P04174 (DYR_NEIGO) Reviewed, UniProtKB/Swiss-Prot

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.
Protein existence	Evidence at protein level

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.
Miscellaneous	Strain T47/F62 is trimethoprim resistant by overproduction of DHFR.
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 metabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP 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
	Nucleotide binding	8 – 9	2	NADP By similarity
	Nucleotide binding	16 – 21	6	NADP By similarity
	Nucleotide binding	45 – 48	4	NADP By similarity
	Nucleotide binding	65 – 68	4	NADP By similarity
	Nucleotide binding	98 – 103	6	NADP By similarity
	Region	7 – 9	3	Substrate binding By similarity
Sites
	Binding site	29	1	Substrate By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	117	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P04174 [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	RDNHD. A00393.
3D structure databases
ProteinModelPortal	P04174.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR012259. DHFR. IPR024072. DHFR-like_dom. IPR017925. DHFR_CS. IPR001796. DHFR_dom. [Graphical view]
Gene3D	G3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit.
PANTHER	PTHR11549:SF1. DHFR. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. [Graphical view]
PIRSF	PIRSF000194. DHFR. 1 hit.
PRINTS	PR00070. DHFR.
SUPFAM	SSF53597. SSF53597. 1 hit.
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:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program