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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: 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 similarity1 Publication

Catalytic activityi

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

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes nicotinate D-ribonucleotide from nicotinate.
Proteins known to be involved in this subpathway in this organism are:
  1. Putative nicotinate phosphoribosyltransferase (Ta1145)
This subpathway is part of the pathway NAD(+) 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 nicotinate D-ribonucleotide from nicotinate, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei21NicotinateCurated1
Binding sitei138NicotinateCurated1
Binding sitei179NicotinateCurated1
Binding sitei235NicotinateCurated1
Binding sitei240Phosphoribosylpyrophosphate1
Binding sitei272Phosphoribosylpyrophosphate; via amide nitrogen1
Binding sitei293Phosphoribosylpyrophosphate1
Metal bindingi330Zinc 11 Publication1
Metal bindingi330Zinc 21 Publication1
Metal bindingi333Zinc 11 Publication1
Metal bindingi348Zinc 21 Publication1
Metal bindingi350Zinc 11 Publication1
Metal bindingi350Zinc 21 Publication1

GO - Molecular functioni

GO - Biological processi

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

BioCyciTACI273075:G13HZ-1158-MONOMER.
BRENDAi6.3.4.21. 6324.
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
Proteomesi
  • UP000001024 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004109761 – 392Putative nicotinate phosphoribosyltransferaseAdd BLAST392

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

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi9 – 13Combined sources5
Helixi21 – 29Combined sources9
Helixi30 – 35Combined sources6
Beta strandi37 – 44Combined sources8
Helixi57 – 64Combined sources8
Beta strandi70 – 73Combined sources4
Beta strandi91 – 98Combined sources8
Helixi99 – 102Combined sources4
Helixi103 – 105Combined sources3
Helixi106 – 130Combined sources25
Beta strandi135 – 137Combined sources3
Helixi140 – 142Combined sources3
Helixi145 – 147Combined sources3
Helixi148 – 157Combined sources10
Beta strandi161 – 163Combined sources3
Helixi166 – 172Combined sources7
Helixi182 – 188Combined sources7
Helixi190 – 199Combined sources10
Beta strandi208 – 210Combined sources3
Beta strandi213 – 215Combined sources3
Helixi217 – 225Combined sources9
Beta strandi233 – 236Combined sources4
Helixi240 – 242Combined sources3
Helixi246 – 259Combined sources14
Beta strandi265 – 272Combined sources8
Helixi275 – 283Combined sources9
Beta strandi288 – 291Combined sources4
Helixi293 – 296Combined sources4
Beta strandi303 – 310Combined sources8
Beta strandi325 – 330Combined sources6
Turni331 – 333Combined sources3
Beta strandi336 – 340Combined sources5
Beta strandi345 – 347Combined sources3
Beta strandi349 – 352Combined sources4
Beta strandi354 – 356Combined sources3
Beta strandi359 – 363Combined sources5
Beta strandi366 – 369Combined sources4
Helixi374 – 384Combined sources11
Helixi385 – 388Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YTDX-ray2.80A1-392[»]
1YTEX-ray2.75A1-392[»]
1YTKX-ray2.65A1-392[»]
2I1OX-ray2.40A1-392[»]
ProteinModelPortaliQ9HJ28.
SMRiQ9HJ28.
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

eggNOGiarCOG01481. Archaea.
COG1488. LUCA.
HOGENOMiHOG000098010.
KOiK00763.
OMAiGPVMRIE.

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:
EMBLi
GenBanki
DDBJi
Links Updated
AL445066 Genomic DNA. Translation: CAC12271.1.
RefSeqiWP_010901554.1. NC_002578.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445066 Genomic DNA. Translation: CAC12271.1.
RefSeqiWP_010901554.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YTDX-ray2.80A1-392[»]
1YTEX-ray2.75A1-392[»]
1YTKX-ray2.65A1-392[»]
2I1OX-ray2.40A1-392[»]
ProteinModelPortaliQ9HJ28.
SMRiQ9HJ28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta1145.

Proteomic databases

PRIDEiQ9HJ28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiarCOG01481. Archaea.
COG1488. LUCA.
HOGENOMiHOG000098010.
KOiK00763.
OMAiGPVMRIE.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00457.
BioCyciTACI273075:G13HZ-1158-MONOMER.
BRENDAi6.3.4.21. 6324.

Miscellaneous databases

EvolutionaryTraceiQ9HJ28.

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.
ProtoNetiSearch...

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: November 2, 2016
This is version 93 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

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 one 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.