Enzyme

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     5. Isomerases
        5.3 Intramolecular oxidoreductases
            5.3.3 Transposing C=C bonds
ID:5.3.3.17
Description:Trans-2,3-dihydro-3-hydroxyanthranilate isomerase.
Cath: 3.10.310.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.3.3.17
BRENDA Enzyme Link: BRENDA 5.3.3.17
KEGG Enzyme Link: KEGG5.3.3.17
BioCyc Enzyme Link: BioCyc 5.3.3.17
ExPASy Enzyme Link: ExPASy5.3.3.17
EC2PDB Enzyme Link: EC2PDB 5.3.3.17
ExplorEnz Enzyme Link: ExplorEnz 5.3.3.17
PRIAM enzyme-specific profiles Link: PRIAM 5.3.3.17
IntEnz Enzyme Link: IntEnz 5.3.3.17
MEDLINE Enzyme Link: MEDLINE 5.3.3.17
MSA:

5.3.3.17;

Phylogenetic Tree:

5.3.3.17;

Uniprot:
M-CSA:
RHEA:28182 (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxyate = (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[CH;+0:4]=[CH;+0:5]-[CH;+0:6](-[OH;+0:7])-[*:8]-1>>[*:1]-[CH;+0:2]1-[*:8]-[C;H0;+0:6](=[O;H0;+0:7])-[CH2;+0:5]-[CH;+0:4]=[CH;+0:3]-1
Reaction
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References

TitleAuthorsDatePubMed ID
PhzA/B catalyzes the formation of the tricycle in phenazine biosynthesis.Ahuja EG, Janning P, Mentel M, Graebsch A, Breinbauer R, Hiller W, Costisella B, Thomashow LS, Mavrodi DV, Blankenfeldt W2008 Dec 1719053436
Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens.Blankenfeldt W, Kuzin AP, Skarina T, Korniyenko Y, Tong L, Bayer P, Janning P, Thomashow LS, Mavrodi DV2004 Nov 2315545603
Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79.Parsons JF, Song F, Parsons L, Calabrese K, Eisenstein E, Ladner JE2004 Oct 515449932