The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily

Proteins: Structure, Function and Genetics

Volumn 42, Issue 2, 2001, Pages 230-236

  Horvath, Monica M ^b   Grishin, Nick V ^a,b  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Fold assignment; Molecular evolution; Protein structure classification; Rossmann fold; ThiJ protease

Indexed keywords

CATALASE; GLUTAMINE PHENYLPYRUVATE AMINOTRANSFERASE; PROTEINASE;

CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; EVOLUTION; MOLECULAR BIOLOGY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANTHRANILATE SYNTHASE; CATALASE; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; NITROGENOUS GROUP TRANSFERASES; PHYLOGENY; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0035254935     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0134(20010201)42:2<230::AID-PROT100>3.0.CO;2-J     Document Type: Conference Paper

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