PQSA_PSEAE
ID PQSA_PSEAE Reviewed; 517 AA.
AC Q9I4X3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Anthranilate--CoA ligase;
DE EC=6.2.1.32;
GN Name=pqsA; OrderedLocusNames=PA0996;
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;
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18083812; DOI=10.1128/jb.01140-07;
RA Coleman J.P., Hudson L.L., McKnight S.L., Farrow J.M. III, Calfee M.W.,
RA Lindsey C.A., Pesci E.C.;
RT "Pseudomonas aeruginosa PqsA is an anthranilate-coenzyme A ligase.";
RL J. Bacteriol. 190:1247-1255(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18728009; DOI=10.1074/jbc.m804555200;
RA Zhang Y.M., Frank M.W., Zhu K., Mayasundari A., Rock C.O.;
RT "PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an
RT extracellular metabolite produced by Pseudomonas aeruginosa.";
RL J. Biol. Chem. 283:28788-28794(2008).
CC -!- FUNCTION: Catalyzes the formation of anthraniloyl-CoA, which is the
CC priming step for entry into the Pseudomonas quinolone signal (PQS)
CC biosynthetic pathway. Also active on a variety of aromatic substrates,
CC including benzoate and chloro and fluoro derivatives of anthranilate.
CC {ECO:0000269|PubMed:18083812, ECO:0000269|PubMed:18728009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anthranilate + ATP + CoA = AMP + anthraniloyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:10828, ChEBI:CHEBI:16567,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57331, ChEBI:CHEBI:456215; EC=6.2.1.32;
CC Evidence={ECO:0000269|PubMed:18083812, ECO:0000269|PubMed:18728009};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for anthranilate {ECO:0000269|PubMed:18083812};
CC KM=22 uM for CoA {ECO:0000269|PubMed:18083812};
CC KM=71 uM for ATP {ECO:0000269|PubMed:18083812};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:18083812};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18083812}.
CC -!- DISRUPTION PHENOTYPE: Mutants show no detectable levels of 2,4-
CC dihydroxyquinoline (DHQ) or other quinolines.
CC {ECO:0000269|PubMed:18728009}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04385.1; -; Genomic_DNA.
DR PIR; G83521; G83521.
DR RefSeq; NP_249687.1; NC_002516.2.
DR RefSeq; WP_003112552.1; NZ_QZGE01000006.1.
DR PDB; 5OE3; X-ray; 1.43 A; A/B/C/D=1-399.
DR PDB; 5OE4; X-ray; 1.90 A; A/B=1-399.
DR PDB; 5OE5; X-ray; 1.74 A; A=1-399.
DR PDB; 5OE6; X-ray; 1.67 A; A/B/C/D=1-399.
DR PDBsum; 5OE3; -.
DR PDBsum; 5OE4; -.
DR PDBsum; 5OE5; -.
DR PDBsum; 5OE6; -.
DR AlphaFoldDB; Q9I4X3; -.
DR SMR; Q9I4X3; -.
DR STRING; 287.DR97_951; -.
DR BindingDB; Q9I4X3; -.
DR ChEMBL; CHEMBL4295626; -.
DR PaxDb; Q9I4X3; -.
DR PRIDE; Q9I4X3; -.
DR EnsemblBacteria; AAG04385; AAG04385; PA0996.
DR GeneID; 880760; -.
DR KEGG; pae:PA0996; -.
DR PATRIC; fig|208964.12.peg.1028; -.
DR PseudoCAP; PA0996; -.
DR HOGENOM; CLU_000022_59_10_6; -.
DR InParanoid; Q9I4X3; -.
DR OMA; PLRDYNA; -.
DR PhylomeDB; Q9I4X3; -.
DR BioCyc; MetaCyc:MON-16009; -.
DR BioCyc; PAER208964:G1FZ6-1015-MON; -.
DR BRENDA; 6.2.1.32; 5087.
DR PHI-base; PHI:3291; -.
DR PHI-base; PHI:5563; -.
DR PHI-base; PHI:5585; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016878; F:acid-thiol ligase activity; IBA:GO_Central.
DR GO; GO:0018860; F:anthranilate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..517
FT /note="Anthranilate--CoA ligase"
FT /id="PRO_0000418540"
FT BINDING 161..172
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:5OE6"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:5OE3"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:5OE5"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:5OE3"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:5OE3"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:5OE3"
SQ SEQUENCE 517 AA; 56608 MW; 8718FDEC315351F5 CRC64;
MSTLANLTEV LFRLDFDPDT AVYHYRGQTL SRLQCRTYIL SQASQLARLL KPGDRVVLAL
NDSPSLACLF LACIAVGAIP AVINPKSREQ ALADIAADCQ ASLVVREADA PSLSGPLAPL
TLRAAAGRPL LDDFSLDALV GPADLDWSAF HRQDPAAACF LQYTSGSTGA PKGVMHSLRN
TLGFCRAFAT ELLALQAGDR LYSIPKMFFG YGMGNSLFFP WFSGASALLD DTWPSPERVL
ENLVAFRPRV LFGVPAIYAS LRPQARELLS SVRLAFSAGS PLPRGEFEFW AAHGLEICDG
IGATEVGHVF LANRPGQARA DSTGLPLPGY ECRLVDREGH TIEEAGRQGV LLVRGPGLSP
GYWRASEEQQ ARFAGGWYRT GDLFERDESG AYRHCGREDD LFKVNGRWVV PTQVEQAICR
HLPEVSEAVL VPTCRLHDGL RPTLFVTLAT PLDDNQILLA QRIDQHLAEQ IPSHMLPSQL
HVLPALPRND NGKLARAELR HLADTLYHDN LPEERAC
