PHACS Protein Overview: Sequence, Structure, Function and Protein Interaction

PHACS Protein Overview

PHACS reagents

By searching EST databases for sequences similar to Fugu ACS, Peixoto et al. (2000) identified a partial human ACS clone in neuronal and fetal liver cDNA libraries. Fugu and human ACS share 53% amino acid identity overall, and the identity increases to 75% in the catalytic core region. By searching EST databases for sequences similar to plant ACSs, followed by 5-prime and 3-prime RACE of a prostate cDNA library, Koch et al. (2001) cloned human ACS, which they called PHACS (putative human ACS). The deduced 501-amino acid protein has a calculated molecular mass of 58 kD. Bioinformatic analysis indicated that PHACS is a member of the alpha family of pyridoxal-5-prime-phosphate enzymes. PHACS contains overlapping aminotransferase I and beta-eliminating lyase domains, and it shares structural similarity with aspartate aminotransferase (see 138180), tyrosine aminotransferase (613018), and enzymes that catalyze beta-elimination reactions on amino acids. Analysis of available ESTs suggested that PHACS is expressed in a wide range of tissues.

PHACS protein family

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

PHACS protein name

Recommended name
1-aminocyclopropane-1-carboxylate synthase-like protein 1
Aliases
ACS, PHACS

PHACS Protein Molecular Weight & PI

The parameters have been computed for the following feature

FT CHAIN 1-501 1-aminocyclopropane-1-carboxylate

Molecular weight (Da)

57323.52

Theoretical pI

6.01

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