PHNB_PSEAE
ID PHNB_PSEAE Reviewed; 200 AA.
AC P09786;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Anthranilate synthase component 2, pyocyanine specific;
DE Short=AS;
DE Short=ASII;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase beta subunit, pyocyanine specific {ECO:0000303|PubMed:2153661};
DE AltName: Full=Anthranilate synthase, GATase component;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN Name=phnB {ECO:0000303|PubMed:3127654};
GN Synonyms=trpG {ECO:0000303|PubMed:3127654}; OrderedLocusNames=PA1002;
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], PROBABLE FUNCTION AS AN ANTHRANILATE
RP SYNTHASE, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, PA04290, and PAC174;
RX PubMed=2153661; DOI=10.1128/jb.172.2.884-900.1990;
RA Essar D.W., Eberly L., Hadero A., Crawford I.P.;
RT "Identification and characterization of genes for a second anthranilate
RT synthase in Pseudomonas aeruginosa: interchangeability of the two
RT anthranilate synthases and evolutionary implications.";
RL J. Bacteriol. 172:884-900(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAC174;
RX PubMed=3127654; DOI=10.1093/oxfordjournals.molbev.a040408;
RA Crawford I.P., Eberly L.;
RT "Structure and regulation of the anthranilate synthase genes in Pseudomonas
RT aeruginosa: I. Sequence of trpG encoding the glutamine amidotransferase
RT subunit.";
RL Mol. Biol. Evol. 3:436-448(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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 [4]
RP DISCUSSION OF FUNCTION.
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 [5]
RP FUNCTION IN PQS BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
RX PubMed=23449919; DOI=10.1099/mic.0.063065-0;
RA Palmer G.C., Jorth P.A., Whiteley M.;
RT "The role of two Pseudomonas aeruginosa anthranilate synthases in
RT tryptophan and quorum signal production.";
RL Microbiology 159:959-969(2013).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, a precursor for Pseudomonas
CC quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which
CC is required to induce the genes for the biosynthesis of the virulence
CC factor pyocyanine (PCN), a characteristic blue-green phenazine pigment
CC produced by P.aeruginosa (PubMed:11591691, PubMed:2153661,
CC PubMed:23449919). In the first step, the glutamine-binding beta subunit
CC (PhnB) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (PhnA) to produce anthranilate (By
CC similarity). {ECO:0000250|UniProtKB:P00900,
CC ECO:0000269|PubMed:11591691, ECO:0000269|PubMed:2153661,
CC ECO:0000269|PubMed:23449919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000305|PubMed:2153661};
CC -!- PATHWAY: Secondary metabolite biosynthesis; pyocyanine biosynthesis.
CC {ECO:0000305|PubMed:2153661}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (PhnB) and a large alpha subunit (PhnA).
CC {ECO:0000250|UniProtKB:P00900}.
CC -!- DISRUPTION PHENOTYPE: Single disruption in strain PA04290 results in
CC decreased pyocyanine synthesis (PubMed:2153661). Double phnA-phnB
CC deletions are tryptophan prototrophs; they make less PQS
CC (PubMed:23449919). {ECO:0000269|PubMed:2153661,
CC ECO:0000269|PubMed:23449919}.
CC -!- MISCELLANEOUS: PhnAB is not feedback inhibited by tryptophan.
CC {ECO:0000305|PubMed:2153661}.
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DR EMBL; M15733; AAA26018.1; -; Genomic_DNA.
DR EMBL; M33810; AAA88449.1; -; Genomic_DNA.
DR EMBL; M33811; AAA88452.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04391.1; -; Genomic_DNA.
DR PIR; B35116; B35116.
DR PIR; C83519; C83519.
DR RefSeq; NP_249693.1; NC_002516.2.
DR RefSeq; WP_003112548.1; NZ_QZGE01000006.1.
DR AlphaFoldDB; P09786; -.
DR SMR; P09786; -.
DR STRING; 287.DR97_944; -.
DR MEROPS; C26.960; -.
DR PaxDb; P09786; -.
DR PRIDE; P09786; -.
DR DNASU; 880689; -.
DR EnsemblBacteria; AAG04391; AAG04391; PA1002.
DR GeneID; 880689; -.
DR KEGG; pae:PA1002; -.
DR PATRIC; fig|208964.12.peg.1034; -.
DR PseudoCAP; PA1002; -.
DR HOGENOM; CLU_014340_1_0_6; -.
DR InParanoid; P09786; -.
DR OMA; HQVVIYR; -.
DR PhylomeDB; P09786; -.
DR BioCyc; MetaCyc:MON-16008; -.
DR BioCyc; PAER208964:G1FZ6-1021-MON; -.
DR BRENDA; 4.1.3.27; 5087.
DR UniPathway; UPA00235; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004049; F:anthranilate synthase activity; IMP:PseudoCAP.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0002047; P:phenazine biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Glutamine amidotransferase; Lyase; Reference proteome; Virulence.
FT CHAIN 1..200
FT /note="Anthranilate synthase component 2, pyocyanine
FT specific"
FT /id="PRO_0000056906"
FT DOMAIN 2..195
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 83
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 56..58
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 87
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 133..134
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT VARIANT 148..149
FT /note="DA -> ES (in strain: PAC174)"
FT /evidence="ECO:0000305"
FT VARIANT 195
FT /note="R -> A (in strain: PAC174)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="R -> A (in Ref. 1; AAA88449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 21845 MW; 9D9E218DDE8D7E30 CRC64;
MRITLLDNFD SFTYNLVEQF CLLGAEVRVM RNDTPLPTIQ AALLADGCEL LVLSPGPGRP
EDAGCMLELL AWARGRLPVL GVCLGHQALA LAAGGAVGEA RKPLHGKSTS LRFDQRHPLF
DGIADLRVAR YHSLVVSRLP EGFDCLADAD GEIMAMADPR NRQLGLQFHP ESILTTHGQR
LLENALLWCG ALAVRERLRA
