EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR013200 HAD superfamily hydrolase-like, type 3

Protein matches Help

UniProtKB

Matches:

7145 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

IPR013200 HAD-SF_hydro-like_3

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF08282	Hydrolase_3	7145
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000150 Cof protein
IPR006379 HAD-superfamily hydrolase, subfamily IIB
IPR006381 HAD-superfamily hydrolase, superfamily IIB, YedP
IPR012815 Mannosyl-3-phosphoglycerate phosphatase-related
IPR017223 Uncharacterised conserved protein UCP037492, HAD, SPs0319

Contains

IPR010023 Phosphatase KdsC

InterPro annotation

Entry Details in BioMart

Abstract

The Haloacid Dehydrogenase (HAD) superfamily includes phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, which are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification [1]. This HAD domain is found in several distinct enzymes including:

Phospholipid-transporting ATPase 1 (EC:3.6.3.1), a putative lipid-flipping enzyme involved in cold tolerance in Arabidopsis [2]
3-deoxy-D-manno-octulosonate (KDO) 8-phosphate phosphatase (EC:3.1.3.45), which catalyses the final step in the biosynthesis of KDO - a component of lipopolysaccharide in Gram-negative bacteria [3]
Mannosyl-3-phosphoglycerate phosphatase (EC:3.1.3.70), which hydrolyzes mannosyl-3-phosphoglycerate to form the osmolyte mannosylglycerate [4]
Phosphoglycolate phopshatase (EC:3.1.3.18), which catalyses the dephosphorylation of 2-phosphoglycolate [5]

Structural links Help

PDB - click here

SCOP: c.108.1.10 , c.108.1.18

CATH: 3.30.1240.10 , 3.40.50.1000 , 3.90.1070.10

Database links Help

Enzyme: EC:3

Blocks: IPB013200

Pfam Clan: CL0137.11

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013200

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O07539 Stress response protein yhaX

O58690 Mannosyl-3-phosphoglycerate phosphatase

O94314 Uncharacterized hydrolase C215.10

P98204 Phospholipid-transporting ATPase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012813	Mannosyl-3-phosphoglycerate phosphatase
IPR018303	ATPase, P-type phosphorylation site
IPR001757	ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
IPR006539	ATPase, P-type, phospholipid-translocating, flippase
IPR005834	Haloacid dehalogenase-like hydrolase
IPR000150	Cof protein
IPR008250	ATPase, P-type, ATPase-associated domain
IPR006379	HAD-superfamily hydrolase, subfamily IIB
IPR006381	HAD-superfamily hydrolase, superfamily IIB, YedP
IPR013200	HAD superfamily hydrolase-like, type 3
	PDB Chain
	ModBase
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Koonin EV, Tatusov RL. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 244 125-32 1994 [PubMed: 7966317] http://dx.doi.org/10.1006/jmbi.1994.1711
2.	Gomes E, Jakobsen MK, Axelsen KB, Geisler M, Palmgren MG. Chilling tolerance in Arabidopsis involves ALA1, a member of a new family of putative aminophospholipid translocases. Plant Cell 12 2441-2454 2000 [PubMed: 11148289] http://dx.doi.org/10.1105/tpc.12.12.2441
3.	Wu J, Woodard RW. Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. J. Biol. Chem. 278 18117-23 2003 [PubMed: 12639950] http://dx.doi.org/10.1074/jbc.M301983200
4.	Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS. Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes. J. Biol. Chem. 276 43580-8 2001 [PubMed: 11562374] http://dx.doi.org/10.1074/jbc.M108054200
5.	Kim Y, Yakunin AF, Kuznetsova E, Xu X, Pennycooke M, Gu J, Cheung F, Proudfoot M, Arrowsmith CH, Joachimiak A, Edwards AM, Christendat D. Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum. J. Biol. Chem. 279 517-26 2004 [PubMed: 14555659] http://dx.doi.org/10.1074/jbc.M306054200

Additional Reading Open in usermanual
	Lu Z, Dunaway-Mariano D, Allen KN. The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state. Proc. Natl. Acad. Sci. U.S.A. 105 2008 5687-92 [PubMed: 18398008] http://dx.doi.org/10.1073/pnas.0710800105
	Lu Z, Dunaway-Mariano D, Allen KN. HAD superfamily phosphotransferase substrate diversification: structure and function analysis of HAD subclass IIB sugar phosphatase BT4131. Biochemistry 44 2005 8684-96 [PubMed: 15952775] http://dx.doi.org/10.1021/bi050009j
	Roberts A, Lee SY, McCullagh E, Silversmith RE, Wemmer DE. YbiV from Escherichia coli K12 is a HAD phosphatase. Proteins 58 2005 790-801 [PubMed: 15657928] http://dx.doi.org/10.1002/prot.20267
	Kawamura T, Watanabe N, Tanaka I. Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii. Acta Crystallogr. D Biol. Crystallogr. 64 2008 1267-76 [PubMed: 19018103] http://dx.doi.org/10.1107/S0907444908033817

InterPro 24.0