P44684 (ADPP_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribose pyrophosphatase
EC=3.6.1.13

Alternative name(s):
ADP-ribose diphosphatase
ADP-ribose phosphohydrolase
Short name=ASPPase
Adenosine diphosphoribose pyrophosphatase
Short name=ADPR-PPase

Gene names

Name:	nudF
Ordered Locus Names:	HI_0398

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process By similarity.
Catalytic activity	ADP-ribose + H2O = AMP + D-ribose 5-phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Sequence similarities	Belongs to the Nudix hydrolase family. NudF subfamily. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 217	217	ADP-ribose pyrophosphatase		PRO_0000057045
Regions
	Domain	58 – 204	147	Nudix hydrolase
	Region	31 – 32	2	Substrate binding By similarity
	Region	54 – 55	2	Substrate binding; shared with dimeric partner By similarity
	Region	139 – 141	3	Substrate binding; shared with dimeric partner By similarity
	Motif	103 – 124	22	Nudix box
Sites
	Active site	168	1	Proton acceptor By similarity
	Metal binding	102	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	118	1	Magnesium 2 By similarity
	Metal binding	118	1	Magnesium 3 By similarity
	Metal binding	122	1	Magnesium 1 By similarity
	Metal binding	122	1	Magnesium 3 By similarity
	Metal binding	170	1	Magnesium 3 By similarity
	Binding site	82	1	Substrate By similarity
	Binding site	104	1	Substrate; via amide nitrogen By similarity
	Binding site	145	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44684 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 6040146E71ABD400	FASTA	217	24,580
	10 20 30 40 50 60 MQFWRKQMSE IQHFSQQDIE ILGEQTLYEG FFTLKRIQFK HKLFAGGQSG VVTRELLIKG 70 80 90 100 110 120 AASAVIAYDP KEDSVILVEQ VRIGAAYHPE SHRSPWLLEL IAGMVEKGEK PEDVALRESE 130 140 150 160 170 180 EEAGIQVKNL THCLSVWDSP GGIVERIHLF AGEVDSAQAK GIHGLAEENE DIKVHVVKRE 190 200 210 QAYQWMCEGK IDNGIAVIGL QWLQLNYAQL QQSWKRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance." Dunn C.A., O'Handley S.F., Frick D.N., Bessman M.J. J. Biol. Chem. 274:32318-32324(1999) [PubMed: 10542272] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22057.1.
PIR	B64151.
RefSeq	NP_438560.2. NC_000907.1.
3D structure databases
ProteinModelPortal	P44684.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	949499.
GenomeReviews	Gene locus HI_0398 in contig L42023_GR.
KEGG	hin:HI0398.
NMPDR	fig|71421.1.peg.373.
PATRIC	20189347. VBIHaeInf48452_0417.
TIGR	HI_0398.
Phylogenomic databases
HOGENOM	HBG692398.
OMA	LQWLELN.
ProtClustDB	CLSK870337.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0398-MONOMER.
Family and domain databases
InterPro	IPR004385. NDP_pyrophosphatase. IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KO	K01515.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
SUPFAM	SSF55811. NUDIX_hydrolase. 1 hit.
TIGRFAMs	TIGR00052. TIGR00052. 1 hit.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADPP_HAEIN

Accession

Primary (citable) accession number: P44684

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program