Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15093 (DYRA_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. 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 HdrA

Short name=DHFR A
Short name=hDHFR-1
EC=1.5.1.3
Gene names
Name:hdrA
Synonyms:folA
Ordered Locus Names:HVO_1279
OrganismHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Reference proteome] [HAMAP]
Taxonomic identifier309800 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Protein attributes

Sequence length162 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. Ref.1

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. Ref.1

Enzyme regulation

Activity unstable at KCl and NaCl concentrations lower than 2 M and activity increases with increasing concentrations of KCl or NaCl. Ref.1

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Dihydrofolate reductase HdrA
PRO_0000186433

Regions

Domain2 – 162161DHFR
Nucleotide binding14 – 207NADP By similarity
Nucleotide binding47 – 482NADP By similarity
Nucleotide binding67 – 682NADP By similarity
Nucleotide binding101 – 1088NADP By similarity

Sites

Binding site81NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site291Substrate By similarity

Secondary structure

.................................. 162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15093 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 31B047661F14281F

FASTA16217,980
        10         20         30         40         50         60 
MELVSVAALA ENRVIGRDGE LPWPSIPADK KQYRSRIADD PVVLGRTTFE SMRDDLPGSA 

        70         80         90        100        110        120 
QIVMSRSERS FSVDTAHRAA SVEEAVDIAA SLDAETAYVI GGAAIYALFQ PHLDRMVLSR 

       130        140        150        160 
VPGEYEGDTY YPEWDAAEWE LDAETDHEGF TLQEWVRSAS SR 

« Hide

References

« Hide 'large scale' references
[1]"Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. The enzyme and its coding gene."
Zusman T., Rosenshine I., Boehm G., Jaenicke R., Leskiw B., Mevarech M.
J. Biol. Chem. 264:18878-18883(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
[2]"The complete genome sequence of Haloferax volcanii DS2, a model archaeon."
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.
PLoS ONE 5:E9605-E9605(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
[3]"Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii."
Pieper U., Kapadia G., Mevarech M., Herzberg O.
Structure 6:75-88(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
[4]"Structure in an extreme environment: NMR at high salt."
Binbuga B., Boroujerdi A.F., Young J.K.
Protein Sci. 16:1783-1787(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"NMR-derived folate-bound structure of dihydrofolate reductase 1 from the halophile Haloferax volcanii."
Boroujerdi A.F., Young J.K.
Biopolymers 91:140-144(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05088 Genomic DNA. Translation: AAA72219.1.
CP001956 Genomic DNA. Translation: ADE04659.1.
PIRA34429.
RefSeqYP_003535331.1. NC_013967.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VDRX-ray2.55A/B1-162[»]
2ITHNMR-A1-162[»]
2JYBNMR-A1-162[»]
ProteinModelPortalP15093.
SMRP15093. Positions 2-158.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE04659; ADE04659; HVO_1279.
GeneID8925483.
KEGGhvo:HVO_1279.

Phylogenomic databases

HOGENOMHOG000040233.
KOK00287.
OMAKEQTINK.

Enzyme and pathway databases

BioCycHVOL309800:GCOK-1284-MONOMER.
UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFPIRSF000194. DHFR. 1 hit.
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15093.

Entry information

Entry nameDYRA_HALVD
AccessionPrimary (citable) accession number: P15093
Secondary accession number(s): D4GXA6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 14, 2014
This is version 88 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