Reviewed, UniProtKB/Swiss-Prot P99079 (DYR_STAAN)

Names and origin

Protein names

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

Gene names

Name:	folA
Ordered Locus Names:	SA1259

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [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)

Function	Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.
Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
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 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_0000186408
Regions
	Domain	2 – 157	156	DHFR
	Nucleotide binding	7 – 8	2	NADP By similarity
	Nucleotide binding	15 – 20	6	NADP By similarity
	Nucleotide binding	44 – 47	4	NADP By similarity
	Nucleotide binding	63 – 66	4	NADP By similarity
	Nucleotide binding	93 – 98	6	NADP By similarity
	Region	6 – 8	3	Substrate binding By similarity
Sites
	Binding site	28	1	Substrate By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99079-1 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB42519.1.
RefSeq	NP_374540.1.
3D structure databases
SMR	P99079. Positions 1-159.
ModBase	Search...
Protein-protein interaction databases
STRING	P99079.
2-D gel databases
SWISS-2DPAGE	P99079.
Genome annotation databases
GeneID	1124097.
GenomeReviews	Gene locus SA1259 in contig BA000018_GR.
KEGG	sau:SA1259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0262.
HOGENOM	HBG665708.
OMA	GLPWHLP.
ProtClustDB	CLSK885344.
Enzyme and pathway databases
BioCyc	SAUR158879:SA1259-MONOMER.
Family and domain databases
InterPro	IPR012259. DHFR. IPR017925. Dihydrofolate_reductase_CS. IPR001796. Dihydrofolate_reductase_dom. [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	P99079.

Entry information

Entry name

DYR_STAAN

Accession

Primary (citable) accession number: P99079
Secondary accession number(s): P10167

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	January 23, 2007
Last modified:	March 2, 2010
This is version 40 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)