Reviewed, UniProtKB/Swiss-Prot P11731 (DYR5_ECOLX)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase type 5
    EC=1.5.1.3
Alternative name(s):
    Dihydrofolate reductase type V

Gene names

Name:

dhfrV

Encoded on

Plasmid pLMO20

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Confers trimethoprim resistance.
Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.
Subunit structure	Homodimer.
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	Antibiotic resistance Methotrexate resistance One-carbon metabolism Trimethoprim resistance
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Plasmid
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 response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW response to methotrexate 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 – 157	157	Dihydrofolate reductase type 5		PRO_0000186422
Regions
	Domain	2 – 156	155	DHFR

Sequences

	Sequence		Length	Mass (Da)
	P11731-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 04B968163A25EFF4	FASTA	157	17,531
	10 20 30 40 50 60 MKVSLMAAKA KNGVIGCGPH IPWSAKGEQL LFKALTYNQW LLVGRKTFES MGALPNRKYA 70 80 90 100 110 120 VVTRSAWTAD NDNVIVFPSI EEAMYGLAEL TDHVIVSGGG EIYRETLPMA STLHISTIDI 130 140 150 EPEGDVFFPN IPNTFEVVFE QHFSSNINYC YQIWQKG

References

[1]

"Site-specific recombination promotes linkage between trimethoprim- and sulfonamide resistance genes. Sequence characterization of dhfrV and sulI and a recombination active locus of Tn21." Sundstroem L., Radstroem P., Swedberg G., Skoeld O. Mol. Gen. Genet. 213:191-201(1988) [PubMed: 3054482] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X12868 Genomic DNA. Translation: CAA31356.1.
PIR	S04810.
3D structure databases
HSSP	HSSP built from PDB template 1DRA based on UniProtKB P00379.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 246.
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

DYR5_ECOLX

Accession

Primary (citable) accession number: P11731

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 53 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)