Top Level Name

  ⌊ Superfamily (extended) Pyruvoyl-Dependent Histidine/Arginine Decarboxylase

Family known
Total 100% <100% Family unknown
Functional domains 335 87 2 246
UniProtKB 593 111 2 480
GI 1521 303 6 1212
Structures 11
Reactions 0
Functional domains of this superfamily were last updated on June 17, 2017
New functional domains were last added to this superfamily on April 30, 2013

There are many non-homologous Pyruvoyl-dependent enzymes, all of which is translated as a proenzyme (pi chain) that undergoes an autocatalytic serinolysis reaction to form two polypeptide chains. By convention, the beta-chain represents the N-terminal fragment and the alpha-chain the larger, C-terminal fragment. The beta-chain terminates with a new carboxyl group formed after cleavage and the a chain begins with the pyruvoyl group. PvlArgDC shares very little appreciable sequence similarity to PvlHisDC, except for a region of 23 amino acids that is similar (nine of these are identical) to the cleavage site. Thus, these proteins have been proposed to be homologous based on this limited sequence conservation, and also the fact that they show a similar core topology in their crystal structures. The main differences are the result of several insertions in PvlHisDC relative to PvlArgDC accounting for about 130 additional amino acid residues.

Tolbert WD, Graham DE, White RH, Ealick SE

Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms

▸ Abstract

Structure 2003;11(3):285-294 | PubMed ID: 12623016

Gallagher T, Snell EE, Hackert ML

Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis.

▸ Abstract

J Biol Chem 1989;264(21):12737-12743 | PubMed ID: 2745463

Pishko EJ, Robertus JD

Site-directed alteration of three active-site residues of a pyruvoyl-dependent histidine decarboxylase

▸ Abstract

Biochemistry 1993;32(18):4943-4948 | PubMed ID: 8490030

van Poelje PD, Snell EE.

Pyruvoyl-dependent enzymes

▸ Abstract

Annu Rev Biochem 1990;59(None):29-59 | PubMed ID: 2197977

No notes.


Pyruvoyl group (Organic Cofactor (PTM))

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Sequence Similarity Networks

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Multiple Sequence Alignment

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Data Type All (#) Known (#) Unknown (#)
Full length FASTA (335) (89) (246)
Complete annotation (.tsv) (335) (89) (246)
Annotation suitable for Excel ® (.tsv) (335) (89) (246)
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Full length sequences in FASTA format.
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Sequences of the Functional Domain in FASTA format.
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Spreadsheet ready annotation
Annotation of sequences sets of this superfamily in a ͟Tab ͟Separated ͟Value (TSV) file. This file can be imported into a spreadsheet application. Cells which exceed the allowed spreadsheet maximum (32.5K) are preceded by the word "Truncated" and clipped short.
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