Reviewed, UniProtKB/Swiss-Prot P78218 (DYR15_ECOLX)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase type 15
    EC=1.5.1.3
Alternative name(s):
    Dihydrofolate reductase type XV

Gene names

Name:	dhfrXV
Synonyms:	dfrXV

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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.
Subunit structure	Homodimer By similarity.
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 – 157	157	Dihydrofolate reductase type 15		PRO_0000186430
Regions
	Domain	2 – 156	155	DHFR

Sequences

	Sequence		Length	Mass (Da)
	P78218-1 [UniParc]. Last modified July 1, 1997. Version 2. Checksum: FF08B9F36650A83F	FASTA	157	17,503
	10 20 30 40 50 60 MKLSLMAAIS KNGVIGNGPD IPWSAKGEQL LFKAITYNQW LLVGRKTFES MGALPNRKYA 70 80 90 100 110 120 VVTRSSFTSS DENVLVFPSI DEALNHLKTI TDHVIVSGGG EIYKSLIDKV DTLHISTIDI 130 140 150 EPEGDVYFPE IPSSFRPVFS QDFVSNINYS YQIWQKG

References

[1]	Adrian P.V., du Plessis M., Klugman K.P., Amyes S.G. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: UI14.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z83311 Genomic DNA. Translation: CAB05887.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 246.
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...

Entry information

Entry name

DYR15_ECOLX

Accession

Primary (citable) accession number: P78218

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	February 9, 2010
This is version 50 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)