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DYR_STAAU
ID   DYR_STAAU               Reviewed;         159 AA.
AC   P0A017; P10167;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Dihydrofolate reductase;
DE            Short=DHFR;
DE            EC=1.5.1.3;
GN   Name=folA;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25923 / DSM 1104 / JCM 2413 / NBRC 14462 / NCIMB 12702 / NCTC
RC   12981 / Seattle 1945;
RX   PubMed=8363365; DOI=10.1128/aac.37.7.1400;
RA   Dale G.E., Then R.L., Stueber D.;
RT   "Characterization of the gene for chromosomal trimethoprim-sensitive
RT   dihydrofolate reductase of Staphylococcus aureus ATCC 25923.";
RL   Antimicrob. Agents Chemother. 37:1400-1405(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-36.
RC   STRAIN=157/4696;
RX   PubMed=3060373; DOI=10.1016/0014-5793(88)81006-8;
RA   Hartman P.G., Stahli M., Kocher H.P., Then R.L.;
RT   "N-terminal amino acid sequence of the chromosomal dihydrofolate reductase
RT   purified from trimethoprim-resistant Staphylococcus aureus.";
RL   FEBS Lett. 242:157-160(1988).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-159.
RX   PubMed=19622858; DOI=10.1107/s0907444909013936;
RA   Oefner C., Parisi S., Schulz H., Lociuro S., Dale G.E.;
RT   "Inhibitory properties and X-ray crystallographic study of the binding of
RT   AR-101, AR-102 and iclaprim in ternary complexes with NADPH and
RT   dihydrofolate reductase from Staphylococcus aureus.";
RL   Acta Crystallogr. D 65:751-757(2009).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH NADPH AND
RP   TRIMETHOPRIM.
RX   PubMed=19280600; DOI=10.1002/prot.22383;
RA   Heaslet H., Harris M., Fahnoe K., Sarver R., Putz H., Chang J.,
RA   Subramanyam C., Barreiro G., Miller J.R.;
RT   "Structural comparison of chromosomal and exogenous dihydrofolate reductase
RT   from Staphylococcus aureus in complex with the potent inhibitor
RT   trimethoprim.";
RL   Proteins 76:706-717(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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate +
CC         H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00660};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC   -!- MISCELLANEOUS: There are two DhfR isozymes in S.aureus, this one is
CC       chromosomal and is sensitive to trimethoprim.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; Z16422; CAA78910.1; -; Genomic_DNA.
DR   PIR; S32014; S32014.
DR   RefSeq; WP_000175746.1; NZ_WYDB01000002.1.
DR   PDB; 2W9G; X-ray; 1.95 A; A=1-159.
DR   PDB; 2W9H; X-ray; 1.48 A; A=1-159.
DR   PDB; 3FRA; X-ray; 2.35 A; X=2-159.
DR   PDB; 3FRB; X-ray; 2.00 A; X=2-159.
DR   PDB; 3FRD; X-ray; 2.10 A; X=2-159.
DR   PDB; 3FRE; X-ray; 2.20 A; X=2-159.
DR   PDB; 3FRF; X-ray; 2.20 A; X=2-159.
DR   PDB; 3FY8; X-ray; 2.20 A; X=2-159.
DR   PDB; 3FY9; X-ray; 2.25 A; X=2-159.
DR   PDB; 3FYV; X-ray; 2.20 A; X=2-159.
DR   PDB; 3FYW; X-ray; 2.10 A; X=2-159.
DR   PDB; 3I8A; X-ray; 2.41 A; X=2-158.
DR   PDB; 3LG4; X-ray; 3.15 A; A/B=1-158.
DR   PDB; 3M08; X-ray; 2.01 A; A=2-158.
DR   PDB; 3M09; X-ray; 2.01 A; A=2-158.
DR   PDB; 3SGY; X-ray; 2.60 A; A/B=2-158.
DR   PDB; 3SH2; X-ray; 3.00 A; A/B=2-158.
DR   PDB; 3SQY; X-ray; 1.50 A; X=1-159.
DR   PDB; 3SR5; X-ray; 1.68 A; X=2-159.
DR   PDB; 3SRQ; X-ray; 1.69 A; X=1-159.
DR   PDB; 3SRR; X-ray; 1.70 A; X=1-159.
DR   PDB; 3SRS; X-ray; 1.70 A; X=1-159.
DR   PDB; 3SRU; X-ray; 1.70 A; X=1-159.
DR   PDB; 3SRW; X-ray; 1.70 A; X=1-159.
DR   PDB; 4FGG; X-ray; 2.30 A; A=1-159.
DR   PDB; 4FGH; X-ray; 2.50 A; A=1-159.
DR   PDB; 4LAE; X-ray; 1.69 A; X=1-159.
DR   PDB; 4LAG; X-ray; 1.70 A; X=1-159.
DR   PDB; 4LAH; X-ray; 1.88 A; X=1-159.
DR   PDB; 4LEK; X-ray; 1.70 A; X=1-159.
DR   PDB; 4XE6; X-ray; 2.69 A; X=1-157.
DR   PDB; 4XEC; X-ray; 2.69 A; X=2-158.
DR   PDB; 5HF0; X-ray; 2.25 A; X=2-158.
DR   PDB; 5HF2; X-ray; 1.81 A; X=2-158.
DR   PDB; 5ISP; X-ray; 1.84 A; X=2-158.
DR   PDB; 5ISQ; X-ray; 1.90 A; X=2-158.
DR   PDB; 5IST; X-ray; 1.72 A; X=2-158.
DR   PDB; 5JG0; X-ray; 1.88 A; X=2-158.
DR   PDB; 6E4E; X-ray; 1.90 A; A=1-159.
DR   PDB; 6ND2; X-ray; 2.24 A; X=2-158.
DR   PDB; 6P9Z; X-ray; 1.86 A; X=2-158.
DR   PDB; 6PBO; X-ray; 1.65 A; X=2-158.
DR   PDB; 6PR6; X-ray; 2.01 A; A=1-159.
DR   PDB; 6PR7; X-ray; 2.01 A; A=1-159.
DR   PDB; 6PR8; X-ray; 2.01 A; A=2-159.
DR   PDB; 6PR9; X-ray; 2.01 A; A=2-159.
DR   PDB; 6PRA; X-ray; 2.01 A; A=1-159.
DR   PDB; 6PRB; X-ray; 2.00 A; A=2-159.
DR   PDB; 6PRD; X-ray; 2.01 A; A=2-159.
DR   PDB; 7T7Q; X-ray; 2.20 A; X=2-158.
DR   PDB; 7T7S; X-ray; 2.20 A; X=2-158.
DR   PDBsum; 2W9G; -.
DR   PDBsum; 2W9H; -.
DR   PDBsum; 3FRA; -.
DR   PDBsum; 3FRB; -.
DR   PDBsum; 3FRD; -.
DR   PDBsum; 3FRE; -.
DR   PDBsum; 3FRF; -.
DR   PDBsum; 3FY8; -.
DR   PDBsum; 3FY9; -.
DR   PDBsum; 3FYV; -.
DR   PDBsum; 3FYW; -.
DR   PDBsum; 3I8A; -.
DR   PDBsum; 3LG4; -.
DR   PDBsum; 3M08; -.
DR   PDBsum; 3M09; -.
DR   PDBsum; 3SGY; -.
DR   PDBsum; 3SH2; -.
DR   PDBsum; 3SQY; -.
DR   PDBsum; 3SR5; -.
DR   PDBsum; 3SRQ; -.
DR   PDBsum; 3SRR; -.
DR   PDBsum; 3SRS; -.
DR   PDBsum; 3SRU; -.
DR   PDBsum; 3SRW; -.
DR   PDBsum; 4FGG; -.
DR   PDBsum; 4FGH; -.
DR   PDBsum; 4LAE; -.
DR   PDBsum; 4LAG; -.
DR   PDBsum; 4LAH; -.
DR   PDBsum; 4LEK; -.
DR   PDBsum; 4XE6; -.
DR   PDBsum; 4XEC; -.
DR   PDBsum; 5HF0; -.
DR   PDBsum; 5HF2; -.
DR   PDBsum; 5ISP; -.
DR   PDBsum; 5ISQ; -.
DR   PDBsum; 5IST; -.
DR   PDBsum; 5JG0; -.
DR   PDBsum; 6E4E; -.
DR   PDBsum; 6ND2; -.
DR   PDBsum; 6P9Z; -.
DR   PDBsum; 6PBO; -.
DR   PDBsum; 6PR6; -.
DR   PDBsum; 6PR7; -.
DR   PDBsum; 6PR8; -.
DR   PDBsum; 6PR9; -.
DR   PDBsum; 6PRA; -.
DR   PDBsum; 6PRB; -.
DR   PDBsum; 6PRD; -.
DR   PDBsum; 7T7Q; -.
DR   PDBsum; 7T7S; -.
DR   AlphaFoldDB; P0A017; -.
DR   BMRB; P0A017; -.
DR   SMR; P0A017; -.
DR   BindingDB; P0A017; -.
DR   ChEMBL; CHEMBL1681620; -.
DR   DrugBank; DB07938; (S)-iclaprim.
DR   DrugBank; DB08234; 5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine.
DR   DrugBank; DB08741; 5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-2H-chromen-5-yl]methyl]pyrimidine-2,4-diamine.
DR   DrugCentral; P0A017; -.
DR   OMA; RDNQLPW; -.
DR   BRENDA; 1.5.1.3; 3352.
DR   UniPathway; UPA00077; UER00158.
DR   EvolutionaryTrace; P0A017; -.
DR   PRO; PR:P0A017; -.
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; PTHR48069; PTHR48069; 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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; NADP; One-carbon metabolism;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3060373"
FT   CHAIN           2..159
FT                   /note="Dihydrofolate reductase"
FT                   /id="PRO_0000186411"
FT   DOMAIN          2..157
FT                   /note="DHFR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT   BINDING         6..7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:19280600"
FT   BINDING         7..8
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19280600"
FT   BINDING         15..20
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19280600"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:19280600"
FT   BINDING         44..47
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19280600"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:19280600"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:19280600"
FT   BINDING         63..66
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19280600"
FT   BINDING         93..98
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19280600"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:19280600"
FT   BINDING         101
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19280600"
FT   BINDING         122
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19280600"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          14..17
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   HELIX           26..36
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   HELIX           45..51
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   HELIX           80..85
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   HELIX           96..102
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          132..139
FT                   /evidence="ECO:0007829|PDB:2W9H"
FT   STRAND          150..157
FT                   /evidence="ECO:0007829|PDB:2W9H"
SQ   SEQUENCE   159 AA;  18251 MW;  811898409FEAFAAB CRC64;
     MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES IGKPLPNRRN
     VVLTSDTSFN VEGVDVIHSI EDIYQLPGHV FIFGGQTLFE EMIDKVDDMY ITVIEGKFRG
     DTFFPPYTFE DWEVASSVEG KLDEKNTIPH TFLHLIRKK
 
 
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