ID   G7M5N2_9CLOT            Unreviewed;       593 AA.
AC   G7M5N2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHJ00147.1};
GN   ORFNames=CDLVIII_3589 {ECO:0000313|EMBL:EHJ00147.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ00147.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHJ00147.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ00147.1,
RC   ECO:0000313|Proteomes:UP000005106};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-e00613(2013).
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; CM001240; EHJ00147.1; -; Genomic_DNA.
DR   RefSeq; WP_009170807.1; NZ_CM001240.1.
DR   AlphaFoldDB; G7M5N2; -.
DR   STRING; 641107.CDLVIII_3589; -.
DR   eggNOG; COG0646; Bacteria.
DR   eggNOG; COG0685; Bacteria.
DR   HOGENOM; CLU_453272_0_0_9; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000005106; Chromosome.
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:UP000005106};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          1..281
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   593 AA;  66675 MW;  8068A273F244DA30 CRC64;
     MIKDYLQNNI LIFDGAMGTY YSELTGNDIS YCEFANLDDG DTIKKIHKEY INAGAKLIRT
     NTFSANTHDL GVSYETLKNI IKCGIDIAKE VTRNTSVFIG ASIGPIKEDN IDESQEDILK
     EYKYIVDCFL DNNINIFVFE TFSNYNYLKE ISEYIKGKDS KSFILTQFAV KPDGFTRDGI
     SASKLIKKVK EIKTIDSYGF NCGSGPTHVA EFIRTIDIEN DIVSAIPNAG YPEIIHERTV
     YPNNPVYFAN KVNAMTTLGV SIIGGCCGTN PNYIKELVSL IKNNSNEINS YSKKEEIKEY
     KEKTENAFKN KLDKNEFTIA IELSAPINTD ISKLMAGAKI CKENNIDLVT IPDSPMSKVR
     ADPTIIASKI KREIGIEVMP HICCRDRNTN AIRSSLIGSH IENIRNILAI TGDPISDANK
     IETKSVFNLN SFRLMKLIND MNEDLFKEDN IYIGGALNLN VLNKDVEFNR MLKKIDNGAK
     FFLTQPIYED DAIEFLSKIK AKTNVKILAG LLPIVSYRNA VFLNNELPGV KIPERYMKMF
     SENMSKEEAQ EIGVKIAVEI GNKLKGVSDG LYFITPFNRV NMLIDIVKQL QLS
//