A9NG16 (DEOB_ACHLI) 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:	ACL_0680

Organism

Acholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]

Taxonomic identifier

441768 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma › Acholeplasma laidlawii

Protein attributes

Sequence length	397 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: UniProtKB-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: UniProtKB-HAMAP phosphopentomutase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 397	397	Phosphopentomutase HAMAP-Rule MF_00740		PRO_1000133054
Sites
	Metal binding	12	1	Manganese By similarity
	Metal binding	296	1	Manganese By similarity
	Metal binding	332	1	Manganese By similarity
	Metal binding	333	1	Manganese By similarity
	Metal binding	344	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9NG16 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 58CE487E95F8CB5C	FASTA	397	44,505
	10 20 30 40 50 60 MRFKRVFLIV MDSLGVGASE DANQYFNEGV DDTKANTFGH IAESMDLRIP NLEKLGVGNI 70 80 90 100 110 120 IPIKGTKSVE LSSSYVTKIR EKSLGKDTMT GHWEIMGLYV TTPFQTFTDT GFPKELLDEL 130 140 150 160 170 180 EERTGRKIIG NIAASGTEIL KDLGEEHMRT GDLIVYTSAD SVLQIAMHEE IIPIEEQYRI 190 200 210 220 230 240 SAIARDITMR PDWKVGRVIT RPFLGTNKDN FKRTSNRKDY ALKPSEETTL NFLSDANYDV 250 260 270 280 290 300 IALGKINDIF DGYGINKYSK TVSNDDGMKQ ITEWAKKDFT GLCFLNLVDF DALYGHRRDP 310 320 330 340 350 360 HGYGKAIMDM DSQLPELMAN LNEDDLLILT ADHGNDPTYV GTDHTREFVP MIAYSKSFKS 370 380 390 GGSLPILNTF ADLGSTISDN FKVKKTEHGD SFLSKLK

References

[1]

"Complete genome and proteome of Acholeplasma laidlawii." Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I. , Alexeev D.G., Ladygina V.G., Govorun V.M. J. Bacteriol. 193:4943-4953(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PG-8A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000896 Genomic DNA. Translation: ABX81296.1.
RefSeq	YP_001620672.1. NC_010163.1.
3D structure databases
ProteinModelPortal	A9NG16.
ModBase	Search...
Protein-protein interaction databases
STRING	441768.ACL_0680.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABX81296; ABX81296; ACL_0680.
GeneID	5803244.
KEGG	acl:ACL_0680.
PATRIC	20638080. VBIAchLai134690_0660.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1015.
HOGENOM	HOG000008159.
KO	K01839.
OMA	CHASGTE.
OrthoDB	EOG6R5C7J.
Enzyme and pathway databases
BioCyc	ALAI441768:GI40-680-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	SSF143856. SSF143856. 1 hit. SSF53649. SSF53649. 2 hits.
TIGRFAMs	TIGR01696. deoB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DEOB_ACHLI

Accession

Primary (citable) accession number: A9NG16

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 5, 2008
Last modified:	November 13, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program