PHZD1_PSEAE
ID PHZD1_PSEAE Reviewed; 207 AA.
AC P0DPB9; O33409; Q7DC80;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Phenazine biosynthesis protein PhzD1 {ECO:0000303|PubMed:11591691};
DE AltName: Full=2-amino-4-deoxychorismate hydrolase {ECO:0000303|PubMed:12741825};
DE EC=3.3.2.15 {ECO:0000269|PubMed:12741825};
DE AltName: Full=Isochorismatase {ECO:0000303|PubMed:12741825};
DE AltName: Full=Trans-2,3-dihydro-3-hydroxyanthranilic acid synthase {ECO:0000305};
GN Name=phzD1 {ECO:0000303|PubMed:11591691}; Synonyms=phzD;
GN OrderedLocusNames=PA4213 {ECO:0000312|EMBL:AAG07600.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11591691; DOI=10.1128/jb.183.21.6454-6465.2001;
RA Mavrodi D.V., Bonsall R.F., Delaney S.M., Soule M.J., Phillips G.,
RA Thomashow L.S.;
RT "Functional analysis of genes for biosynthesis of pyocyanin and phenazine-
RT 1-carboxamide from Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 183:6454-6465(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000312|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP INDUCTION.
RX PubMed=11544214; DOI=10.1128/jb.183.19.5529-5534.2001;
RA Whiteley M., Greenberg E.P.;
RT "Promoter specificity elements in Pseudomonas aeruginosa quorum-sensing-
RT controlled genes.";
RL J. Bacteriol. 183:5529-5534(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=12741825; DOI=10.1021/bi027385d;
RA Parsons J.F., Calabrese K., Eisenstein E., Ladner J.E.;
RT "Structure and mechanism of Pseudomonas aeruginosa PhzD, an isochorismatase
RT from the phenazine biosynthetic pathway.";
RL Biochemistry 42:5684-5693(2003).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=23129634; DOI=10.1073/pnas.1213901109;
RA Recinos D.A., Sekedat M.D., Hernandez A., Cohen T.S., Sakhtah H.,
RA Prince A.S., Price-Whelan A., Dietrich L.E.;
RT "Redundant phenazine operons in Pseudomonas aeruginosa exhibit environment-
RT dependent expression and differential roles in pathogenicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19420-19425(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the antibiotic phenazine, a
CC nitrogen-containing heterocyclic molecule. PhzD1 (operon
CC phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during
CC planktonic growth (PubMed:23129634). Catalyzes the hydrolysis of the
CC vinyl ether functional group of 2-amino-2-deoxyisochorismate (ADIC),
CC yielding pyruvate and trans-2,3-dihydro-3-hydroxyanthranilic acid
CC (DHHA) (PubMed:12741825, PubMed:23129634). Also able to act on
CC isochorismate, chorismate and 4-amino-4-deoxychorismate (ADC) as
CC substrates (PubMed:12741825). {ECO:0000269|PubMed:12741825,
CC ECO:0000269|PubMed:23129634, ECO:0000305|PubMed:11591691}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-amino-4-deoxychorismate + H2O = (5S,6S)-6-amino-5-
CC hydroxycyclohexa-1,3-diene-1-carboxyate + pyruvate;
CC Xref=Rhea:RHEA:49456, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58792, ChEBI:CHEBI:60849; EC=3.3.2.15;
CC Evidence={ECO:0000269|PubMed:12741825};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for isochorismate {ECO:0000269|PubMed:12741825};
CC KM=68 uM for 2-amino-2-deoxyisochorismate
CC {ECO:0000269|PubMed:12741825};
CC KM=590 uM for 4-amino-4-deoxychorismate
CC {ECO:0000269|PubMed:12741825};
CC KM=983 uM for chorismate {ECO:0000269|PubMed:12741825};
CC Note=kcat is 7.3 sec(-1) with 2-amino-2-deoxyisochorismate as
CC substrate. kcat is 1.2 sec(-1) with chorismate as substrate. kcat is
CC 0.2 sec(-1) with isochorismate as substrate. kcat is 0.02 sec(-1)
CC with 4-amino-4-deoxychorismate as substrate.
CC {ECO:0000269|PubMed:12741825};
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC {ECO:0000305|PubMed:11591691}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12741825}.
CC -!- INDUCTION: Under control of LasR (PubMed:11544214). In liquid cultures
CC (aerobic), phz1 operon is induced by quinolone signal via 2-heptyl-3-
CC hydroxy-4-quinolone (PQS) (PubMed:23129634). In biofilm (microaerobic),
CC phz1 operon is not induced by PQS, because the biosynthesis of PQS by
CC the monooxygenase PqsH requires molecular oxygen (PubMed:23129634).
CC {ECO:0000269|PubMed:11544214, ECO:0000269|PubMed:23129634}.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is part of the operon phzABCDEFG
CC which is duplicated in P.aeruginosa. Cristallographic study
CC (PubMed:12741825) has been arbitrarily placed in PhzD2 (AC P0DPC1),
CC because it is impossible to differentiate between the duplicate which
CC has been chosen for the study, and because PhzD2 (AC P0DPC1) displays
CC an important role in phenazine production and host infection.
CC {ECO:0000305}.
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DR EMBL; AF005404; AAC64487.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07600.1; -; Genomic_DNA.
DR PIR; H83118; H83118.
DR RefSeq; NP_250593.1; NC_002516.2.
DR RefSeq; NP_252902.1; NC_002516.2.
DR RefSeq; WP_003093625.1; NZ_QZGE01000046.1.
DR AlphaFoldDB; P0DPB9; -.
DR SMR; P0DPB9; -.
DR STRING; 287.DR97_3698; -.
DR DNASU; 881873; -.
DR EnsemblBacteria; AAG07600; AAG07600; PA4213.
DR GeneID; 880504; -.
DR GeneID; 881873; -.
DR KEGG; pae:PA1902; -.
DR KEGG; pae:PA4213; -.
DR PseudoCAP; PA4213; -.
DR HOGENOM; CLU_068979_2_1_6; -.
DR OMA; RDIKPFF; -.
DR UniPathway; UPA00099; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008908; F:isochorismatase activity; IEA:InterPro.
DR GO; GO:0002047; P:phenazine biosynthetic process; IDA:PseudoCAP.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR016291; Isochorismatase.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR Pfam; PF00857; Isochorismatase; 1.
DR PIRSF; PIRSF001111; Isochorismatase; 1.
DR PRINTS; PR01398; ISCHRISMTASE.
DR SUPFAM; SSF52499; SSF52499; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Hydrolase; Reference proteome.
FT CHAIN 1..207
FT /note="Phenazine biosynthesis protein PhzD1"
FT /id="PRO_0000442350"
FT ACT_SITE 38
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0DPC1"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0DPC1"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0DPC1"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0DPC1"
FT BINDING 151..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0DPC1"
SQ SEQUENCE 207 AA; 23196 MW; 37F33F086022F527 CRC64;
MSGIPEITAY PLPTAQQLPA NLARWSLEPR RAVLLVHDMQ RYFLRPLPES LRAGLVANAA
RLRRWCVEQG VQIAYTAQPG SMTEEQRGLL KDFWGPGMRA SPADREVVEE LAPGPDDWLL
TKWRYSAFFH SDLLQRMRAA GRDQLVLCGV YAHVGVLIST VDAYSNDIQP FLVADAIADF
SEAHHRMALE YAASRCAMVV TTDEVLE
