Protein Family Models for Protein (Select 489145671) - Protein Family Models - NCBI

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Items: 11

Select item 4230161.

HAD hydrolase-like protein

Date:: 2024-08-14

Family Accession:: NF024639.5
Method:: HMM

Select item 4220682.

HAD hydrolase-like protein

Date:: 2024-08-14

Family Accession:: NF024811.5
Method:: HMM

Select item 4112293.

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

Select item 3999504.

new record, indexing in progress

Family Accession:

Select item 3993475.

new record, indexing in progress

Family Accession:

Select item 3892226.

new record, indexing in progress

Family Accession:

Select item 3587837.

new record, indexing in progress

Family Accession:

Select item 3577188.

new record, indexing in progress

Family Accession:

Select item 3469839.

new record, indexing in progress

Family Accession:

Select item 14159110.

HAD-IA family hydrolase

This HMM represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs [PMID:7966317]. The subfamilies are defined [PMID:11601995] based on the location and the observed or predicted fold of a so-called "capping domain" [PMID:10956028], or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.

GO Terms:

Biological Process:: metabolic process (GO:0008152)

Molecular Function:: hydrolase activity (GO:0016787)

Date:: 2021-04-27

Family Accession:: TIGR01549.1
Method:: HMM

Select item 5228711.

HAD family hydrolase

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Date:: 2024-05-13

Family Accession:: 11436852
Method:: Sparcle

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