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InterPro: IPR005834 Haloacid dehalogenase-like hydrolase

Protein matches Help

UniProtKB

Matches:

29201 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR005834 Dehalogen-like_hydro

Secondary

IPR001454

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00702	Hydrolase	29201
Signatures in BioMart

InterPro Relationships Help

Children

IPR006402 HAD-superfamily hydrolase, subfamily IA, variant 3
IPR006438 HAD-superfamily hydrolase, subfamily IA, hypothetical 1
IPR006545 EYA
IPR010041 2,3-diketo-5-methylthio-1-phosphopentane phosphatase

Found in

IPR000579 ATPase, P type cation-transporter
IPR000695 ATPase, P-type, H+ transporting proton pump
IPR001756 ATPase, P-type copper-transporter
IPR001757 ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
IPR004446 D,D-heptose 1,7-bisphosphate phosphatase
IPR005782 ATPase, P-type, calcium-transporting
IPR006328 Haloacid dehalogenase, type II
IPR006346 2-phosphoglycolate phosphatase, prokaryotic
IPR006349 2-phosphoglycolate phosphatase, eukaryotic
IPR006353 HAD-superfamily hydrolase, subfamily IIA, CECR5
IPR006354 HAD-superfamily hydrolase, subfamily IIA, hypothetical 1
IPR006355 HAD-superfamily hydrolase, subfamily IIA, hypothetical 2
IPR006356 HAD-superfamily hydrolase, subfamily IIA, hypothetical 3
IPR006357 HAD-superfamily hydrolase, subfamily IIA
IPR006385 HAD-superfamily hydrolase, subfamily IB, PSPase-like, bacterial
IPR006388 HAD-superfamily hydrolase, subfamily IA, variant 2
IPR006391 Potassium-transporting ATPase, B chain
IPR006403 ATPase, P type, cation/copper-transporter
IPR006404 ATPase, P-type, heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating
IPR006408 ATPase, P-type, calcium-transporting, PMCA-type
IPR006413 ATPase, P-type, calcium-transporting, PMR1-type
IPR006414 ATPase, P-type, potassium/sodium efflux, fungal
IPR006415 ATPase, P-type, magnesium-translocating
IPR006416 ATPase, P-type, heavy metal translocating
IPR006439 HAD-superfamily hydrolase, subfamily IA, variant 1
IPR006534 ATPase, P-type, plasma-membrane proton-efflux
IPR006539 ATPase, P-type, phospholipid-translocating, flippase
IPR006543 Histidinol-phosphate phosphatase
IPR006544 ATPase, P-type, unknown pump specificity (type V)
IPR006549 HAD-superfamily hydrolase, subfamily IIIA
IPR010021 HAD-superfamily phosphatase, subfamily IIIA
IPR011863 Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein
IPR011949 HAD-superfamily hydrolase, subfamily IA, REG-2-like
IPR011950 HAD-superfamily hydrolase, subfamily IA, CTE7
IPR011951 HAD-superfamily hydrolase, subfamily IA, YjjG/YfnB
IPR014098 Phenylphosphate carboxylase, delta subunit

Contains

IPR018303 ATPase, P-type phosphorylation site

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

This group of hydrolase enzymes is structurally different from the alpha/beta hydrolase family (abhydrolase). This group includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of HAD1_PSESP. The rest of the fold is composed of the core alpha/beta domain.

Structural links Help

PDB - click here

SCOP: c.108.1.1 , c.108.1.10 , c.108.1.11 , c.108.1.14 , c.108.1.19 , c.108.1.2 , c.108.1.22 , c.108.1.3 , c.108.1.4 , c.108.1.5 , c.108.1.6 , c.108.1.7 , d.220.1.1

CATH: 1.10.150.210 , 1.10.150.240 , 1.10.164.10 , 3.30.1240.10 , 3.40.1110.10 , 3.40.50.1000 , 3.40.50.10410 , 3.90.1070.10 , 3.90.1470.10

Database links Help

Enzyme: EC:3

PANDIT: PF00702

Pfam Clan: CL0137.11

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005834

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00167 Eyes absent homolog 2

P13607 Sodium/potassium-transporting ATPase subunit alpha

P32626 Enolase-phosphatase E1

P34492 Putative NipSnap protein K02D10.1

P34914 Epoxide hydrolase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006439	HAD-superfamily hydrolase, subfamily IA, variant 1
IPR006402	HAD-superfamily hydrolase, subfamily IA, variant 3
IPR012577	NIPSNAP
IPR006068	ATPase, P-type cation-transporter, C-terminal
IPR004014	ATPase, P-type cation-transporter, N-terminal
IPR006357	HAD-superfamily hydrolase, subfamily IIA
IPR010041	2,3-diketo-5-methylthio-1-phosphopentane phosphatase
IPR006069	ATPase, P-type cation exchange, alpha subunit
IPR018303	ATPase, P-type phosphorylation site
IPR006545	EYA
IPR006349	2-phosphoglycolate phosphatase, eukaryotic
IPR001757	ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
IPR000639	Epoxide hydrolase-like
IPR005834	Haloacid dehalogenase-like hydrolase
IPR005775	ATPase, P-type cation exchange, alpha subunit, eukaryotic
IPR008250	ATPase, P-type, ATPase-associated domain
IPR000073	Alpha/beta hydrolase fold-1
	PDB Chain
	ModBase
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K. Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold. J. Biol. Chem. 271 1996 20322-30 [PubMed: 8702766] http://dx.doi.org/10.1074/jbc.271.34.20322
	Toyoshima C, Norimatsu Y, Iwasawa S, Tsuda T, Ogawa H. How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Proc. Natl. Acad. Sci. U.S.A. 104 2007 19831-6 [PubMed: 18077416] http://dx.doi.org/10.1073/pnas.0709978104
	Takahashi M, Kondou Y, Toyoshima C. Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors. Proc. Natl. Acad. Sci. U.S.A. 104 2007 5800-5 [PubMed: 17389383] http://dx.doi.org/10.1073/pnas.0700979104
	Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK. Structural genomics of protein phosphatases. J. Struct. Funct. Genomics 8 2007 121-40 [PubMed: 18058037] http://dx.doi.org/10.1007/s10969-007-9036-1
	Olesen C, Picard M, Winther AM, Gyrup C, Morth JP, Oxvig C, Moller JV, Nissen P. The structural basis of calcium transport by the calcium pump. Nature 450 2007 1036-42 [PubMed: 18075584] http://dx.doi.org/10.1038/nature06418
	Yamamoto H, Takio K, Sugahara M, Kunishima N. Structure of a haloacid dehalogenase superfamily phosphatase PH1421 from Pyrococcus horikoshii OT3: oligomeric state and thermoadaptation mechanism. Acta Crystallogr. D Biol. Crystallogr. 64 2008 1068-77 [PubMed: 18931414] http://dx.doi.org/10.1107/S0907444908025948

InterPro 23.1