Reviewed, UniProtKB/Swiss-Prot Q9K168 (DYR_NEIMB)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:	folA
Ordered Locus Names:	NMB0308

Organism

Neisseria meningitidis serogroup B [Complete proteome] [HAMAP]

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	162 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.
Sequence similarities	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
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
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_0000186403
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)
	Q9K168-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B5EBB53CEABB8F62	FASTA	162	17,752
	10 20 30 40 50 60 MLKITLIAAC AENLCIGAGN AMPWHIPEDF AFFKAYTLGK PVIMGRKTWE SLPVKPLPGR 70 80 90 100 110 120 RNIVISRQAD YCAAGAETAA SLEAALALCA GAEEAVIMGG AQIYGQAMPL ATDLRITEVD 130 140 150 160 LSVEGDAFFP AIDRTHWKEA ERTERRVSSK GTRYAFVHYL RY

References

[1]

"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF40754.1.
PIR	G81214.
RefSeq	NP_273358.1.
3D structure databases
SMR	Q9K168. Positions 4-161.
ModBase	Search...
Genome annotation databases
GeneID	902424.
GenomeReviews	Gene locus NMB0308 in contig AE002098_GR.
KEGG	nme:NMB0308.
NMPDR	fig|122586.1.peg.292.
TIGR	NMB0308.
Phylogenomic databases
HOGENOM	HBG665708.
OMA	IRRTIIA.
Enzyme and pathway databases
BioCyc	NMEN122586:NMB_0308-MONOMER.
BRENDA	1.5.1.3. 293828.
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

DYR_NEIMB

Accession

Primary (citable) accession number: Q9K168

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 54 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)