P84142 (ACYP_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acylphosphatase
EC=3.6.1.7

Alternative name(s):
Acylphosphate phosphohydrolase

Gene names

Name:	acyP
Ordered Locus Names:	PH0305.1

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	91 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	An acylphosphate + H2O = a carboxylate + phosphate. HAMAP MF_01450
Subunit structure	Monomer. Ref.4
Sequence similarities	Belongs to the acylphosphatase family. Contains 1 acylphosphatase-like domain.
Biophysicochemical properties	Kinetic parameters: KM=0.12 mM for benzoylphosphate at 25 degrees Celsius Ref.4 pH dependence: Optimum pH is 5.3 at 25 degrees Celsius. Temperature dependence: Optimum temperature is 98 degrees Celsius. Poorly active at 25 degrees Celsius. Thermostable up to 100 degrees Celsius.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Molecular function	acylphosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 91

91

Acylphosphatase HAMAP MF_01450

PRO_0000158560

Regions

Domain

5 – 91

87

Acylphosphatase-like

Sites

Active site

20

1

Active site

38

1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

91

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Beta strand

15 – 18

4

Helix

19 – 30

12

Beta strand

33 – 38

6

Beta strand

44 – 51

8

Helix

52 – 61

10

Turn

62 – 64

3

Beta strand

70 – 79

10

Sequences

	Sequence		Length	Mass (Da)
	P84142 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 6DDB6B69DBA17087	FASTA	91	10,260
	10 20 30 40 50 60 MAIVRAHLKI YGRVQGVGFR WSMQREARKL GVNGWVRNLP DGSVEAVLEG DEERVEALIG 70 80 90 WAHQGPPLAR VTRVEVKWEQ PKGEKGFRIV G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]	"Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii." Cheung Y.-Y., Allen M.D., Bycroft M., Wong K.-B. Acta Crystallogr. D 60:1308-1310(2004) [PubMed: 15213401] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[3]	"Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3." Miyazono K.I., Kudo N., Tanokura M. Acta Crystallogr. D 60:1135-1136(2004) [PubMed: 15159579] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
[4]	"Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii -- structural insights into enzymatic catalysis, thermostability, and dimerization." Cheung Y.-Y., Lam S.Y., Chu W.-K., Allen M.D., Bycroft M., Wong K.-B. Biochemistry 44:4601-4611(2005) [PubMed: 15779887] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), MASS SPECTROMETRY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. No translation available.

RefSeq

NP_142291.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V3Z	X-ray	1.72	A/B	1-91	[»]
1W2I	X-ray	1.50	A/B	1-91	[»]
2W4D	X-ray	2.40	A/B/C/D/E/F	2-90	[»]

ProteinModelPortal

P84142.

SMR

P84142. Positions 2-91.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001866; EBPYRP00000001866; EBPYRG00000001866.

GeneID

1444186.

GenomeReviews

Gene locus PH0305.1 in contig BA000001_GR.

NMPDR

fig|70601.1.peg.286.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022948.

HOGENOM

HBG750266.

OMA

ALIGWAH.

PhylomeDB

P84142.

Family and domain databases

HAMAP

MF_01450. Acylphosphatase.
[Tree]

InterPro

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

Pfam

PF00708. Acylphosphatase. 1 hit.
[Graphical view]

PRINTS

PR00112. ACYLPHPHTASE.

SUPFAM

SSF54975. Acylphosphatase. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

ACYP_PYRHO

Accession

Primary (citable) accession number: P84142

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	September 13, 2004
Last modified:	December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program