KEGG ENZYME: 2.3.1.262

ENZYME: 2.3.1.262

Entry

EC 2.3.1.262                Enzyme

Name

anthraniloyl-CoA anthraniloyltransferase;
pqsD (gene name)

Class

Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups

Sysname

anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase

Reaction(IUBMB)

anthraniloyl-CoA + malonyl-CoA = (2-aminobenzoyl)acetyl-CoA + CoA + CO2 (overall reaction) [RN:R11588];
(1a) anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA [RN:R11586];
(1b) S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA = (2-aminobenzoyl)acetyl-CoA + CO2 + L-cysteinyl-[PqsD protein] [RN:R11587]

Reaction(KEGG)

R11586 R11587 R11588

Substrate

anthraniloyl-CoA [CPD:C02247];
malonyl-CoA [CPD:C00083];
L-cysteinyl-[PqsD protein];
S-anthraniloyl-L-cysteinyl-[PqsD protein]

Product

(2-aminobenzoyl)acetyl-CoA [CPD:C21452];
CoA [CPD:C00010];
CO2 [CPD:C00011];
S-anthraniloyl-L-cysteinyl-[PqsD protein];
L-cysteinyl-[PqsD protein]

Comment

The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thioesterase, is present, it removes the CoA moiety from the product, forming the stable (2-aminobenzoyl)acetate.

History

EC 2.3.1.262 created 2017

Pathway

ec00405

Phenazine biosynthesis

ec01110

Biosynthesis of secondary metabolites

Orthology

K18003

anthraniloyl-CoA anthraniloyltransferase

Genes

PAE:	PA0999(pqsD)

PAEV:

N297_1032(pqsD)

PAEI:

N296_1032(pqsD)

PAU:	PA14_51390(pqsD)

PAP:	PSPA7_4399(fabH1)

PAG:	PLES_43261(pqsD)

PAF:	PAM18_4049(pqsD)

PNC:	NCGM2_1853(pqsD)

PAEB:

NCGM1900_1669(pqsD)

PDK:	PADK2_20745

PSG:	G655_20305

PRP:	M062_05445

PAEP:

PA1S_20975

PAER:

PA1R_gp4596

PAEM:

U769_20820

PAEL:

T223_22100

PAES:

SCV20265_4443

PAEU:

BN889_01051(pqsD)

PAEG:

AI22_12965

PAEC:

M802_1029(pqsD)

PAEO:

M801_1032(pqsD)

PPAA:

B7D75_20130

SECH:

B18_16625

AVM:	JQX13_30195

COY:	HF329_06225

» show all

Reference

1 [PMID:19694421]

Authors

Bera AK, Atanasova V, Robinson H, Eisenstein E, Coleman JP, Pesci EC, Parsons JF

Title

Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate.

Journal

Biochemistry 48:8644-55 (2009)
DOI:10.1021/bi9009055

Sequence

[pae:PA0999]

Reference

2 [PMID:24239007]

Authors

Dulcey CE, Dekimpe V, Fauvelle DA, Milot S, Groleau MC, Doucet N, Rahme LG, Lepine F, Deziel E

Title

The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids.

Journal

Chem Biol 20:1481-91 (2013)
DOI:10.1016/j.chembiol.2013.09.021

Reference

3 [PMID:25960261]

Authors

Drees SL, Fetzner S

Title

PqsE of Pseudomonas aeruginosa Acts as Pathway-Specific Thioesterase in the Biosynthesis of Alkylquinolone Signaling Molecules.

Journal

Chem Biol 22:611-8 (2015)
DOI:10.1016/j.chembiol.2015.04.012

Other DBs

ExplorEnz - The Enzyme Database:

2.3.1.262

IUBMB Enzyme Nomenclature:

2.3.1.262

ExPASy - ENZYME nomenclature database:

2.3.1.262

BRENDA, the Enzyme Database:

2.3.1.262

DBGET integrated database retrieval system