(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZJZ7_PSEAB

ID   A0A0H2ZJZ7_PSEAB        Unreviewed;       168 AA.
AC   A0A0H2ZJZ7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
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:ABJ15314.1};
GN   OrderedLocusNames=PA14_04580 {ECO:0000313|EMBL:ABJ15314.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15314.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15314.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15314.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15314.1; -; Genomic_DNA.
DR   RefSeq; WP_003084430.1; NC_008463.1.
DR   SMR; A0A0H2ZJZ7; -.
DR   EnsemblBacteria; ABJ15314; ABJ15314; PA14_04580.
DR   KEGG; pau:PA14_04580; -.
DR   KO; K00287; -.
DR   OMA; RDNQLPW; -.
DR   BioCyc; PAER208963:G1G74-382-MONOMER; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000000653; 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; -; 1.
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; A0A0H2ZJZ7.
DR   SWISS-2DPAGE; A0A0H2ZJZ7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   NADP {ECO:0000256|PIRNR:PIRNR000194};
KW   One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000194}.
FT   DOMAIN        4    167       DHFR. {ECO:0000259|PROSITE:PS51330}.
SQ   SEQUENCE   168 AA;  18203 MW;  13C1E9741A162409 CRC64;
     MARPLAMIAA LGENRAIGID NRLPWRLPAD LKHFKAMTLG KPVIMGRKTW DSLGRPLPGR
     LNLVVSRQAG LALEGAEVFA SLDAALARAE AWAQAEDADE LMLIGGAQLY AEALPRAARL
     YLTRVGLAPE GDAFFPEIDG AAWRLASSIE HAAADDAPAY AFEVWERR
//

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