Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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: 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.PROSITE-ProRule annotation1 Publication

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

Pathway:itetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydrofolate reductase HdrA (hdrA)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciHVOL309800:GCOK-1284-MONOMER.
BRENDAi1.5.1.3. 2561.
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 lineageiArchaeaEuryarchaeotaHalobacteriaHaloferacalesHaloferacaceaeHaloferax
ProteomesiUP000008243 Componenti: Chromosome

PTM / Processingi

Molecule processing

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

Interactioni

Protein-protein interaction databases

STRINGi309800.HVO_1279.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiWEMADES.

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi309800.HVO_1279.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000040233.
KOiK00287.
OMAiWEMADES.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BioCyciHVOL309800:GCOK-1284-MONOMER.
BRENDAi1.5.1.3. 2561.

Miscellaneous databases

EvolutionaryTraceiP15093.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.