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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
 
 
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