSDLIGASS IGLKNVLCLT GDPPKMGNYP DATAVFDVDA IGLTKIVRGL
     NHGLDIGNNP IGGSTGFAIA VAANPGVADL DFEVRRFEAK VEAGAEFCIT QPVFDLQVLE
     DFLRRIEGFR IPVIAGIWPL TSLKNAEFMK NDLKVRVPDQ IMTRMGKASG PDAARAEGLA
     IAREMLAEAR LLGHMMVRGV QVSAPFGKYK AAADVLGLEG
//
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