1.3.99.36: cypemycin cysteine dehydrogenase (decarboxylating)

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For detailed information about cypemycin cysteine dehydrogenase (decarboxylating), go to the full flat file.

Reaction

Synonyms

CYPD, cypemycin decarboxylase, cypemycin dehydratase.

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.99 With unknown physiological acceptors

                1.3.99.36 cypemycin cysteine dehydrogenase (decarboxylating)

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Results

in table

3

AA Sequence

2

Cloned(Commentary)

5

Cofactor

1

Crystallization (Commentary)

2

Engineering

16

General Information

8

Natural Substrates/ Products (Substrates)

23

Organism

1

PDB ID

1

pH Optimum

2

Purification (Commentary)

1

Reaction

10

Reference

12

Substrates and Products (Substrate)

4

Subunits

16

Synonyms

1

Systematic Name

1

Temperature Optimum [�C]

Subunits

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Subunits on EC 1.3.99.36 - cypemycin cysteine dehydrogenase (decarboxylating)

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dodecamer

4 entries

dodecamer

Streptomyces coelicolor

-

a CypD monomer consists of a single classic Rossmann-fold domain, which is composed of a central beta-sheet formed by six parallel strands (labeled beta1-beta6) enclosed by eight alpha helices (labeled alpha1-alpha8). Residues that participate in forming the trimer (trimer contacts) are found in a region spanning alpha5 and alpha6, and a region containing alpha7 and a long loop in the terminus of alpha7, whereas interactions between trimers (dimer contacts) are found mainly within alpha1, and a region spanning alpha2 and alpha3

763030

dodecamer

Streptomyces coelicolor

-

each monomer consists of a classic Rossmann-fold domain. This domain is constructed by a central beta sheet consisting of six parallel strands, which are enclosed by eight alpha helices. A fragment spanning Asn156-Ala166 is not observed in the CypD structure, which is likely responsible in substrate binding

763314

dodecamer

Streptomyces coelicolor M1414

-

a CypD monomer consists of a single classic Rossmann-fold domain, which is composed of a central beta-sheet formed by six parallel strands (labeled beta1-beta6) enclosed by eight alpha helices (labeled alpha1-alpha8). Residues that participate in forming the trimer (trimer contacts) are found in a region spanning alpha5 and alpha6, and a region containing alpha7 and a long loop in the terminus of alpha7, whereas interactions between trimers (dimer contacts) are found mainly within alpha1, and a region spanning alpha2 and alpha3

-

dodecamer

Streptomyces coelicolor M1414

-

each monomer consists of a classic Rossmann-fold domain. This domain is constructed by a central beta sheet consisting of six parallel strands, which are enclosed by eight alpha helices. A fragment spanning Asn156-Ala166 is not observed in the CypD structure, which is likely responsible in substrate binding

-