(data stored in SCRATCH zone)

SWISSPROT: Q8XA18_ECO57

ID   Q8XA18_ECO57            Unreviewed;       159 AA.
AC   Q8XA18; Q7AHS8;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 117.
DE   RecName: Full=Dihydrofolate reductase {ECO:0000256|PIRNR:PIRNR000194};
DE            EC=1.5.1.3 {ECO:0000256|PIRNR:PIRNR000194};
GN   OrderedLocusNames=ECs0051 {ECO:0000313|EMBL:BAB33474.1}, Z0055
GN   {ECO:0000313|EMBL:AAG54351.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB33474.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB33474.1};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [2] {ECO:0000313|EMBL:AAG54351.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54351.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G.III., Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
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: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
CC       dihydrofolate + NADPH. {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; AE005174; AAG54351.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33474.1; -; Genomic_DNA.
DR   PIR; C85486; C85486.
DR   PIR; C90635; C90635.
DR   RefSeq; NP_308078.1; NC_002695.1.
DR   RefSeq; WP_000624372.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; Q8XA18; -.
DR   STRING; 155864.Z0055; -.
DR   EnsemblBacteria; AAG54351; AAG54351; Z0055.
DR   EnsemblBacteria; BAB33474; BAB33474; BAB33474.
DR   GeneID; 913450; -.
DR   KEGG; ece:Z0055; -.
DR   KEGG; ecs:ECs0051; -.
DR   PATRIC; fig|386585.9.peg.150; -.
DR   eggNOG; ENOG4108YYV; Bacteria.
DR   eggNOG; COG0262; LUCA.
DR   HOGENOM; HOG000040233; -.
DR   KO; K00287; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:0009165; P:nucleotide 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; -; 1.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR024072; DHFR-like_dom.
DR   InterPro; IPR017925; DHFR_CS.
DR   InterPro; IPR001796; DHFR_dom.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PIRSF; PIRSF000194; DHFR; 1.
DR   PRINTS; PR00070; DHFR.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XA18.
DR   SWISS-2DPAGE; Q8XA18.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
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 (dihydrofolate reductase).
FT                                {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;  17969 MW;  99D8A6A0C984EE0F CRC64;
     MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTRESI GRPLPGRKNI
     ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE
     GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR
//

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