AERD_PLAAG
ID AERD_PLAAG Reviewed; 202 AA.
AC A0A073CEA3;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Prephenate decarboxylase {ECO:0000303|PubMed:20863139};
DE EC=4.1.1.100 {ECO:0000269|PubMed:20863139};
DE AltName: Full=Aeruginosin biosynthesis protein AerD {ECO:0000303|PubMed:20863139};
GN Name=aerD {ECO:0000303|PubMed:20863139}; ORFNames=A19Y_1631;
OS Planktothrix agardhii (Oscillatoria agardhii).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Planktothrix.
OX NCBI_TaxID=1160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8;
RX PubMed=24907328; DOI=10.1128/aem.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NIVA-CYA 126/8;
RX PubMed=17524987; DOI=10.1016/j.chembiol.2007.04.006;
RA Ishida K., Christiansen G., Yoshida W.Y., Kurmayer R., Welker M., Valls N.,
RA Bonjoch J., Hertweck C., Boerner T., Hemscheidt T., Dittmann E.;
RT "Biosynthesis and structure of aeruginoside 126A and 126B, cyanobacterial
RT peptide glycosides bearing a 2-carboxy-6-hydroxyoctahydroindole moiety.";
RL Chem. Biol. 14:565-576(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NIVA-CYA 126/8;
RX PubMed=20863139; DOI=10.1021/bi101457h;
RA Mahlstedt S., Fielding E.N., Moore B.S., Walsh C.T.;
RT "Prephenate decarboxylases: a new prephenate-utilizing enzyme family that
RT performs nonaromatizing decarboxylation en route to diverse secondary
RT metabolites.";
RL Biochemistry 49:9021-9023(2010).
CC -!- FUNCTION: In vivo, involved in the biosynthesis of 2-carboxy-6-
CC hydroxyoctahydroindole (Choi) present in the nonribosomal glycopeptides
CC aeruginoside 126A and B. AerD is an unusual prephenate decarboxylase
CC that avoids the typical aromatization of the cyclohexadienol ring of
CC prephenate. AerD catalyzes the protonation at C8 followed by
CC decarboxylation to produce the dihydro-4-hydroxyphenylpyruvate
CC regioisomer A258 (H2HPP A258)(3-(4-hydroxycyclohexa- 1,5-dienyl)-2-
CC oxopropanoic acid), which is able to undergo a nonenzymatic
CC isomerization to produce dihydro-4-hydroxyphenylpyruvate regioisomer
CC A295 (H2HPP A295)(3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoic
CC acid). {ECO:0000269|PubMed:17524987, ECO:0000269|PubMed:20863139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-
CC 2-oxopropanoate + CO2; Xref=Rhea:RHEA:33499, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:29934, ChEBI:CHEBI:84354;
CC EC=4.1.1.100; Evidence={ECO:0000269|PubMed:20863139};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=170 uM for prephenate {ECO:0000269|PubMed:20863139};
CC Note=kcat is 245 min(-1) for decarboxylase activity with prephenate
CC as substrate. {ECO:0000269|PubMed:20863139};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC aeruginoside 126A and B. {ECO:0000269|PubMed:17524987}.
CC -!- SIMILARITY: Belongs to the prephenate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CM002803; KEI66644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A073CEA3; -.
DR SMR; A0A073CEA3; -.
DR EnsemblBacteria; KEI66644; KEI66644; A19Y_1631.
DR PATRIC; fig|388467.6.peg.1566; -.
DR HOGENOM; CLU_109848_0_1_3; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Lyase.
FT CHAIN 1..202
FT /note="Prephenate decarboxylase"
FT /id="PRO_0000435423"
SQ SEQUENCE 202 AA; 23114 MW; 4C630F43ACE7CAB4 CRC64;
MLKFSMEFCY PQPDVKTLIV GTLGPKETSS EQTLNYLITQ WQAEQISVTS HLFDTFTELK
EALLQDRVDL ALVPHAYERV NDFYMEPSLK LGFVFTYPTP IYGLAKRKNE ELVWENCTLV
THPAPFPLLP YLLPGYPHQK NIKVEFVNST SAAAIQVKQG LADLAITNEN ALKENDLEFI
AEYGKIEMSW SIFHKKGTVH RE