(data stored in ACNUC7421 zone)

SWISSPROT: Q8XA18_ECO57

ID   Q8XA18_ECO57            Unreviewed;       196 AA.
AC   Q8XA18; Q7AHS8;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 2.
DT   10-APR-2019, entry version 128.
DE   SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:BAB33474.2};
GN   Name=folA {ECO:0000313|EMBL:BAB33474.2};
GN   ORFNames=ECs_0051 {ECO:0000313|EMBL:BAB33474.2};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33474.2, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33474.2, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
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.G., 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).
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000256|RuleBase:RU004474}.
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DR   EMBL; BA000007; BAB33474.2; -; Genomic_DNA.
DR   RefSeq; NP_308078.1; NC_002695.1.
DR   STRING; 155864.EDL933_0049; -.
DR   EnsemblBacteria; AAG54351; AAG54351; Z0055.
DR   EnsemblBacteria; BAB33474; BAB33474; BAB33474.
DR   GeneID; 913450; -.
DR   KEGG; ecs:ECs0051; -.
DR   PATRIC; fig|386585.9.peg.150; -.
DR   eggNOG; ENOG4108YYV; Bacteria.
DR   eggNOG; COG0262; LUCA.
DR   KO; K00287; -.
DR   BioCyc; ECOO157:Z0055-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
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; Q8XA18.
DR   SWISS-2DPAGE; Q8XA18.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
SQ   SEQUENCE   196 AA;  22270 MW;  0B0CC79319E566FC CRC64;
     MDSPAEYKIF LNIILAPVDD GLRFTYSGDN FFYREISMIS LIAALAVDRV IGMENAMPWN
     LPADLAWFKR NTLNKPVIMG RHTRESIGRP LPGRKNIILS SQPGTDDRVT WVKSVDEAIA
     ACGDVPEIMV IGGGRVYEQF LPKAQKLYLT HIDAEVEGDT HFPDYEPDDW ESVFSEFHDA
     DAQNSHSYCF EILERR
//

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