P39683 (NPT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nicotinate phosphoribosyltransferase
Short name=NAPRTase
EC=2.4.2.11

Gene names

Name:	NPT1
Ordered Locus Names:	YOR209C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for growth under anaerobic conditions. Ref.5
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.
Subcellular location	Cytoplasm. Nucleus Ref.6.
Miscellaneous	Present with 32100 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the NAPRTase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm Nucleus
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway chromatin silencing at rDNA Inferred from mutant phenotype PubMed 11901108. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype PubMed 11901108. Source: SGD nicotinate nucleotide salvage Inferred from direct assay PubMed 11884393. Source: SGD replicative cell aging Inferred from mutant phenotype PubMed 11000115. Source: SGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 11884393. Source: SGD
Molecular_function	nicotinate phosphoribosyltransferase activity Inferred from direct assay PubMed 9521740. Source: SGD nicotinate-nucleotide diphosphorylase (carboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRP40	P33203	2	EBI-12218,EBI-701
RSP5	P39940	2	EBI-12218,EBI-16219

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 429

429

Nicotinate phosphoribosyltransferase

PRO_0000205862

Experimental info

Sequence conflict

131 – 137

7

YEIPLLS → MRSLTV in CAA85352. Ref.1

Sequence conflict

144 – 158

15

FKFVD…ENQLE → LIVTSTGLRNHR Ref.1

Sequence conflict

175 – 177

3

SEF → RIH in CAA85352. Ref.1

Sequence conflict

243

1

E → EL in CAA85352. Ref.1

Secondary structure

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429

Helix Strand Turn

Details...

Beta strand

11 – 13

3

Helix

14 – 26

13

Beta strand

31 – 39

9

Helix

47 – 59

13

Helix

60 – 62

3

Helix

67 – 76

10

Helix

82 – 89

8

Helix

97 – 100

4

Beta strand

101 – 108

8

Beta strand

111 – 124

14

Helix

125 – 128

4

Helix

132 – 146

15

Helix

156 – 169

14

Beta strand

174 – 176

3

Helix

185 – 201

17

Helix

203 – 206

4

Turn

207 – 209

3

Beta strand

210 – 215

6

Helix

216 – 222

7

Helix

232 – 242

11

Helix

248 – 260

13

Helix

262 – 264

3

Beta strand

267 – 269

3

Helix

275 – 279

5

Helix

286 – 289

4

Beta strand

292 – 295

4

Helix

300 – 312

13

Beta strand

321 – 326

6

Helix

332 – 344

13

Beta strand

348 – 353

6

Helix

355 – 358

4

Beta strand

364 – 366

3

Beta strand

369 – 371

3

Beta strand

376 – 383

8

Helix

402 – 411

10

Sequences

	Sequence		Length	Mass (Da)
	P39683 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: F3F7941476C3398B	FASTA	429	49,019
	10 20 30 40 50 60 MSEPVIKSLL DTDMYKITMH AAVFTNFPDV TVTYKYTNRS SQLTFNKEAI NWLKEQFSYL 70 80 90 100 110 120 GNLRFTEEEI EYLKQEIPYL PSAYIKYISS SNYKLHPEEQ ISFTSEEIEG KPTHYKLKIL 130 140 150 160 170 180 VSGSWKDTIL YEIPLLSLIS EAYFKFVDID WDYENQLEQA EKKAETLFDN GIRFSEFGTR 190 200 210 220 230 240 RRRSLKAQDL IMQGIMKAVN GNPDRNKSLL LGTSNILFAK KYGVKPIGTV AHEWVMGVAS 250 260 270 280 290 300 ISEDYLHANK NAMDCWINTF GAKNAGLALT DTFGTDDFLK SFRPPYSDAY VGVRQDSGDP 310 320 330 340 350 360 VEYTKKISHH YHDVLKLPKF SKIICYSDSL NVEKAITYSH AAKENGMLAT FGIGTNFTND 370 380 390 400 410 420 FRKKSEPQVK SEPLNIVIKL LEVNGNHAIK ISDNLGKNMG DPATVKRVKE ELGYTERSWS GDNEAHRWT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The BRF1-STE4 region chromosome XV contains eleven genes: two of them define distinct RNA polymerase subunits and one encodes a putative nicotinate phosphorybosyl transferase." Lalo D., Doira C., Thuriaux P. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Interactions between three common subunits of yeast RNA polymerases I and III." Lalo D., Carles C., Sentenac A., Thuriaux P. Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43. Strain: ATCC 28383 / FL100 / VTT C-80102.
[5]	"Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae." Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M., Rytka J., Herbert C.J. FEBS Lett. 517:97-102(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z36878 Genomic DNA. Translation: CAA85352.1.
Z75117 Genomic DNA. Translation: CAA99424.1.
L11274 Genomic DNA. Translation: AAB59317.1.
BK006948 Genomic DNA. Translation: DAA10981.1.

PIR

S67101.

RefSeq

NP_014852.1. NM_001183628.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VLP	X-ray	1.75	A/B/C/D	1-429	[»]

ProteinModelPortal

P39683.

SMR

P39683. Positions 1-419.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4984N.

IntAct

P39683. 8 interactions.

MINT

MINT-567492.

STRING

4932.YOR209C.

Proteomic databases

PaxDb

P39683.

PeptideAtlas

P39683.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR209C; YOR209C; YOR209C.

GeneID

854384.

KEGG

sce:YOR209C.

Organism-specific databases

CYGD

YOR209c.

SGD

S000005735. NPT1.

Phylogenomic databases

eggNOG

COG1488.

HOGENOM

HOG000284928.

KO

K00763.

OMA

SFGWGTN.

OrthoDB

EOG479JGB.

Enzyme and pathway databases

BioCyc

YEAST:YOR209C-MONOMER.

BRENDA

2.4.2.11. 984.

UniPathway

UPA00253; UER00457.

Gene expression databases

Genevestigator

P39683.

GermOnline

YOR209C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR006406. Nic_PRibTrfase.
IPR015977. Nic_PRibTrfase-like.
IPR007229. Nic_PRibTrfase-rel.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]

PANTHER

PTHR11098:SF1. PTHR11098:SF1. 1 hit.

Pfam

PF04095. NAPRTase. 1 hit.
[Graphical view]

PIRSF

PIRSF000484. NAPRT. 1 hit.

SUPFAM

SSF51690. Q_phspho_trans. 1 hit.

TIGRFAMs

TIGR01514. NAPRTase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P39683.

NextBio

976529.

Entry information

Entry name

NPT1_YEAST

Accession

Primary (citable) accession number: P39683
Secondary accession number(s): D6W2R5, Q08626

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program