Reviewed, UniProtKB/Swiss-Prot P04174 (DYR_NEIGO)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:

folA

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

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.
Miscellaneous	Strain T47/F62 is trimethoprim resistant by overproduction of DHFR. 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 One-carbon metabolism Trimethoprim resistance
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 response to antibiotic 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		PRO_0000186401
Regions
	Domain	3 – 161	159	DHFR

Sequences

	Sequence		Length	Mass (Da)
	P04174-1 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: A23BA94E6764E564	FASTA	162	17,731
	10 20 30 40 50 60 MLKITIIAAC AENLCIGAGN AMPWHIPEDF AFFKVYTLGK PVIMGRKTWE SLPVKPLPGR 70 80 90 100 110 120 RNIVISRQAD YCAAGAETVA SLEVALALCA GAEEAVIMGG AQIYGQAMPL ATDLRITEVD 130 140 150 160 LSVEGDAFFP EIDRTHWREA ERTERRVSSK GVAYTFVHYL GK

References

[1]	"Characterization and amino acid sequence of Neisseria gonorrhoeae dihydrofolate reductase." Baccanari D.P., Tansik R.L., Paterson S.J., Stone D. J. Biol. Chem. 259:12291-12298(1984) [PubMed: 6434541] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: T47/F62.

Cross-references

Sequence databases
PIR	RDNHD. A00393.
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. 588.
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_NEIGO

Accession

Primary (citable) accession number: P04174

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	March 20, 1987
Last modified:	June 16, 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)