B1XFJ3 (DEOB_ECODH) 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:	ECDH10B_4541

Organism

Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]

Taxonomic identifier

316385 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli › Escherichia coli (strain K12)

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.
Sequence similarities	Belongs to the phosphopentomutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Isomerase
PTM	Acetylation
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_1000133072
Sites
	Metal binding	10	1	Manganese By similarity
	Metal binding	311	1	Manganese By similarity
	Metal binding	347	1	Manganese By similarity
	Metal binding	348	1	Manganese By similarity
	Metal binding	359	1	Manganese By similarity
Amino acid modifications
	Modified residue	287	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1XFJ3 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 516F3018DC77A077	FASTA	407	44,370
	10 20 30 40 50 60 MKRAFIMVLD SFGIGATEDA ERFGDVGADT LGHIAEACAK GEADNGRKGP LNLPNLTRLG 70 80 90 100 110 120 LAKAHEGSTG FIPAGMDGNA EVIGAYAWAH EMSSGKDTPS GHWEIAGVPV LFEWGYFSDH 130 140 150 160 170 180 ENSFPQELLD KLVERANLPG YLGNCHSSGT VILDQLGEEH MKTGKPIFYT SADSVFQIAC 190 200 210 220 230 240 HEETFGLDKL YELCEIAREE LTNGGYNIGR VIARPFIGDK AGNFQRTGNR HDLAVEPPAP 250 260 270 280 290 300 TVLQKLVDEK HGQVVSVGKI ADIYANCGIT KKVKATGLDA LFDATIKEMK EAGDNTIVFT 310 320 330 340 350 360 NFVDFDSSWG HRRDVAGYAA GLELFDRRLP ELMSLLRDDD ILILTADHGC DPTWTGTDHT 370 380 390 400 REHIPVLVYG PKVKPGSLGH RETFADIGQT LAKYFGTSDM EYGKAMF

References

[1]

"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / DH10B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000948 Genomic DNA. Translation: ACB05311.1.
RefSeq	YP_001733089.1. NC_010473.1.
3D structure databases
ProteinModelPortal	B1XFJ3.
SMR	B1XFJ3. Positions 2-407.
ModBase	Search...
Protein-protein interaction databases
STRING	316385.ECDH10B_4541.
Proteomic databases
PRIDE	B1XFJ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB05311; ACB05311; ECDH10B_4541.
GeneID	6060377.
KEGG	ecd:ECDH10B_4541.
PATRIC	18469144. VBIEscCol59506_4588.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1015.
HOGENOM	HOG000008159.
KO	K01839.
OMA	PNMAKLG.
ProtClustDB	PRK05362.
Enzyme and pathway databases
BioCyc	ECOL316385:GJ8B-4337-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_ECODH

Accession

Primary (citable) accession number: B1XFJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program