(data stored in ACNUC7421 zone)

SWISSPROT: B7UI94_ECO27

ID   B7UI94_ECO27            Unreviewed;       159 AA.
AC   B7UI94;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
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:CAS07597.1};
GN   OrderedLocusNames=E2348C_0049 {ECO:0000313|EMBL:CAS07597.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07597.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07597.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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}.
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; FM180568; CAS07597.1; -; Genomic_DNA.
DR   RefSeq; WP_000624375.1; NC_011601.1.
DR   SMR; B7UI94; -.
DR   EnsemblBacteria; CAS07597; CAS07597; E2348C_0049.
DR   KEGG; ecg:E2348C_0049; -.
DR   HOGENOM; HOG000040233; -.
DR   KO; K00287; -.
DR   OMA; RDNQLPW; -.
DR   BioCyc; ECOL574521:E2348C_RS00255-MONOMER; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000008205; 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; B7UI94.
DR   SWISS-2DPAGE; B7UI94.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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
//

If you have problems or comments...

PBIL Back to PBIL home page