Reviewed, UniProtKB/Swiss-Prot Q59408 (DYR13_ECOLX)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase type A13
    EC=1.5.1.3
Alternative name(s):
    Dihydrofolate reductase type XIII
      Short name=DHFRXIII

Gene names

Name:	dfrA13
Synonyms:	dfr13

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Subunit structure	Homodimer By similarity.
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
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 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 – 165	165	Dihydrofolate reductase type A13		PRO_0000186429
Regions
	Domain	7 – 162	156	DHFR

Sequences

	Sequence		Length	Mass (Da)
	Q59408-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 656E9E214DDFDA9D	FASTA	165	17,925
	10 20 30 40 50 60 MNPESVRIYL VAAMGANRVI GNGPDIPWKI PGEQKIFRRL TESKVVVMGR KTFESIGKPL 70 80 90 100 110 120 PNRHTVVLSR QAGYSAPGCA VVSTLSHVSP STAEHGKELY VARGAEVYAL ALPHANGVFL 130 140 150 160 SEVHQTFEGD AFFPVLNAAE FEVVSSETIQ GTITYTHSVY ARRNG

References

[1]

"New gene cassettes for trimethoprim resistance, dfr13, and Streptomycin-spectinomycin resistance, aadA4, inserted on a class 1 integron." Adrian P.V., Thomson C.J., Klugman K.P., Amyes S.G. Antimicrob. Agents Chemother. 44:355-361(2000) [PubMed: 10639362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: RA33.2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z50802 Genomic DNA. Translation: CAA90683.1.
PIR	S60665.
3D structure databases
HSSP	HSSP built from PDB template 1DF7 based on UniProtKB O33305.
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

DYR13_ECOLX

Accession

Primary (citable) accession number: Q59408

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	September 22, 2009
This is version 49 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)