PHZD_PSEFL
ID PHZD_PSEFL Reviewed; 207 AA.
AC Q51790;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Phenazine biosynthesis protein PhzD {ECO:0000303|PubMed:9573209};
DE AltName: Full=2-amino-4-deoxychorismate hydrolase {ECO:0000303|PubMed:21454481};
DE EC=3.3.2.15 {ECO:0000269|PubMed:21454481};
DE AltName: Full=Trans-2,3-dihydro-3-hydroxyanthranilic acid synthase {ECO:0000305};
GN Name=phzD {ECO:0000303|PubMed:9573209};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=NRRL B-15132 / 2-79;
RX PubMed=9573209; DOI=10.1128/jb.180.9.2541-2548.1998;
RA Mavrodi D.V., Ksenzenko V.N., Bonsall R.F., Cook R.J., Boronin A.M.,
RA Thomashow L.S.;
RT "A seven-gene locus for synthesis of phenazine-1-carboxylic acid by
RT Pseudomonas fluorescens 2-79.";
RL J. Bacteriol. 180:2541-2548(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT ALA-38 IN COMPLEX WITH
RP SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-38, ACTIVE
RP SITE, AND SUBUNIT.
RC STRAIN=NRRL B-15132 / 2-79;
RX PubMed=21454481; DOI=10.1074/jbc.m110.183418;
RA Li Q.A., Mavrodi D.V., Thomashow L.S., Roessle M., Blankenfeldt W.;
RT "Ligand binding induces an ammonia channel in 2-amino-2-desoxyisochorismate
RT (ADIC) synthase PhzE.";
RL J. Biol. Chem. 286:18213-18221(2011).
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. 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). {ECO:0000269|PubMed:21454481, ECO:0000305|PubMed:9573209}.
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:21454481};
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC {ECO:0000305|PubMed:9573209}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:21454481}.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR EMBL; L48616; AAC18903.1; -; Genomic_DNA.
DR RefSeq; WP_043050173.1; NZ_JXCQ01000041.1.
DR PDB; 3R77; X-ray; 1.90 A; A/B=1-207.
DR PDBsum; 3R77; -.
DR AlphaFoldDB; Q51790; -.
DR SMR; Q51790; -.
DR BRENDA; 3.3.2.15; 5121.
DR BRENDA; 3.3.2.B1; 5121.
DR UniPathway; UPA00099; -.
DR GO; GO:0008908; F:isochorismatase activity; IEA:InterPro.
DR GO; GO:0002047; P:phenazine biosynthetic process; IEA:UniProtKB-UniPathway.
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; Virulence.
FT CHAIN 1..207
FT /note="Phenazine biosynthesis protein PhzD"
FT /id="PRO_0000201826"
FT ACT_SITE 38
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21454481"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21454481,
FT ECO:0007744|PDB:3R77"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21454481,
FT ECO:0007744|PDB:3R77"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21454481,
FT ECO:0007744|PDB:3R77"
FT BINDING 151..155
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21454481,
FT ECO:0007744|PDB:3R77"
FT MUTAGEN 38
FT /note="D->A: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:21454481"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3R77"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3R77"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 49..68
FT /evidence="ECO:0007829|PDB:3R77"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3R77"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3R77"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3R77"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:3R77"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:3R77"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:3R77"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:3R77"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3R77"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3R77"
SQ SEQUENCE 207 AA; 23074 MW; 4313D62FBBACAB03 CRC64;
MTGIPSIVPY ALPTSRDLPA NLAQWHIDPE RAVLLVHDMQ RYFLRPLPDA LRDQVVGNAA
RIRQWAADNG VPVAYTAQPG SMNEEQRGLL KDFWGPGMKA SPTDREVVDA LAPQPGDWLL
TKWRYSAFFN SDLLQRLHAS GRDQLILCGV YAHVGVLISS VDAYSNDIQP FLVADAIADF
SKEHHWMAME YAASRCAMVI TTDEVVL
