Reviewed, UniProtKB/Swiss-Prot Q5V600 (DYR2_HALMA)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase 2
    EC=1.5.1.3

Gene names

Name:	folA2
Ordered Locus Names:	pNG7359

Encoded on

Plasmid pNG700

Organism

Haloarcula marismortui (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

2238 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length	167 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 Plasmid
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 – 167	167	Dihydrofolate reductase 2		PRO_0000186432
Regions
	Domain	4 – 167	164	DHFR

Sequences

	Sequence		Length	Mass (Da)
	Q5V600-1 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 37176A5FE13B17EC	FASTA	167	18,093
	10 20 30 40 50 60 MCMKLSLIAA VAANGVIGAG GDIPWQYPED LTHFKETTVG HPVIMGRRTF ESIRRDLDGP 70 80 90 100 110 120 LPERLNIVLT TTPHQLPDSV TAVTSTTAAV AEAADSDAST TYVIGGATVY EQFLPQADEL 130 140 150 160 ILTELAAAFD GDTVFPTVDW SNWTEMERTT HSEFAIVRYT RTSSDSA

References

[1]

"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea." Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V. Genome Res. 14:2221-2234(2004) [PubMed: 15520287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY596296 Genomic DNA. Translation: AAV45052.1.
RefSeq	YP_134758.1.
3D structure databases
SMR	Q5V600. Positions 3-151.
ModBase	Search...
Genome annotation databases
GeneID	3127320.
GenomeReviews	Gene locus pNG7359 in contig AY596296_GR.
KEGG	hma:pNG7359.
NMPDR	fig|272569.1.peg.3548.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG665708.
OMA	GLPWHLP.
Enzyme and pathway databases
BioCyc	HMAR272569:PNG7359-MONOMER.
BRENDA	1.5.1.3. 88.
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

DYR2_HALMA

Accession

Primary (citable) accession number: Q5V600

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	December 7, 2004
Last modified:	February 9, 2010
This is version 43 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)