Reviewed, UniProtKB/Swiss-Prot P31073 (DYR_CITFR)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:

folA

Organism

Citrobacter freundii

Taxonomic identifier

546 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

Protein attributes

Sequence length	159 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
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 – 159	159	Dihydrofolate reductase		PRO_0000186386
Regions
	Domain	1 – 158	158	DHFR
	Nucleotide binding	13 – 19	7	NADP By similarity
	Nucleotide binding	45 – 46	2	NADP By similarity
	Nucleotide binding	63 – 64	2	NADP By similarity
	Nucleotide binding	95 – 102	8	NADP By similarity
Sites
	Binding site	5	1	Substrate; via carbonyl oxygen By similarity
	Binding site	7	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	27	1	Substrate By similarity
	Binding site	52	1	Substrate By similarity
	Binding site	57	1	Substrate By similarity
	Binding site	76	1	NADP; via carbonyl oxygen By similarity
	Binding site	113	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31073-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 3CE7D7688577DCEE	FASTA	159	18,028
	10 20 30 40 50 60 MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV VMGRHTWESI GRPLPGRKNI 70 80 90 100 110 120 VISSKPGTDD RVQWVKSVDE AIAACGDEPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE 130 140 150 GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR

References

[1]	"Temporal and topological clustering of diverged residues among enterobacterial dihydrofolate reductases." Garvin L.D., Hardies S.C. Mol. Biol. Evol. 8:654-668(1991) [PubMed: 1766362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M26023 Genomic DNA. Translation: AAA23093.1.
PIR	B39799.
3D structure databases
SMR	P31073. Positions 1-159.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 2347.
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_CITFR

Accession

Primary (citable) accession number: P31073

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	February 9, 2010
This is version 49 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)