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Q9HJ28

- PNCB_THEAC

UniProt

Q9HJ28 - PNCB_THEAC

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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

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
Complete GO annotation...

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

        10         20         30         40         50
MNVFNTASDE DIKKGLASDV YFERTISAIG DKCNDLRVAM EATVSGPLDT
60 70 80 90 100
WINFTGLDEV LKLLEGLDVD LYAIPEGTIL FPRDANGLPV PFIRVEGRYC
110 120 130 140 150
DFGMYETAIL GFICQASGIS TKASKVRLAA GDSPFFSFGI RRMHPAISPM
160 170 180 190 200
IDRSAYIGGA DGVSGILGAK LIDQDPVGTM PHALSIMLGD EEAWKLTLEN
210 220 230 240 250
TKNGQKSVLL IDTYMDEKFA AIKIAEMFDK VDYIRLDTPS SRRGNFEALI
260 270 280 290 300
REVRWELALR GRSDIKIMVS GGLDENTVKK LREAGAEAFG VGTSISSAKP
310 320 330 340 350
FDFAMDIVEV NGKPETKRGK MSGRKNVLRC TSCHRIEVVP ANVQEKTCIC
360 370 380 390
GGSMQNLLVK YLSHGKRTSE YPRPKEIRSR SMKELEYFKD IS
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

« Hide 'large scale' publications
  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