(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}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
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
//
If you have problems or comments...
Back to PBIL home page