Q9VF36 (ACYP2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acylphosphatase-2
EC=3.6.1.7

Alternative name(s):
Acylphosphate phosphohydrolase 2
Short name=AcPDro2

Gene names

Name:	Acyp2
ORF Names:	CG18505

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	102 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	An acylphosphate + H2O = a carboxylate + phosphate. Ref.4
Sequence similarities	Belongs to the acylphosphatase family. Ref.4 Ref.5 Contains 1 acylphosphatase-like domain.
Biophysicochemical properties	Kinetic parameters: KM=0.80 mM for benzoylphosphate Ref.4 pH dependence: Optimum pH is 4.8-5.8. Ref.4
Mass spectrometry	Molecular mass is 11778 Da from positions 1 - 102. Determined by ESI. Ref.4

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular metabolic process Traceable author statement Ref.4. Source: UniProtKB
Cellular component	cytoplasm Traceable author statement Ref.4. Source: UniProtKB
Molecular function	acylphosphatase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 102

102

Acylphosphatase-2

PRO_0000158551

Regions

Domain

12 – 102

91

Acylphosphatase-like

Sites

Active site

27

1

Probable Ref.4

Active site

45

1

Probable Ref.4

Secondary structure

1

.

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.

.

102

Helix Strand Turn

Details...

Beta strand

10 – 20

11

Beta strand

22 – 25

4

Helix

26 – 37

12

Beta strand

40 – 45

6

Beta strand

51 – 57

7

Helix

59 – 71

13

Beta strand

78 – 84

7

Beta strand

88 – 92

5

Beta strand

96 – 100

5

Sequences

	Sequence		Length	Mass (Da)
	Q9VF36 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3CDC09E7FF96FBDE	FASTA	102	11,766
	10 20 30 40 50 60 MAGSGVAKQI FALDFEIFGR VQGVFFRKHT SHEAKRLGVR GWCMNTRDGT VKGQLEAPMM 70 80 90 100 NLMEMKHWLE NNRIPNAKVS KAEFSQIQEI EDYTFTSFDI KH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
[4]	"Characterization of a novel Drosophila melanogaster acylphosphatase." Degl'Innocenti D., Ramazzotti M., Marzocchini R., Chiti F., Raugei G., Ramponi G. FEBS Lett. 535:171-174(2003) [PubMed: 12560098] [Abstract] Cited for: CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase." Zuccotti S., Rosano C., Ramazzotti M., Degl'Innocenti D., Stefani M., Manao G., Bolognesi M. Acta Crystallogr. D 60:1177-1179(2004) [PubMed: 15159593] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), ACTIVE SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE014297 Genomic DNA. Translation: AAF55224.1.
BT024404 mRNA. Translation: ABC86466.1.

RefSeq

NP_650491.1. NM_142234.1.

UniGene

Dm.11656.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1URR	X-ray	1.50	A	1-102	[»]

ProteinModelPortal

Q9VF36.

SMR

Q9VF36. Positions 6-102.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9VF36.

Proteomic databases

PRIDE

Q9VF36.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0083174; FBpp0082628; FBgn0038363.

GeneID

41910.

KEGG

dme:Dmel_CG18505.

NMPDR

fig|7227.3.peg.13030.

Organism-specific databases

CTD

98.

FlyBase

FBgn0038363. Acyp2.

Phylogenomic databases

eggNOG

inNOG11458.

GeneTree

EMGT00050000016359.

InParanoid

Q9VF36.

OrthoDB

EOG4NZS9T.

PhylomeDB

Q9VF36.

Gene expression databases

Bgee

Q9VF36.

GermOnline

CG18505. Drosophila melanogaster.

Family and domain databases

InterPro

IPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like.
IPR017968. Acylphosphatase_CS.
[Graphical view]

KO

K01512.

Pfam

PF00708. Acylphosphatase. 1 hit.
[Graphical view]

PRINTS

PR00112. ACYLPHPHTASE.

SUPFAM

SSF54975. Acylphosphatase. 1 hit.

PROSITE

PS00150. ACYLPHOSPHATASE_1. 1 hit.
PS00151. ACYLPHOSPHATASE_2. False negative.
PS51160. ACYLPHOSPHATASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

826227.

Entry information

Entry name

ACYP2_DROME

Accession

Primary (citable) accession number: Q9VF36
Secondary accession number(s): Q29QI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project