Reviewed, UniProtKB/Swiss-Prot P0ABQ6 (DYR_SHIFL)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:	folA
Ordered Locus Names:	SF0045, S0047

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

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
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
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_0000186404
Regions
	Domain	1 – 158	158	DHFR
	Nucleotide binding	6 – 7	2	NADP By similarity
	Nucleotide binding	14 – 19	6	NADP By similarity
	Nucleotide binding	43 – 46	4	NADP By similarity
	Nucleotide binding	62 – 65	4	NADP By similarity
	Nucleotide binding	94 – 99	6	NADP By similarity
	Region	5 – 7	3	Substrate binding By similarity
Sites
	Binding site	27	1	Substrate By similarity
	Binding site	57	1	Substrate By similarity
	Binding site	78	1	NADP; via amide nitrogen By similarity
	Binding site	113	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0ABQ6-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 6A03CDCD7F5F8562	FASTA	159	17,999
	10 20 30 40 50 60 MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI GRPLPGRKNI 70 80 90 100 110 120 ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE 130 140 150 GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR

References

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005674 Genomic DNA. Translation: AAN41711.1. Different initiation. AE014073 Genomic DNA. Translation: AAP15591.1.
RefSeq	NP_706004.2. NP_835786.1.
3D structure databases
SMR	P0ABQ6. Positions 1-159.
ModBase	Search...
Genome annotation databases
GeneID	1024577. 1076432.
GenomeReviews	Gene locus SF0045 in contig AE005674_GR. Gene locus S0047 in contig AE014073_GR.
KEGG	sfl:SF0045. sfx:S0047.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG665708.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN41711.1-MONOMER.
BRENDA	1.5.1.3. 189495.
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...
Other Resources
BindingDB	P0ABQ6.

Entry information

Entry name

DYR_SHIFL

Accession

Primary (citable) accession number: P0ABQ6
Secondary accession number(s): P00379

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	February 9, 2010
This is version 39 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)