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P15093

- DYRA_HALVD

UniProt

P15093 - DYRA_HALVD

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
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    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

    MELVSVAALA ENRVIGRDGE LPWPSIPADK KQYRSRIADD PVVLGRTTFE    50
    SMRDDLPGSA QIVMSRSERS FSVDTAHRAA SVEEAVDIAA SLDAETAYVI 100
    GGAAIYALFQ PHLDRMVLSR VPGEYEGDTY YPEWDAAEWE LDAETDHEGF 150
    TLQEWVRSAS SR 162
    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

    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