PHZD2_PSEAE
ID PHZD2_PSEAE Reviewed; 207 AA.
AC P0DPC1; O33409; Q7DC80;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Phenazine biosynthesis protein PhzD2 {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=phzD2 {ECO:0000303|PubMed:11591691}; Synonyms=phzD;
GN OrderedLocusNames=PA1902 {ECO:0000312|EMBL:AAG05291.1};
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 [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 [2]
RP 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 [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-38 IN
RP COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-38 AND LYS-122, ACTIVE
RP SITE, SUBUNIT, AND 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).
CC -!- FUNCTION: Involved in the biosynthesis of the antibiotic phenazine, a
CC nitrogen-containing heterocyclic molecule having important roles in
CC virulence, competition and biological control. PhzD2 (operon
CC phzA2B2C2E2F2G2) has a role in the biosynthesis of the phenazine during
CC both planktonic growth and biofilm development, and in host infection
CC during biofilm development (PubMed:23129634). Catalyzes the hydrolysis
CC of the vinyl ether functional group of 2-amino-2-deoxyisochorismate
CC (ADIC), yielding pyruvate and trans-2,3-dihydro-3-hydroxyanthranilic
CC acid (DHHA) (PubMed:23129634, PubMed:12741825). 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: In liquid cultures (aerobic), phz2 operon is induced by
CC quinolone signal via 2-heptyl-3-hydroxy-4-quinolone (PQS). In biofilm
CC (microaerobic), phz2 operon is induced by quinolone signal via 4-
CC hydroxy-2-heptylquinoline (HHQ), a precursor of PQS.
CC {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 this entry (AC
CC P0DPC1), because it is impossible to differentiate between the
CC duplicate which has been chosen for the study, and because PhzD2 (AC
CC P0DPC1) displays an important role in phenazine production and host
CC infection. {ECO:0000305}.
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DR EMBL; AE004091; AAG05291.1; -; Genomic_DNA.
DR PIR; H83407; H83407.
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 PDB; 1NF8; X-ray; 1.60 A; A=1-207.
DR PDB; 1NF9; X-ray; 1.50 A; A=1-207.
DR PDBsum; 1NF8; -.
DR PDBsum; 1NF9; -.
DR AlphaFoldDB; P0DPC1; -.
DR SMR; P0DPC1; -.
DR DNASU; 881873; -.
DR EnsemblBacteria; AAG05291; AAG05291; PA1902.
DR GeneID; 880504; -.
DR GeneID; 881873; -.
DR KEGG; pae:PA1902; -.
DR KEGG; pae:PA4213; -.
DR PseudoCAP; PA1902; -.
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 3D-structure; Antibiotic biosynthesis; Hydrolase; Reference proteome;
KW Virulence.
FT CHAIN 1..207
FT /note="Phenazine biosynthesis protein PhzD2"
FT /id="PRO_0000442351"
FT ACT_SITE 38
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12741825"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12741825,
FT ECO:0007744|PDB:1NF8, ECO:0007744|PDB:1NF9"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12741825,
FT ECO:0007744|PDB:1NF8, ECO:0007744|PDB:1NF9"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12741825,
FT ECO:0007744|PDB:1NF8"
FT BINDING 151..155
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12741825,
FT ECO:0007744|PDB:1NF8"
FT MUTAGEN 38
FT /note="D->A: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:12741825"
FT MUTAGEN 122
FT /note="K->A: Strong decrease of the catalytic efficiency
FT with 2-amino-2-deoxyisochorismate as substrate, but only
FT slight decrease with isochorismate."
FT /evidence="ECO:0000269|PubMed:12741825"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1NF9"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 49..69
FT /evidence="ECO:0007829|PDB:1NF9"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1NF9"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1NF9"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1NF9"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:1NF9"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1NF9"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1NF9"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:1NF9"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1NF9"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:1NF9"
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
