Reviewed, UniProtKB/Swiss-Prot Q8NWQ9 (DYR_STAAW)

Names and origin

Protein names

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

Gene names

Name:	folA
Ordered Locus Names:	MW1316

Organism

Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]

Taxonomic identifier

196620 [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	Inferred from homology.

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	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	Complete proteome
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 By similarity
	Chain	2 – 159	158	Dihydrofolate reductase		PRO_0000186412
Regions
	Domain	2 – 157	156	DHFR

Sequences

	Sequence		Length	Mass (Da)
	Q8NWQ9-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 321B48938DC9E7A9	FASTA	159	18,233
	10 20 30 40 50 60 MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES IGKPLPNRRN 70 80 90 100 110 120 VVLTSDTSFN VVGVDVIHSI EDIYQLPGHV FIFGGQILFE EMIDKVDDMY ITVIEGKFRG 130 140 150 DTFFPPYTFE DWEVASSVEG KLDEKNTIPH TFLHLIRKK

References

[1]

"Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000033 Genomic DNA. Translation: BAB95181.1.
RefSeq	NP_646133.1.
3D structure databases
HSSP	HSSP built from PDB template 1DHI based on UniProtKB P00379.
ModBase	Search...
Genome annotation databases
GeneID	1003428.
GenomeReviews	Gene locus MW1316 in contig BA000033_GR.
KEGG	sam:MW1316.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8NWQ9.
OMA	Q8NWQ9. HANAMYL.
Enzyme and pathway databases
BioCyc	SAUR196620:MW1316-MON.
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...

Entry information

Entry name

DYR_STAAW

Accession

Primary (citable) accession number: Q8NWQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 39 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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