Q8PGU5 (PNCB_XANAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	pncB
Ordered Locus Names:	XAC3521

Organism

Xanthomonas axonopodis pv. citri (strain 306) [Complete proteome] [HAMAP]

Taxonomic identifier

190486 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas citri group › Xanthomonas campestris pv. citri › Xanthomonas citri pv. citri

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Beta-nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00570
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1. HAMAP-Rule MF_00570
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the NAPRTase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: HAMAP nicotinate nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nicotinate phosphoribosyltransferase activity Inferred from electronic annotation. Source: HAMAP nicotinate-nucleotide diphosphorylase (carboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	Nicotinate phosphoribosyltransferase HAMAP-Rule MF_00570		PRO_0000205851

Sequences

	Sequence		Length	Mass (Da)
	Q8PGU5 [UniParc]. Last modified October 10, 2002. Version 1. Checksum: 319B228E08823664	FASTA	392	44,920
	10 20 30 40 50 60 MIIHSLLDTD LYKFTMMQAV LHQHPAAQVD YRFKCRTPGV DLAQFIDEIS REIDALCRLR 70 80 90 100 110 120 LREDEVDYLR SLRFIKPDFA DFLALFHLDR KYLSLTASAT HPGEIELTIR GPWLHTILFE 130 140 150 160 170 180 VPLLAIINEV WFRNTSEPDF EEGRSRLREK VASLRSMPAG CKIADYGTRR RYSRQWHGEL 190 200 210 220 230 240 LPLLRDGLGE QFVGTSNVYF AKQYGLTPLG TMAHEYLQAF QALGPRLRDS QVAALESWAR 250 260 270 280 290 300 EYRGDLGIAL SDVVGLDAFL RDFDLYFCKL FDGMRHDSGD PFEWGERVIA HLEAHRVDPR 310 320 330 340 350 360 TKVLVFSDGL NIDKVMRLYQ HFHTRCRLAF GVGTSLTNDL GPTPLQIVIK MVRCNGQPVA 370 380 390 KLSDSPGKSM CEDIGYLRYL RDVFGLPPMA ET

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008923 Genomic DNA. Translation: AAM38364.1.
RefSeq	NP_643828.1. NC_003919.1.
3D structure databases
ProteinModelPortal	Q8PGU5.
ModBase	Search...
Protein-protein interaction databases
STRING	190486.XAC3521.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM38364; AAM38364; XAC3521.
GeneID	1157592.
KEGG	xac:XAC3521.
PATRIC	24059186. VBIXanAxo33670_3644.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1488.
HOGENOM	HOG000284929.
KO	K00763.
OMA	SFGWGTN.
ProtClustDB	PRK05321.
Enzyme and pathway databases
UniPathway	UPA00253; UER00457.
Family and domain databases
HAMAP	MF_00570. NAPRTase.
InterPro	IPR006406. Nic_PRibTrfase. IPR015977. Nic_PRibTrfase-like. IPR007229. Nic_PRibTrfase-rel. IPR002638. Quinolinate_PRibosylTrfase_C. [Graphical view]
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...

Entry information

Entry name

PNCB_XANAC

Accession

Primary (citable) accession number: Q8PGU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 10, 2002
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program