Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9HJ28 (PNCB_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative nicotinate phosphoribosyltransferase
Short name=NAPRTase
EC=2.4.2.11
Gene names
Ordered Locus Names:Ta1145
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma ›

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 Potential. Ref.2

Catalytic activity

Beta-nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.

Subunit structure

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

Domain

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. Ref.2

Sequence similarities

Belongs to the NAPRTase family. Highly divergent.

Caution

Although this protein is stated to be a nicotinate phosphoribosyltransferase (Ref.2), it has not been functionally characterized, and it might be a quinolinate phosphoribosyltransferase (QPRTase).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Putative nicotinate phosphoribosyltransferase
PRO_0000410976

Sites

Metal binding3301Zinc 1
Metal binding3301Zinc 2
Metal binding3331Zinc 1
Metal binding3481Zinc 2
Metal binding3501Zinc 1
Metal binding3501Zinc 2
Binding site211Nicotinate Probable
Binding site1381Nicotinate Probable
Binding site1791Nicotinate Probable
Binding site2351Nicotinate Probable
Binding site2401Phosphoribosylpyrophosphate
Binding site2721Phosphoribosylpyrophosphate; via amide nitrogen
Binding site2931Phosphoribosylpyrophosphate

Secondary structure

1 .......................................................................... 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HJ28 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: CC9BCD4E77E7C9AA

FASTA39243,297
        10         20         30         40         50         60 
MNVFNTASDE DIKKGLASDV YFERTISAIG DKCNDLRVAM EATVSGPLDT WINFTGLDEV 

        70         80         90        100        110        120 
LKLLEGLDVD LYAIPEGTIL FPRDANGLPV PFIRVEGRYC DFGMYETAIL GFICQASGIS 

       130        140        150        160        170        180 
TKASKVRLAA GDSPFFSFGI RRMHPAISPM IDRSAYIGGA DGVSGILGAK LIDQDPVGTM 

       190        200        210        220        230        240 
PHALSIMLGD EEAWKLTLEN TKNGQKSVLL IDTYMDEKFA AIKIAEMFDK VDYIRLDTPS 

       250        260        270        280        290        300 
SRRGNFEALI REVRWELALR GRSDIKIMVS GGLDENTVKK LREAGAEAFG VGTSISSAKP 

       310        320        330        340        350        360 
FDFAMDIVEV NGKPETKRGK MSGRKNVLRC TSCHRIEVVP ANVQEKTCIC GGSMQNLLVK 

       370        380        390 
YLSHGKRTSE YPRPKEIRSR SMKELEYFKD IS

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL445066 Genomic DNA. Translation: CAC12271.1.
RefSeqNP_394603.1. NC_002578.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YTDX-ray2.80A1-392[»]
1YTEX-ray2.75A1-392[»]
1YTKX-ray2.65A1-392[»]
2I1OX-ray2.40A1-392[»]
ProteinModelPortalQ9HJ28.
SMRQ9HJ28. Positions 1-389.
ModBaseSearch...

Protein-protein interaction databases

STRING273075.Ta1145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12271; CAC12271; CAC12271.
GeneID1456649.
KEGGtac:Ta1145.

Phylogenomic databases

eggNOGCOG1488.
HOGENOMHOG000098010.
KOK00763.
OMAGPYLEFA.
ProtClustDBPRK08662.

Enzyme and pathway databases

UniPathwayUPA00253; UER00457.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.90.1170.20. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR007229. Nic_PRibTrfase-rel.
IPR002638. Quinolinate_PRibosylTrfase_C.
IPR022412. Quinolinate_PRibosylTrfase_N.
[Graphical view]
PANTHERPTHR11098:SF1. PTHR11098:SF1. 1 hit.
PfamPF01729. QRPTase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000484. NAPRT. 1 hit.
SUPFAMSSF51690. Q_phspho_trans. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9HJ28.

Entry information

Entry namePNCB_THEAC
AccessionPrimary (citable) accession number: Q9HJ28
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents