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P15093

- DYRA_HALVD

UniProt

P15093 - DYRA_HALVD

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Protein

Dihydrofolate reductase HdrA

Gene

hdrA

Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.1 Publication

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.1 PublicationPROSITE-ProRule annotation

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei29 – 291SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 207NADPBy similarity
Nucleotide bindingi47 – 482NADPBy similarity
Nucleotide bindingi67 – 682NADPBy similarity
Nucleotide bindingi101 – 1088NADPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. NADP binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciHVOL309800:GCOK-1284-MONOMER.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase HdrA (EC:1.5.1.3)
Short name:
DHFR A
Short name:
hDHFR-1
Gene namesi
Name:hdrA
Synonyms:folA
Ordered Locus Names:HVO_1279
OrganismiHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Taxonomic identifieri309800 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax
ProteomesiUP000008243: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Dihydrofolate reductase HdrAPRO_0000186433Add
BLAST

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Beta strandi13 – 175
Helixi27 – 3610
Beta strandi38 – 403
Beta strandi42 – 454
Helixi46 – 516
Turni52 – 543
Beta strandi58 – 647
Beta strandi73 – 753
Beta strandi78 – 814
Helixi82 – 9110
Beta strandi97 – 1015
Helixi103 – 1097
Helixi110 – 1123
Beta strandi114 – 12411
Beta strandi128 – 1303
Turni136 – 1383
Beta strandi139 – 1468
Beta strandi151 – 1577

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VDRX-ray2.55A/B1-162[»]
2ITHNMR-A1-162[»]
2JYBNMR-A1-162[»]
ProteinModelPortaliP15093.
SMRiP15093. Positions 2-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15093.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 162161DHFRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000040233.
KOiK00287.
OMAiKEQTINK.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15093-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELVSVAALA ENRVIGRDGE LPWPSIPADK KQYRSRIADD PVVLGRTTFE
60 70 80 90 100
SMRDDLPGSA QIVMSRSERS FSVDTAHRAA SVEEAVDIAA SLDAETAYVI
110 120 130 140 150
GGAAIYALFQ PHLDRMVLSR VPGEYEGDTY YPEWDAAEWE LDAETDHEGF
160
TLQEWVRSAS SR
Length:162
Mass (Da):17,980
Last modified:April 1, 1990 - v1
Checksum:i31B047661F14281F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05088 Genomic DNA. Translation: AAA72219.1.
CP001956 Genomic DNA. Translation: ADE04659.1.
PIRiA34429.
RefSeqiWP_004043660.1. NZ_AOHU01000091.1.
YP_003535331.1. NC_013967.1.

Genome annotation databases

EnsemblBacteriaiADE04659; ADE04659; HVO_1279.
GeneIDi8925483.
KEGGihvo:HVO_1279.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05088 Genomic DNA. Translation: AAA72219.1 .
CP001956 Genomic DNA. Translation: ADE04659.1 .
PIRi A34429.
RefSeqi WP_004043660.1. NZ_AOHU01000091.1.
YP_003535331.1. NC_013967.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VDR X-ray 2.55 A/B 1-162 [» ]
2ITH NMR - A 1-162 [» ]
2JYB NMR - A 1-162 [» ]
ProteinModelPortali P15093.
SMRi P15093. Positions 2-158.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADE04659 ; ADE04659 ; HVO_1279 .
GeneIDi 8925483.
KEGGi hvo:HVO_1279.

Phylogenomic databases

HOGENOMi HOG000040233.
KOi K00287.
OMAi KEQTINK.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .
BioCyci HVOL309800:GCOK-1284-MONOMER.

Miscellaneous databases

EvolutionaryTracei P15093.

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000194. DHFR. 1 hit.
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDYRA_HALVD
AccessioniPrimary (citable) accession number: P15093
Secondary accession number(s): D4GXA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 1, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3