Enzyme

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EC Tree
     6. Ligases
        6.2 Forming carbon-sulfur bonds
            6.2.1 Acid-thiol ligases
ID:6.2.1.32
Description:Anthranilate--CoA ligase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.2.1.32
BRENDA Enzyme Link: BRENDA 6.2.1.32
KEGG Enzyme Link: KEGG6.2.1.32
BioCyc Enzyme Link: BioCyc 6.2.1.32
ExPASy Enzyme Link: ExPASy6.2.1.32
EC2PDB Enzyme Link: EC2PDB 6.2.1.32
ExplorEnz Enzyme Link: ExplorEnz 6.2.1.32
PRIAM enzyme-specific profiles Link: PRIAM 6.2.1.32
IntEnz Enzyme Link: IntEnz 6.2.1.32
MEDLINE Enzyme Link: MEDLINE 6.2.1.32
MSA:

6.2.1.32;

Phylogenetic Tree:

6.2.1.32;

Uniprot:
M-CSA:
RHEA:10828 anthranilate + ATP + CoA = AMP + anthraniloyl-CoA + diphosphate
RULE(radius=1) [*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]-[SH;+0:8].[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]>>[*:6]-[OH;+0:5].[*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[OH;+0:12].[*:7]-[S;H0;+0:8]-[C;H0;+0:10](=[*:9])-[*:11]
Reaction
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References

TitleAuthorsDatePubMed ID
Evidence that enzymes of a novel aerobic 2-amino-benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid.Altenschmidt U, Eckerskorn C, Fuchs G1990 Dec 122176602
Purification and characterization of benzoate-coenzyme A ligase and 2-aminobenzoate-coenzyme A ligases from a denitrifying Pseudomonas sp.Altenschmidt U, Oswald B, Fuchs G1991 Sep1885526
PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by Pseudomonas aeruginosa.Zhang YM, Frank MW, Zhu K, Mayasundari A, Rock CO2008 Oct 2418728009
Pseudomonas aeruginosa PqsA is an anthranilate-coenzyme A ligase.Coleman JP, Hudson LL, McKnight SL, Farrow JM 3rd, Calfee MW, Lindsey CA, Pesci EC2008 Feb18083812