Reviewed, UniProtKB/Swiss-Prot P00377 (DYR_PIG)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:

DHFR

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	186 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; 5,6,7,8-tetrahydrofolate from 7,8-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	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 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 – 186	186	Dihydrofolate reductase		PRO_0000186365
Regions
	Domain	3 – 184	182	DHFR
Amino acid modifications
	Modified residue	162	1	Cysteine derivative; partial

Sequences

	Sequence		Length	Mass (Da)
	P00377-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: D05DB526FE5C12CE	FASTA	186	21,455
	10 20 30 40 50 60 VRPLNCIVAV SQNMGIGKNG DLPWPPLRNE YKYFQRMTTT SSVEGKQNLV IMGRKTWFSI 70 80 90 100 110 120 PEKNRPLKDR INIVLSRELK EPPQGAHFLA KSLDDALKLT EQPELKDKVD MVWIVGGSSV 130 140 150 160 170 180 YKEAMNKPGH IRLFVTRIMK EFESDTFFPE IDLEKYKLLS ECSGVPSDVQ EEKGIKYKFE VYEKNN

References

[1]	"Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence." Smith S.L., Patrick P., Stone D., Phillips A.W., Burchall J.J. J. Biol. Chem. 254:11475-11484(1979) [PubMed: 500653] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver.

Cross-references

Sequence databases
PIR	RDPGD. A00389.
3D structure databases
HSSP	HSSP built from PDB template 1KMS based on UniProtKB P00374.
SMR	P00377. Positions 1-186.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00377.
Enzyme and pathway databases
BRENDA	1.5.1.3. 249.
Family and domain databases
InterPro	IPR012259. DHFR. IPR001796. DHFR_reg. IPR017925. Dihydrofolate_reductase_CS. [Graphical view]
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_PIG

Accession

Primary (citable) accession number: P00377

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	September 22, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)