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Links from Protein

Items: 11

1.

HAD hydrolase-like protein

Date:
2024-08-14
Family Accession:
NF024639.5
Method:
HMM
2.

Haloacid dehalogenase-like hydrolase

This family is part of the HAD superfamily. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024740.5
Method:
HMM
3.

HAD family hydrolase

This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family 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 Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2]. [1]. 8702766. 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. Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K;. J Biol Chem 1996;271:20322-20330. [2]. 20485265. A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4. Osman C, Haag M, Wieland FT, Brugger B, Langer T;. EMBO J. 2010;29:1976-1987 (from Pfam)

Date:
2024-10-16
Family Accession:
NF012905.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.

HAD family hydrolase

HAD (haloacid dehalogenase) family hydrolase belongs to a wider superfamily that includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Date:
2022-09-28
Family Accession:
11576378
Method:
Sparcle
10.

HAD-IIA family hydrolase

This HMM represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Class II consists of sequences in which the capping domain is found between the second and third motifs. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in Gram-positive bacteria and TIGR01459 in Gram-negative bacteria), and the Escherishia coli NagD gene and the Bacillus subtilus AraL proteins.

GO Terms:
Biological Process:
metabolic process (GO:0008152)
Molecular Function:
hydrolase activity (GO:0016787)
Date:
2021-04-27
Family Accession:
TIGR01460.1
Method:
HMM
11.

TIGR01459 family HAD-type hydrolase

This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily HMM)

Date:
2019-09-10
Family Accession:
TIGR01459.1
Method:
HMM
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