Q5WYR0 (DEOB_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphopentomutase
EC=5.4.2.7

Alternative name(s):
Phosphodeoxyribomutase

Gene names

Name:	deoB
Ordered Locus Names:	lpl0676

Organism

Legionella pneumophila (strain Lens) [Complete proteome] [HAMAP]

Taxonomic identifier

297245 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella › Legionella pneumophila

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Phosphotransfer between the C1 and C5 carbon atoms of pentose By similarity. HAMAP-Rule MF_00740
Catalytic activity	Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. HAMAP-Rule MF_00740 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate. HAMAP-Rule MF_00740
Cofactor	Binds 1 or 2 manganese ions Potential.
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 1/3. HAMAP-Rule MF_00740
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00740.
Sequence similarities	Belongs to the phosphopentomutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cellular metabolic compound salvage Inferred from electronic annotation. Source: InterPro deoxyribonucleotide catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: HAMAP phosphopentomutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 407	407	Phosphopentomutase HAMAP-Rule MF_00740		PRO_0000258291
Sites
	Metal binding	11	1	Manganese By similarity
	Metal binding	310	1	Manganese By similarity
	Metal binding	346	1	Manganese By similarity
	Metal binding	347	1	Manganese By similarity
	Metal binding	358	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5WYR0 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: E8209170E1F3CCDA	FASTA	407	44,481
	10 20 30 40 50 60 MTGRICILVM DSFGIGASLD AARYGDAGAN TLVHIYEACK RGECDIEGAR KGPLMLPNLA 70 80 90 100 110 120 GKGLYHAAMA SSGLPFIDLA TLAIPSGYYG YAVEQSLGKD TPSGHWEMAG VPVTFEWGYF 130 140 150 160 170 180 PDKPYCFPEE LISEFIKQCN LPGVLGEKHA SGTIIMDELG EEHIRTGKPI VYTSADSVFQ 190 200 210 220 230 240 IAAHEEAFGL QRLYDICKIA RNLVDKYQIG RVIARPFTGK PGSFKRTGNR KDYATPPPEK 250 260 270 280 290 300 TLLDFLKEDG REVIAIGKIA DIYAHQGVTQ EIKADGNMAL FDATLSAMKT APQGSLVFTN 310 320 330 340 350 360 FVDFDSSYGH RRDIAGYAHA LEQFDARLPE LEVLLQPNDM VFIAADHGCD PTFPGSDHTR 370 380 390 400 EHIPVLVFGP QVNSKFIGRR DCFADIGQSI AEHLQLSSPL THGVSFL

References

[1]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Lens.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR628337 Genomic DNA. Translation: CAH14910.1.
RefSeq	YP_126038.1. NC_006369.1.
3D structure databases
ProteinModelPortal	Q5WYR0.
ModBase	Search...
Protein-protein interaction databases
STRING	297245.lpl0676.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAH14910; CAH14910; lpl0676.
GeneID	3113682.
KEGG	lpf:lpl0676.
PATRIC	22314897. VBILegPne33733_0783.
Organism-specific databases
LegioList	lpl0676.
CMR	Search...
Phylogenomic databases
eggNOG	COG1015.
HOGENOM	HOG000008159.
KO	K01839.
OMA	PNMAKLG.
ProtClustDB	PRK05362.
Enzyme and pathway databases
BioCyc	LPNE297245:GJD4-728-MONOMER.
UniPathway	UPA00087; UER00173.
Family and domain databases
Gene3D	3.30.70.1250. 1 hit. 3.40.720.10. 2 hits.
HAMAP	MF_00740. Phosphopentomut.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR010045. DeoB. IPR006124. Metalloenzyme. IPR024052. Phosphopentomutase_DeoB_cap. [Graphical view]
Pfam	PF01676. Metalloenzyme. 1 hit. [Graphical view]
PIRSF	PIRSF001491. Ppentomutase. 1 hit.
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit. SSF143856. SSF143856. 1 hit.
TIGRFAMs	TIGR01696. deoB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DEOB_LEGPL

Accession

Primary (citable) accession number: Q5WYR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	November 23, 2004
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program