Reviewed, UniProtKB/Swiss-Prot P0A017 (DYR_STAAU)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
      Short name=DHFR
    EC=1.5.1.3

Gene names

Name:

folA

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.
Miscellaneous	There are two dhfR isozymes in S.aureus, this one is chromosomal and is sensitive to trimethoprim. The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
Sequence similarities	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 159	158	Dihydrofolate reductase		PRO_0000186411
Regions
	Domain	2 – 157	156	DHFR

Sequences

	Sequence		Length	Mass (Da)
	P0A017-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 811898409FEAFAAB	FASTA	159	18,251
	10 20 30 40 50 60 MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES IGKPLPNRRN 70 80 90 100 110 120 VVLTSDTSFN VEGVDVIHSI EDIYQLPGHV FIFGGQTLFE EMIDKVDDMY ITVIEGKFRG 130 140 150 DTFFPPYTFE DWEVASSVEG KLDEKNTIPH TFLHLIRKK

References

[1]	"Characterization of the gene for chromosomal trimethoprim-sensitive dihydrofolate reductase of Staphylococcus aureus ATCC 25923." Dale G.E., Then R.L., Stueber D. Antimicrob. Agents Chemother. 37:1400-1405(1993) [PubMed: 8363365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.
[2]	"N-terminal amino acid sequence of the chromosomal dihydrofolate reductase purified from trimethoprim-resistant Staphylococcus aureus." Hartman P.G., Stahli M., Kocher H.P., Then R.L. FEBS Lett. 242:157-160(1988) [PubMed: 3060373] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-36. Strain: 157/4696.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z16422 Genomic DNA. Translation: CAA78910.1.

PIR

S32014.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W9G	X-ray	1.95	A	1-159	[»]
2W9H	X-ray	1.48	A	1-159	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.5.1.3. 95.

Family and domain databases

InterPro

IPR012259. DHFR.
IPR001796. DHFR_reg.
IPR017925. Dihydrofolate_reductase_CS.
[Graphical view]

PANTHER

PTHR11549:SF1. DHFR. 1 hit.

Pfam

PF00186. DHFR_1. 1 hit.
[Graphical view]

PRINTS

PR00070. DHFR.

PROSITE

PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P0A017.

Entry information

Entry name

DYR_STAAU

Accession

Primary (citable) accession number: P0A017
Secondary accession number(s): P10167

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 27 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)