Dihydrofolate reductase - Mycobacterium tuberculosis

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Reviewed, UniProtKB/Swiss-Prot P0A546 (DYR_MYCTU)

Last modified June 16, 2009. Version 36. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Dihydrofolate reductase
EC=1.5.1.3

Gene names

Name:	folA
Synonyms:	dfrA
Ordered Locus Names:	Rv2763c, MT2833
ORF Names:	MTV002.28c

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	159 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; tetrahydrofolate from 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	3D-structure 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 compound 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

159

Dihydrofolate reductase

PRO_0000186400

Regions

Domain

158

DHFR

Secondary structure

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159

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P0A546-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: F17C038F1B773797
Show »

159

17,640

        10         20         30         40         50         60 
MVGLIWAQAT SGVIGRGGDI PWRLPEDQAH FREITMGHTI VMGRRTWDSL PAKVRPLPGR 

        70         80         90        100        110        120 
RNVVLSRQAD FMASGAEVVG SLEEALTSPE TWVIGGGQVY ALALPYATRC EVTEVDIGLP 

       130        140        150 
REAGDALAPV LDETWRGETG EWRFSRSGLR YRLYSYHRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs." Li R., Sirawaraporn R., Chitnumsub P., Sirawaraporn W., Wooden J., Athappilly F., Turley S., Hol W.G.J. J. Mol. Biol. 295:307-323(2000) [PubMed: 10623528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

BX842580 Genomic DNA. Translation: CAA15559.1.
AE000516 Genomic DNA. Translation: AAK47152.1.

PIR

RefSeq

NP_217279.1.
NP_337338.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DF7	X-ray	1.70	A	1-159	[»]
1DG5	X-ray	2.00	A	1-159	[»]
1DG7	X-ray	1.80	A	1-159	[»]
1DG8	X-ray	2.00	A	1-159	[»]
2CIG	X-ray	1.90	A	1-159	[»]

ModBase

Genome annotation databases

GeneID

887777.
925455.

GenomeReviews

Gene locus MT2833 in contig AE000516_GR.
Gene locus Rv2763c in contig AL123456_GR.

KEGG

mtc:MT2833.
mtu:Rv2763c.

TIGR

Organism-specific databases

TubercuList

Phylogenomic databases

HOGENOM

OMA

P0A546. WVIGGER.

Enzyme and pathway databases

BRENDA

1.5.1.3. 809.

Family and domain databases

InterPro

IPR012259. DHFR.
IPR001796. DHFR_reg.
IPR017925. Dihydrofolate_reductase_CS.
[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

Entry information

Entry name

DYR_MYCTU

Accession

Primary (citable) accession number: P0A546
Secondary accession number(s): O33305

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	June 16, 2009
This is version 36 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents