Reviewed, UniProtKB/Swiss-Prot P00380 (DYR_ENTFC)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:

folA

Organism

Enterococcus faecium (Streptococcus faecium)

Taxonomic identifier

1352 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	167 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	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	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
	Chain	1 – 167	167	Dihydrofolate reductase		PRO_0000186390
Regions
	Domain	1 – 162	162	DHFR

Sequences

	Sequence		Length	Mass (Da)
	P00380-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: E00C2CF3BC420585	FASTA	167	19,583
	10 20 30 40 50 60 MFISMWAQDK NGLIGKDGLL PWRLPNDMRF FREHTMDKIL VMGRKTYEGM GKLSLPYRHI 70 80 90 100 110 120 IVLTTQKDFK VEKNAEVLHS IDELLAYAKD IPEDIYVSGG SRIFQALLPE TKIIWRTLID 130 140 150 160 AEFEGDTFIG EIDFTSFELV EEHEGIVNQE NQYPHRFQKW QKMSKVV

References

[1]

"The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the protein." Peterson D.L., Gleisner J.M., Blakley R.L. J. Biol. Chem. 250:4945-4954(1975) [PubMed: 1097435] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: A / var. Durans.

Cross-references

Sequence databases
PIR	RDSODF. A00392.
3D structure databases
HSSP	HSSP built from PDB template 1VDR based on UniProtKB P15093.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 702.
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_ENTFC

Accession

Primary (citable) accession number: P00380

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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