B2AIF3 (RBKTP_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional ribose 1,5-bisphosphokinase-thymidine phosphorylase

Including the following 2 domains:

1. Ribose 1,5-bisphosphate phosphokinase PhnN
   EC=2.7.4.23
   Alternative name(s):
   Ribose 1,5-bisphosphokinase
2. Putative thymidine phosphorylase
   EC=2.4.2.4
   Alternative name(s):
   TdRPase

Gene names

Name:	phnN
Ordered Locus Names:	RALTA_B0356

Organism

Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]

Taxonomic identifier

164546 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	601 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP) By similarity. HAMAP-Rule MF_00703
Catalytic activity	ATP + alpha-D-ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00703 Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_00703
Pathway	Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 3/3. HAMAP-Rule MF_00703
Sequence similarities	In the N-terminal section; belongs to the ribose 1,5-bisphosphokinase family. In the C-terminal section; belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway pyrimidine nucleobase metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleoside metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorylase activity Inferred from electronic annotation. Source: InterPro ribose 1,5-bisphosphate phosphokinase activity Inferred from electronic annotation. Source: EC thymidine phosphorylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 601	601	Bifunctional ribose 1,5-bisphosphokinase-thymidine phosphorylase HAMAP-Rule MF_00703		PRO_0000412779
Regions
	Nucleotide binding	12 – 19	8	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2AIF3 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 2C4BD4BA05B4E774	FASTA	601	63,485
	10 20 30 40 50 60 MNASGTFFFV VGPSGAGKDA LMDGARAALD DNYVFARRVI TRPEGAVGEA HEAVSEAEFA 70 80 90 100 110 120 RRQRSGEFLV TWDAHDLRYG LPCSLMSELE RGRHVVANGS RAVIAELAQR LPRFVVVLVT 130 140 150 160 170 180 APQDVLARRI AARGRESGEQ IARRVARTGA ALPPEVRCLT VLNDSTLEVG RARFVEALRH 190 200 210 220 230 240 GTRVASDGAP ASRTNLMAKL RGEPLDQAAY VAVLQDAMAG RYTEAELTEF LVAATRSLDD 250 260 270 280 290 300 QEVVALARAR TVFTPRIKWD EPIVVDKHSI GGVPGSRITL IVVPIVAAYG LAMPKTSSRA 310 320 330 340 350 360 ITSAAGTADA METVARVDLA HDDVRRCVAQ ARACIAWNGR LNHSVVDDVM NAITRPLRLD 370 380 390 400 410 420 SRRWAVASIL SKKYTAGATH VIVDLPYGPQ TKLATRADAE ALGAMFEHVG KGLGLHVRAL 430 440 450 460 470 480 VTDGSRPIGR GIGPALEVRD VRQVLANDPC APADLREKAL RFAGEIIAFD ARVGSPAEGL 490 500 510 520 530 540 RIATALLSEG KAKAAFDRIA ATQGARPEPV APGAHTCVVS ATMQGRVAAI DGLRISGVAR 550 560 570 580 590 600 AAGAPRELGA GVDLLCTIGA KVESGQPLYR IHAGSDAALA AAAALARAGG ECSEAVRIDP D

References

[1]

"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia." Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C. Genome Res. 18:1472-1483(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: R1 / LMG 19424.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU633750 Genomic DNA. Translation: CAP63552.1.
RefSeq	YP_001796789.1. NC_010530.1.
3D structure databases
ProteinModelPortal	B2AIF3.
ModBase	Search...
Protein-protein interaction databases
STRING	164546.RALTA_B0356.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAP63552; CAP63552; RALTA_B0356.
GeneID	6302658.
KEGG	cti:RALTA_B0356.
PATRIC	21534507. VBICupTai42494_3868.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0213.
HOGENOM	HOG000252767.
KO	K00758.
OMA	VGDHFGI.
ProtClustDB	PRK04350.
Enzyme and pathway databases
BioCyc	CTAI164546:GJNE-3573-MONOMER.
UniPathway	UPA00087; UER00175.
Family and domain databases
Gene3D	3.40.1030.10. 1 hit. 3.90.1170.30. 1 hit.
HAMAP	MF_00703. Thymid_phosp_2. Fused. MF_00836. PhnN. Fused.
InterPro	IPR000312. Glycosyl_Trfase_fam3. IPR008145. Guanylate_kin/L-typ_Ca_channel. IPR012699. PhnN. IPR013102. PYNP_C. IPR000053. Pyrmidine_PPase. IPR017872. Pyrmidine_PPase_CS. IPR013466. Thymidine_Pase_type2. [Graphical view]
PANTHER	PTHR10515. PTHR10515. 1 hit.
Pfam	PF00591. Glycos_transf_3. 1 hit. PF07831. PYNP_C. 1 hit. [Graphical view]
SMART	SM00072. GuKc. 1 hit. SM00941. PYNP_C. 1 hit. [Graphical view]
SUPFAM	SSF52418. Glyco_trans_3. 1 hit. SSF54680. PYNP_C. 1 hit.
TIGRFAMs	TIGR02322. phosphon_PhnN. 1 hit.
PROSITE	PS50052. GUANYLATE_KINASE_2. False negative. PS00647. THYMID_PHOSPHORYLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBKTP_CUPTR

Accession

Primary (citable) accession number: B2AIF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program