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P15093 (DYR_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrofolate reductase
EC=1.5.1.3
Gene names
Name:folA
Synonyms:hdrA
Ordered Locus Names:HVO_1279
OrganismHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Complete proteome] [HAMAP]
Taxonomic identifier309800 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloferax

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Dihydrofolate reductase
PRO_0000186433

Regions

Domain2 – 162161DHFR

Secondary structure

1 .................................. 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: 2509470] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: 20333302] [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: 9493269] [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: 17656587] [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: 18825778] [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...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8925483.
KEGGhvo:HVO_1279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

PhylomeDBP15093.
ProtClustDBCLSK2468396.

Family and domain databases

InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
Gene3DG3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit.
KOK00287.
PANTHERPTHR11549:SF1. DHFR. 1 hit.
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...

Entry information

Entry nameDYR_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: January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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