(data stored in SCRATCH zone)

SWISSPROT: Q3Z5W1_SHISS

ID   Q3Z5W1_SHISS            Unreviewed;       159 AA.
AC   Q3Z5W1;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 86.
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:AAZ86851.1};
GN   OrderedLocusNames=SSON_0056 {ECO:0000313|EMBL:AAZ86851.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ86851.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ86851.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ86851.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ86851.1; -; Genomic_DNA.
DR   SMR; Q3Z5W1; -.
DR   EnsemblBacteria; AAZ86851; AAZ86851; SSON_0056.
DR   KEGG; ssn:SSON_0056; -.
DR   HOGENOM; HOG000040233; -.
DR   KO; K00287; -.
DR   OMA; RDNQLPW; -.
DR   BioCyc; SSON300269:G1GL2-65-MONOMER; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000002529; 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; Q3Z5W1.
DR   SWISS-2DPAGE; Q3Z5W1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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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