(data stored in ACNUC7421 zone)

SWISSPROT: C8W5Z9_DESAS

ID   C8W5Z9_DESAS            Unreviewed;       294 AA.
AC   C8W5Z9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE            EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862};
GN   OrderedLocusNames=Dtox_0534 {ECO:0000313|EMBL:ACV61454.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61454.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61454.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-
CC         5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH;
CC         Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.5.1.20; Evidence={ECO:0000256|RuleBase:RU003862};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003862};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|RuleBase:RU003862}.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase
CC       family. {ECO:0000256|RuleBase:RU003862}.
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DR   EMBL; CP001720; ACV61454.1; -; Genomic_DNA.
DR   RefSeq; WP_015756173.1; NC_013216.1.
DR   STRING; 485916.Dtox_0534; -.
DR   EnsemblBacteria; ACV61454; ACV61454; Dtox_0534.
DR   KEGG; dae:Dtox_0534; -.
DR   eggNOG; ENOG4105SYT; Bacteria.
DR   eggNOG; COG0685; LUCA.
DR   HOGENOM; HOG000246233; -.
DR   KO; K00297; -.
DR   OMA; FIRAETG; -.
DR   OrthoDB; 1425269at2; -.
DR   BioCyc; DACE485916:G1GFV-540-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00537; MTHFR; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003171; Mehydrof_redctse.
DR   InterPro; IPR004620; MTHF_reductase_bac.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51730; SSF51730; 1.
DR   TIGRFAMs; TIGR00676; fadh2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W5Z9.
DR   SWISS-2DPAGE; C8W5Z9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   FAD {ECO:0000256|RuleBase:RU003862};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003862};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003862,
KW   ECO:0000313|EMBL:ACV61454.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
SQ   SEQUENCE   294 AA;  32679 MW;  39C93E054A77E59F CRC64;
     MKLSEIFKTG KPTLSFEFFP ARNEKAAETF NQTIEDLVEL KPDFVSVTFG AGGSTKEGSY
     ELVKKLKKEK ELEVVAYLAA FALKKDEINA VLNSYQDLGI ENILALRGDP PKDADVTQVS
     AESFKYASEL AAFIHQNYSF CLGVAGYPEG HIEAPSLKKD IEYLKHKVDQ GVDFIIAQFF
     YDNVCFFDFR ERCQKSGINI PVLPGIMPVY SVKMMEMLAG SCGAKIPEKL RKGISELPEG
     DTKALVDFGI EYATGQCEEL LKEGARGLHF YTMDKSESTV GIVKGLRNRG FLTI
//

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