Haloacid dehydrogenase superfamily

Last updated
Hydrolase_3
PDB 1rkq EBI.jpg
crystal structure of had-like phosphatase yida from e. coli
Identifiers
SymbolHydrolase_3
Pfam PF08282
Pfam clan CL0137
ECOD 2006.1.1
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The haloacid dehydrogenase superfamily (HAD superfamily) is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification. [1]

Examples

A HAD domain is found in several distinct proteins including:

Human genes encoding proteins that contain this domain include:

Related Research Articles

<span class="mw-page-title-main">Phosphoglycerate mutase</span> Class of enzymes

Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis - the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase.

The crotonase family comprises mechanistically diverse proteins that share a conserved trimeric quaternary structure, the core of which consists of 4 turns of a (beta/beta/alpha)n superhelix.

The enzyme 3-deoxy-manno-octulosonate-8-phosphatase (EC 3.1.3.45) catalyzes the reaction

The enzyme mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) catalyzes the reaction

In enzymology, a 3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-deoxy-manno-octulosonate cytidylyltransferase is an enzyme that catalyzes the chemical reaction

UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) (EC 1.1.1.305, UDP-GlcUA decarboxylase, ArnADH) is an enzyme with systematic name UDP-glucuronate:NAD+ oxidoreductase (decarboxylating). This enzyme catalyses the following chemical reaction

Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase is an enzyme with systematic name dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha- )-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase. This enzyme catalyses the following chemical reaction

Mannosylglycerate synthase is an enzyme with systematic name GDP-mannose:D-glycerate 2-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction

Lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase is an enzyme with systematic name 4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans, octacis-undecaprenyl phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase. This enzyme catalyses the following chemical reaction

Lipid IVA 3-deoxy-D-manno-octulosonic acid transferase is an enzyme with systematic name CMP-3-deoxy-D-manno-oct-2-ulosonate:lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase. This enzyme catalyses the following chemical reaction

(KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase is an enzyme with systematic name CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase. This enzyme catalyses the following chemical reaction

Quinolinate synthase (EC 2.5.1.72, NadA, QS, quinolinate synthetase) is an enzyme with systematic name glycerone phosphate:iminosuccinate alkyltransferase (cyclizing). This enzyme catalyses the following chemical reaction

DTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase is an enzyme with systematic name dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase is an enzyme with systematic name UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

3-deoxy-D-manno-octulosonic acid kinase is an enzyme with systematic name ATP:(KDO)-lipid IVA 3-deoxy-alpha-D-manno-oct-2-ulopyranose 4-phosphotransferase. This enzyme catalyses the following chemical reaction

D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase is an enzyme with systematic name GTP:D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase. This enzyme catalyses the following chemical reaction

Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase is an enzyme with systematic name UDP-4-amino-4-deoxy-alpha-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-alpha-L-arabinosyltransferase. This enzyme catalyses the following chemical reaction

Mannosylglycerate hydrolase (EC 3.2.1.170, 2-O-(6-phospho-mannosyl)-D-glycerate hydrolase, alpha-mannosidase, mngB (gene)) is an enzyme with systematic name 2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate acylhydrolase. This enzyme catalyses the following chemical reaction

D-sedoheptulose 7-phosphate isomerase is an enzyme with systematic name D-glycero-D-manno-heptose 7-phosphate aldose-ketose-isomerase. This enzyme catalyses the following chemical reaction

References

  1. Koonin EV, Tatusov RL (November 1994). "Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search". Journal of Molecular Biology. 244 (1): 125–32. doi:10.1006/jmbi.1994.1711. PMID   7966317.
  2. Gomès E, Jakobsen MK, Axelsen KB, Geisler M, Palmgren MG (December 2000). "Chilling tolerance in Arabidopsis involves ALA1, a member of a new family of putative aminophospholipid translocases". The Plant Cell. 12 (12): 2441–2454. doi:10.2307/3871240. JSTOR   3871240. PMC   102229 . PMID   11148289.
  3. Wu J, Woodard RW (May 2003). "Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase". The Journal of Biological Chemistry. 278 (20): 18117–23. doi: 10.1074/jbc.M301983200 . PMID   12639950.
  4. Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS (November 2001). "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes". The Journal of Biological Chemistry. 276 (47): 43580–8. doi: 10.1074/jbc.M108054200 . PMID   11562374.
  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 (January 2004). "Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum". The Journal of Biological Chemistry. 279 (1): 517–26. doi: 10.1074/jbc.M306054200 . PMC   2795321 . PMID   14555659.
This article incorporates text from the public domain Pfam and InterPro: IPR013200