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Database: UniProt
Entry: D6Z0B2_DESAT
LinkDB: D6Z0B2_DESAT
Original site: D6Z0B2_DESAT 
ID   D6Z0B2_DESAT            Unreviewed;       631 AA.
AC   D6Z0B2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADH87145.1};
GN   OrderedLocusNames=DaAHT2_2481 {ECO:0000313|EMBL:ADH87145.1};
OS   Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH87145.1, ECO:0000313|Proteomes:UP000001508};
RN   [1] {ECO:0000313|Proteomes:UP000001508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC   {ECO:0000313|Proteomes:UP000001508};
RG   US DOE Joint Genome Institute;
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA   Woyke T.;
RT   "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL   Submitted (FEB-2010) 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; CP001940; ADH87145.1; -; Genomic_DNA.
DR   RefSeq; WP_013164655.1; NC_014216.1.
DR   AlphaFoldDB; D6Z0B2; -.
DR   STRING; 589865.DaAHT2_2481; -.
DR   KEGG; dak:DaAHT2_2481; -.
DR   eggNOG; COG0646; Bacteria.
DR   eggNOG; COG0685; Bacteria.
DR   HOGENOM; CLU_453272_0_0_7; -.
DR   InParanoid; D6Z0B2; -.
DR   OrthoDB; 9803687at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001508; 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:UP000001508};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          5..294
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   631 AA;  67799 MW;  36408261AC787161 CRC64;
     MSANKPDFLE YIRERVLLAD GALGSYLYAK GIELGKNIER LNLADPDLVY SVHEEYIRAG
     SRLIETNTFG ANRLKLENAG LEDKARQINL AGAELAVRAG SGEVYVAGSV GPSGADFPLG
     ETEGPEREAV EAAFKEQIEA LLEGGVDLLI LETFSHLDEL LLALKVARRL AGKMPIVANM
     VYPKQGCTAA GLDALECGRA ALAAGADVVG SNCGRGARAM LTAMERLAAL GEEVPLAAFP
     NAGFPEIVNH RLIYPAEPPY MAQLVREMVK TGARLVGGCC GTTPAHIQEF GKHLRLKRRP
     LTQVASDKQA TGPDSQAPTA AKAGSLLKRL PTDKLPVLVE VDPPTHLDIS GVLGGAKELA
     AAGADAITLG ENPLAVLRAD NISLAHKIRS EVGIATVAHV TCRDRNALGL QSQIMGAHLL
     EIDSILAVTG DPATTGDQPA ATGVFDVQSF GLIRMLNQFN QGRNPAGKAM KGQCDFSIGA
     AFSYRPNNPD LQIRRLERKA ALGAVYAMTQ PFFSAGAVED MLERTRHLEM LIFPGIFPLI
     SARNAEFLHH EVPGINIPED LRRKLGRYEA VEDQRRVADE FTRELIAEIC PIIDGLYLIS
     PLNKWEVTAE LTREVRQAGW KGSGRLAALV Q
//
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