Reviewed, UniProtKB/Swiss-Prot P0ABQ8 (DYR8_SHISO)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase type 8
    EC=1.5.1.3
Alternative name(s):
    Dihydrofolate reductase type VIII
    DHFR type IIIC

Gene names

Name:	dhfrVIII
Synonyms:	dhfrIIIc

Encoded on

Plasmid pBH700

Organism

Shigella sonnei

Taxonomic identifier

624 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	169 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.
Subunit structure	Homodimer By similarity.
Miscellaneous	Confers high-level trimethoprim resistance.
Sequence similarities	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	Antibiotic resistance Methotrexate resistance One-carbon metabolism Trimethoprim resistance
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	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 response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW response to methotrexate 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 – 169	169	Dihydrofolate reductase type 8		PRO_0000186426
Regions
	Domain	3 – 169	167	DHFR

Sequences

	Sequence		Length	Mass (Da)
	P0ABQ8-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 76E1ABA0C0DE30CC	FASTA	169	19,021
	10 20 30 40 50 60 MIELHAILAA TANGCIGKDN ALPWPPLKGD LARFKKLTMG KVVIMGRKTY ESLPVKLEGR 70 80 90 100 110 120 TCIVMTRQAL ELPGVRDANG AIFVNNVSDA MRFAQEESVG DVAYVIGGAE IFKRLALMIT 130 140 150 160 QIELTFVKRL YEGDTYVDLA EMVKDYEQNG MEEHDLHTYF TYRKKELTE

References

[1]	"Sequence identity with type VIII and association with IS176 of type IIIc dihydrofolate reductase from Shigella sonnei." Barg N.L., Register S., Thomson C., Amyes S. Antimicrob. Agents Chemother. 39:112-116(1995) [PubMed: 7695291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09273 Genomic DNA. Translation: AAA79232.1.
3D structure databases
SMR	P0ABQ8. Positions 10-169.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 74546.
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

DYR8_SHISO

Accession

Primary (citable) accession number: P0ABQ8
Secondary accession number(s): Q57452

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	February 9, 2010
This is version 25 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)