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Q60034 (DYR_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrofolate reductase

Short name=DHFR
EC=1.5.1.3
Gene names
Name:folA
Synonyms:dyrA
Ordered Locus Names:TM_1641
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence similarities

Belongs to the dihydrofolate reductase family.

Contains 1 DHFR (dihydrofolate reductase) domain.

Biophysicochemical properties

Temperature dependence:

Highly thermostable.

Sequence caution

The sequence AAD36708.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 169169Dihydrofolate reductase
PRO_0000186418

Regions

Domain3 – 169167DHFR
Nucleotide binding46 – 516NADP
Nucleotide binding65 – 673NADP
Nucleotide binding103 – 1053NADP

Sites

Binding site71Substrate; via carbonyl oxygen
Binding site91NADP; via amide nitrogen and carbonyl oxygen
Binding site161NADP; via carbonyl oxygen
Binding site281Substrate
Binding site591Substrate By similarity
Binding site811NADP; via carbonyl oxygen

Experimental info

Sequence conflict68 – 8114PKTSN…VFFNG → TQNFQQSFTRFFQR Ref.1
Sequence conflict1081T → S Ref.1
Sequence conflict138 – 1392FE → LQ Ref.1

Secondary structure

................................ 169
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60034 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: F5DA22C978E2C39D

FASTA16919,367
        10         20         30         40         50         60 
MAKVIFVLAM DVSGKIASSV ESWSSFEDRK NFRKITTEIG NVVMGRITFE EIGRPLPERL 

        70         80         90        100        110        120 
NVVLTRRPKT SNNPSLVFFN GSPADVVKFL EGKGYERVAV IGGKTVFTEF LREKLVDELF 

       130        140        150        160 
VTVEPYVFGK GIPFFDEFEG YFPLKLLEMR RLNERGTLFL KYSVEKSHR 

« Hide

References

« Hide 'large scale' references
[1]"The dihydrofolate reductase-encoding gene dyrA of the hyperthermophilic bacterium Thermotoga maritima."
van de Casteele M., Legrain C., Wilquet V., Glansdorff N.
Gene 158:101-105(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability."
Dams T., Schurig H., Jaenicke R.
Biol. Chem. 379:367-371(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[4]"The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability."
Dams T., Auerbach G., Bader G., Jacob U., Ploom T., Huber R., Jaenicke R.
J. Mol. Biol. 297:659-672(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH METHOTREXATE AND NADPH.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81845 Genomic DNA. Translation: CAA57437.1.
Y11021 Genomic DNA. Translation: CAA71903.1.
AE000512 Genomic DNA. Translation: AAD36708.1. Different initiation.
PIRA72231.
RefSeqNP_229441.1. NC_000853.1.
YP_007977999.1. NC_021214.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZ3X-ray2.10A/B2-169[»]
1D1GX-ray2.10A/B2-169[»]
ProteinModelPortalQ60034.
SMRQ60034. Positions 2-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36708; AAD36708; TM_1641.
GeneID896828.
KEGGtma:TM1641.
tmm:Tmari_1650.
PATRIC23938256. VBITheMar51294_1660.

Phylogenomic databases

eggNOGCOG0262.
KOK00287.
OMAKGYERVA.
OrthoDBEOG6KT2V2.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-461.
TMAR243274:GC6P-1687-MONOMER.
UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60034.

Entry information

Entry nameDYR_THEMA
AccessionPrimary (citable) accession number: Q60034
Secondary accession number(s): P96109
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways