Reviewed, UniProtKB/Swiss-Prot P43791 (DYR_HAEIN)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:	folA
Synonyms:	folH
Ordered Locus Names:	HI0899

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	160 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.
Miscellaneous	Isolates R906, R1042, and R1047 are trimethoprim-resistant.
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	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 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 – 160	160	Dihydrofolate reductase		PRO_0000186391
Regions
	Domain	2 – 159	158	DHFR
	Nucleotide binding	14 – 20	7	NADP By similarity
	Nucleotide binding	46 – 47	2	NADP By similarity
	Nucleotide binding	64 – 65	2	NADP By similarity
	Nucleotide binding	96 – 103	8	NADP By similarity
Sites
	Binding site	6	1	Substrate; via carbonyl oxygen By similarity
	Binding site	8	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	28	1	Substrate By similarity
	Binding site	53	1	Substrate By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	114	1	Substrate By similarity
Natural variations
	Natural variant	13	1	N → S in strain: Isolate R1042 and Isolate R1047.
	Natural variant	21	1	M → I in strain: Isolate R1047.
	Natural variant	54	1	P → A in strain: Isolate R1047.
	Natural variant	56	1	P → A in strain: Isolate R906.
	Natural variant	67	1	L → P in strain: Isolate R1042.
	Natural variant	69	1	E → K in strain: Isolate R1042.
	Natural variant	74	1	I → V in strain: Isolate R1042.
	Natural variant	77	1	D → N in strain: Isolate R1042.
	Natural variant	79	1	F → L in strain: Isolate R1042.
	Natural variant	95	1	I → L in strain: Isolate R1047.
	Natural variant	135	1	E → K in strain: Isolate R1042.
	Natural variant	142	1	R → H in strain: Isolate R1042.
	Natural variant	154	1	F → S in strain: Isolate R1042.

Sequences

	Sequence		Length	Mass (Da)
	P43791-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 384A1D64092B8C4F	FASTA	160	18,913
	10 20 30 40 50 60 MTFSLIVATT LNNVIGKDNQ MPWHLPADLA WFRQNTTGKP VIMGRKTFES IGRPLPKRTN 70 80 90 100 110 120 IVLSRQLFEH EGVIWKDSFE SAVNFVRDFD EIMLIGGGEL FKQYLPKADK LYLTQIQTEL 130 140 150 160 DGDTFFPQLN WEEWEIEFDE YRKADEQNRY DCRFLILTRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	de Groot R. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate R1042, Isolate R1047 and Isolate R906.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22559.1. X84207 Genomic DNA. Translation: CAA58993.1. X84205 Genomic DNA. Translation: CAA58991.1. X84206 Genomic DNA. Translation: CAA58992.1.
PIR	C64101. S52336. S52337. S52338.
RefSeq	NP_439060.1.
3D structure databases
SMR	P43791. Positions 3-160.
ModBase	Search...
Genome annotation databases
GeneID	949905.
GenomeReviews	Gene locus HI0899 in contig L42023_GR.
KEGG	hin:HI0899.
TIGR	HI0899.
Phylogenomic databases
HOGENOM	HBG665708.
OMA	LAHFKRT.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0899-MONOMER.
BRENDA	1.5.1.3. 109.
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_HAEIN

Accession

Primary (citable) accession number: P43791

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	February 9, 2010
This is version 71 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)