(data stored in ACNUC10821 zone)

SWISSPROT: C8U1C1_ECO10

ID   C8U1C1_ECO10            Unreviewed;       159 AA.
AC   C8U1C1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Dihydrofolate reductase {ECO:0000256|PIRNR:PIRNR000194};
DE            EC=1.5.1.3 {ECO:0000256|PIRNR:PIRNR000194};
GN   Name=folA {ECO:0000313|EMBL:BAI28929.1};
GN   OrderedLocusNames=ECO103_0051 {ECO:0000313|EMBL:BAI28929.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28929.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28929.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential
CC       reaction for de novo glycine and purine synthesis, and for DNA
CC       precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
CC         dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000194};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR000194}.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000256|PIRNR:PIRNR000194, ECO:0000256|RuleBase:RU004474}.
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DR   EMBL; AP010958; BAI28929.1; -; Genomic_DNA.
DR   RefSeq; WP_000624375.1; NC_013353.1.
DR   SMR; C8U1C1; -.
DR   EnsemblBacteria; BAI28929; BAI28929; ECO103_0051.
DR   KEGG; eoh:ECO103_0051; -.
DR   HOGENOM; HOG000040233; -.
DR   KO; K00287; -.
DR   OMA; RDNQLPW; -.
DR   BioCyc; ECOL585395:ECO103_RS00260-MONOMER; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00209; DHFR; 1.
DR   Gene3D; 3.40.430.10; -; 2.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR017925; DHFR_CS.
DR   InterPro; IPR001796; DHFR_dom.
DR   PANTHER; PTHR22778:SF16; PTHR22778:SF16; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PIRSF; PIRSF000194; DHFR; 1.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1C1.
DR   SWISS-2DPAGE; C8U1C1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   NADP {ECO:0000256|PIRNR:PIRNR000194};
KW   One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000194}.
FT   DOMAIN        1    158       DHFR. {ECO:0000259|PROSITE:PS51330}.
FT   NP_BIND      13     19       NADP. {ECO:0000256|PIRSR:PIRSR000194-1}.
FT   NP_BIND      45     46       NADP. {ECO:0000256|PIRSR:PIRSR000194-1}.
FT   NP_BIND      63     64       NADP. {ECO:0000256|PIRSR:PIRSR000194-1}.
FT   NP_BIND      95    102       NADP. {ECO:0000256|PIRSR:PIRSR000194-1}.
FT   BINDING       5      5       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000194-1}.
FT   BINDING       7      7       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000194-
FT                                1}.
FT   BINDING      27     27       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000194-1}.
FT   BINDING      52     52       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000194-1}.
FT   BINDING      57     57       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000194-1}.
FT   BINDING      76     76       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000194-1}.
FT   BINDING     113    113       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000194-1}.
SQ   SEQUENCE   159 AA;  17999 MW;  6A03CDCD7F5F8562 CRC64;
     MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI GRPLPGRKNI
     ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE
     GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR
//

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