Reviewed, UniProtKB/Swiss-Prot P15093 (DYR_HALVO)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:

folA

Organism

Halobacterium volcanii (Haloferax volcanii)

Taxonomic identifier

2246 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloferax

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	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	One-carbon metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
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
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_0000186433

Regions

Domain

2 – 162

161

DHFR

Secondary structure

1

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162

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

13 – 17

5

Helix

27 – 36

10

Beta strand

38 – 40

3

Beta strand

42 – 45

4

Helix

46 – 51

6

Turn

52 – 54

3

Beta strand

58 – 64

7

Beta strand

73 – 75

3

Beta strand

78 – 81

4

Helix

82 – 91

10

Beta strand

97 – 101

5

Helix

103 – 109

7

Helix

110 – 112

3

Beta strand

114 – 124

11

Beta strand

128 – 130

3

Turn

136 – 138

3

Beta strand

139 – 146

8

Beta strand

151 – 157

7

Sequences

	Sequence		Length	Mass (Da)
	P15093-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 31B047661F14281F	FASTA	162	17,980
	10 20 30 40 50 60 MELVSVAALA ENRVIGRDGE LPWPSIPADK KQYRSRIADD PVVLGRTTFE SMRDDLPGSA 70 80 90 100 110 120 QIVMSRSERS FSVDTAHRAA SVEEAVDIAA SLDAETAYVI GGAAIYALFQ PHLDRMVLSR 130 140 150 160 VPGEYEGDTY YPEWDAAEWE LDAETDHEGF TLQEWVRSAS SR

References

[1]	"Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. The enzyme and its coding gene." Zusman T., Rosenshine I., Boehm G., Jaenicke R., Leskiw B., Mevarech M. J. Biol. Chem. 264:18878-18883(1989) [PubMed: 2509470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii." Pieper U., Kapadia G., Mevarech M., Herzberg O. Structure 6:75-88(1998) [PubMed: 9493269] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05088 Genomic DNA. Translation: AAA72219.1.

PIR

A34429.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VDR	X-ray	2.55	A/B	1-162	[»]
2ITH	NMR	-	A	1-162	[»]
2JYB	NMR	-	A	1-162	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.5.1.3. 430.

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_HALVO

Accession

Primary (citable) accession number: P15093

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 59 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)