Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9HJ28

- PNCB_THEAC

UniProt

Q9HJ28 - PNCB_THEAC

Protein

Putative nicotinate phosphoribosyltransferase

Gene

Ta1145

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the transfer of the phosphoribosyl moiety of phosphoribosylpyrophosphate (PRPP) onto nicotinate (NA) to yield nicotinate mononucleotide (NAMN), an intermediate in the biosynthesis of NAD.Curated
    Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.By similarity

    Catalytic activityi

    Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211NicotinateCurated
    Binding sitei138 – 1381NicotinateCurated
    Binding sitei179 – 1791NicotinateCurated
    Binding sitei235 – 2351NicotinateCurated
    Binding sitei240 – 2401Phosphoribosylpyrophosphate
    Binding sitei272 – 2721Phosphoribosylpyrophosphate; via amide nitrogen
    Binding sitei293 – 2931Phosphoribosylpyrophosphate
    Metal bindingi330 – 3301Zinc 11 Publication
    Metal bindingi330 – 3301Zinc 21 Publication
    Metal bindingi333 – 3331Zinc 11 Publication
    Metal bindingi348 – 3481Zinc 21 Publication
    Metal bindingi350 – 3501Zinc 11 Publication
    Metal bindingi350 – 3501Zinc 21 Publication

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: InterPro
    4. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. NAD biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase, Transferase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00457.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative nicotinate phosphoribosyltransferase (EC:6.3.4.21)
    Short name:
    NAPRTase
    Gene namesi
    Ordered Locus Names:Ta1145
    OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
    Taxonomic identifieri273075 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    ProteomesiUP000001024: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 392392Putative nicotinate phosphoribosyltransferasePRO_0000410976Add
    BLAST

    Proteomic databases

    PRIDEiQ9HJ28.

    Interactioni

    Subunit structurei

    Homodimer. Forms a trimer of dimers in the crystal.2 Publications

    Protein-protein interaction databases

    STRINGi273075.Ta1145.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi9 – 135
    Helixi21 – 299
    Helixi30 – 356
    Beta strandi37 – 448
    Helixi57 – 648
    Beta strandi70 – 734
    Beta strandi91 – 988
    Helixi99 – 1024
    Helixi103 – 1053
    Helixi106 – 13025
    Beta strandi135 – 1373
    Helixi140 – 1423
    Helixi145 – 1473
    Helixi148 – 15710
    Beta strandi161 – 1633
    Helixi166 – 1727
    Helixi182 – 1887
    Helixi190 – 19910
    Beta strandi208 – 2103
    Beta strandi213 – 2153
    Helixi217 – 2259
    Beta strandi233 – 2364
    Helixi240 – 2423
    Helixi246 – 25914
    Beta strandi265 – 2728
    Helixi275 – 2839
    Beta strandi288 – 2914
    Helixi293 – 2964
    Beta strandi303 – 3108
    Beta strandi325 – 3306
    Turni331 – 3333
    Beta strandi336 – 3405
    Beta strandi345 – 3473
    Beta strandi349 – 3524
    Beta strandi354 – 3563
    Beta strandi359 – 3635
    Beta strandi366 – 3694
    Helixi374 – 38411
    Helixi385 – 3884

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YTDX-ray2.80A1-392[»]
    1YTEX-ray2.75A1-392[»]
    1YTKX-ray2.65A1-392[»]
    2I1OX-ray2.40A1-392[»]
    ProteinModelPortaliQ9HJ28.
    SMRiQ9HJ28. Positions 1-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HJ28.

    Family & Domainsi

    Domaini

    Consists of three domains, an N-terminal domain, a central functional domain, and a unique C-terminal domain containing a zinc knuckle-like motif containing 4 cysteines.1 Publication

    Sequence similaritiesi

    Belongs to the NAPRTase family. Highly divergent.Curated

    Phylogenomic databases

    eggNOGiCOG1488.
    HOGENOMiHOG000098010.
    KOiK00763.
    OMAiSPMIDRS.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    3.90.1170.20. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR007229. Nic_PRibTrfase-Fam.
    IPR002638. Quinolinate_PRibosylTrfase_C.
    IPR022412. Quinolinate_PRibosylTrfase_N.
    [Graphical view]
    PANTHERiPTHR11098. PTHR11098. 1 hit.
    PfamiPF01729. QRPTase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000484. NAPRT. 1 hit.
    SUPFAMiSSF51690. SSF51690. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9HJ28-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVFNTASDE DIKKGLASDV YFERTISAIG DKCNDLRVAM EATVSGPLDT    50
    WINFTGLDEV LKLLEGLDVD LYAIPEGTIL FPRDANGLPV PFIRVEGRYC 100
    DFGMYETAIL GFICQASGIS TKASKVRLAA GDSPFFSFGI RRMHPAISPM 150
    IDRSAYIGGA DGVSGILGAK LIDQDPVGTM PHALSIMLGD EEAWKLTLEN 200
    TKNGQKSVLL IDTYMDEKFA AIKIAEMFDK VDYIRLDTPS SRRGNFEALI 250
    REVRWELALR GRSDIKIMVS GGLDENTVKK LREAGAEAFG VGTSISSAKP 300
    FDFAMDIVEV NGKPETKRGK MSGRKNVLRC TSCHRIEVVP ANVQEKTCIC 350
    GGSMQNLLVK YLSHGKRTSE YPRPKEIRSR SMKELEYFKD IS 392
    Length:392
    Mass (Da):43,297
    Last modified:March 1, 2001 - v1
    Checksum:iCC9BCD4E77E7C9AA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL445066 Genomic DNA. Translation: CAC12271.1.
    RefSeqiNP_394603.1. NC_002578.1.
    WP_010901554.1. NC_002578.1.

    Genome annotation databases

    EnsemblBacteriaiCAC12271; CAC12271; CAC12271.
    GeneIDi1456649.
    KEGGitac:Ta1145.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL445066 Genomic DNA. Translation: CAC12271.1 .
    RefSeqi NP_394603.1. NC_002578.1.
    WP_010901554.1. NC_002578.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YTD X-ray 2.80 A 1-392 [» ]
    1YTE X-ray 2.75 A 1-392 [» ]
    1YTK X-ray 2.65 A 1-392 [» ]
    2I1O X-ray 2.40 A 1-392 [» ]
    ProteinModelPortali Q9HJ28.
    SMRi Q9HJ28. Positions 1-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273075.Ta1145.

    Proteomic databases

    PRIDEi Q9HJ28.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC12271 ; CAC12271 ; CAC12271 .
    GeneIDi 1456649.
    KEGGi tac:Ta1145.

    Phylogenomic databases

    eggNOGi COG1488.
    HOGENOMi HOG000098010.
    KOi K00763.
    OMAi SPMIDRS.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00457 .

    Miscellaneous databases

    EvolutionaryTracei Q9HJ28.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.90.1170.20. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR007229. Nic_PRibTrfase-Fam.
    IPR002638. Quinolinate_PRibosylTrfase_C.
    IPR022412. Quinolinate_PRibosylTrfase_N.
    [Graphical view ]
    PANTHERi PTHR11098. PTHR11098. 1 hit.
    Pfami PF01729. QRPTase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000484. NAPRT. 1 hit.
    SUPFAMi SSF51690. SSF51690. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
      Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
      Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
    2. "Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum."
      Shin D.H., Oganesyan N., Jancarik J., Yokota H., Kim R., Kim S.H.
      J. Biol. Chem. 280:18326-18335(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH NICOTINATE MONONUCLEOTIDE AND PRPP, FUNCTION, DOMAIN, SUBUNIT.
      Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
    3. "Crystal structure of a zinc ion bound nicotinate phosphoribosyltransferase from Thermoplasma acidophilum."
      Berkeley structural genomics center (BSGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC.

    Entry informationi

    Entry nameiPNCB_THEAC
    AccessioniPrimary (citable) accession number: Q9HJ28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Although this protein is stated to be a nicotinate phosphoribosyltransferase, it has not been functionally characterized, and it might be a quinolinate phosphoribosyltransferase (QPRTase).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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