Reviewed, UniProtKB/Swiss-Prot P12833 (DYR3_SALTY)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase type 3
    EC=1.5.1.3
Alternative name(s):
    Dihydrofolate reductase type III

Gene names

Name:

dhfrIII

Encoded on

Plasmid pAZ1

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	162 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.
Subunit structure	Monomer.
Miscellaneous	The plasmid pAZ1 determines trimethoprim and sulphonamide resistance. 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	Direct protein sequencing 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 – 162	162	Dihydrofolate reductase type 3		PRO_0000186421
Regions
	Domain	2 – 160	159	DHFR
Experimental info
	Sequence conflict	8	1	A → S AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P12833-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 199343AE8675FDED	FASTA	162	18,033
	10 20 30 40 50 60 MLISLIAALA HNNLIGKDNL IPWHLPADLR HFKAVTLGKP VVMGRRTFES IGRPLPGRRN 70 80 90 100 110 120 VVVSRNPQWQ AEGVEVAPSL DAALALLTDC EEAMIIGGGQ LYAEALPRAD RLYLTYIDAQ 130 140 150 160 LNGDTHFPDY LSLGWQELER STHPADDKNS YACEFVTLSR QR

References

[1]	"Characterization of plasmid pAZ1 and the type III dihydrofolate reductase gene." Fling M.E., Kopf J., Richards C. Plasmid 19:30-38(1988) [PubMed: 2840679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of an R-plasmid dihydrofolate reductase with a monomeric structure." Joyner S.S., Fling M.E., Stone D., Baccanari D.P. J. Biol. Chem. 259:5851-5856(1984) [PubMed: 6371010] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03306 Genomic DNA. Translation: AAA25550.1.
PIR	B22241. RDEBDT. JT0266.
3D structure databases
HSSP	HSSP built from PDB template 1DHI based on UniProtKB P00379.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 2.
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

DYR3_SALTY

Accession

Primary (citable) accession number: P12833

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 60 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)