Q9I4X3 (PQSA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anthranilate--CoA ligase
EC=6.2.1.32

Gene names

Name:	pqsA
Ordered Locus Names:	PA0996

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of anthraniloyl-CoA, which is the priming step for entry into the Pseudomonas quinolone signal (PQS) biosynthetic pathway. Also active on a variety of aromatic substrates, including benzoate and chloro and fluoro derivatives of anthranilate. Ref.2 Ref.3
Catalytic activity	ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA. Ref.2 Ref.3
Subunit structure	Monomer. Ref.2
Disruption phenotype	Mutants show no detectable levels of 2,4-dihydroxyquinoline (DHQ) or other quinolines. Ref.3
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Biophysicochemical properties	Kinetic parameters: KM=3 µM for anthranilate Ref.2 KM=22 µM for CoA KM=71 µM for ATP pH dependence: Optimum pH is 8.5.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW anthranilate-CoA ligase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 517	517	Anthranilate--CoA ligase		PRO_0000418540
Regions
	Nucleotide binding	161 – 172	12	AMP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9I4X3 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 8718FDEC315351F5	FASTA	517	56,608
	10 20 30 40 50 60 MSTLANLTEV LFRLDFDPDT AVYHYRGQTL SRLQCRTYIL SQASQLARLL KPGDRVVLAL 70 80 90 100 110 120 NDSPSLACLF LACIAVGAIP AVINPKSREQ ALADIAADCQ ASLVVREADA PSLSGPLAPL 130 140 150 160 170 180 TLRAAAGRPL LDDFSLDALV GPADLDWSAF HRQDPAAACF LQYTSGSTGA PKGVMHSLRN 190 200 210 220 230 240 TLGFCRAFAT ELLALQAGDR LYSIPKMFFG YGMGNSLFFP WFSGASALLD DTWPSPERVL 250 260 270 280 290 300 ENLVAFRPRV LFGVPAIYAS LRPQARELLS SVRLAFSAGS PLPRGEFEFW AAHGLEICDG 310 320 330 340 350 360 IGATEVGHVF LANRPGQARA DSTGLPLPGY ECRLVDREGH TIEEAGRQGV LLVRGPGLSP 370 380 390 400 410 420 GYWRASEEQQ ARFAGGWYRT GDLFERDESG AYRHCGREDD LFKVNGRWVV PTQVEQAICR 430 440 450 460 470 480 HLPEVSEAVL VPTCRLHDGL RPTLFVTLAT PLDDNQILLA QRIDQHLAEQ IPSHMLPSQL 490 500 510 HVLPALPRND NGKLARAELR HLADTLYHDN LPEERAC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]	"Pseudomonas aeruginosa PqsA is an anthranilate-coenzyme A ligase." Coleman J.P., Hudson L.L., McKnight S.L., Farrow J.M. III, Calfee M.W., Lindsey C.A., Pesci E.C. J. Bacteriol. 190:1247-1255(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]	"PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by Pseudomonas aeruginosa." Zhang Y.M., Frank M.W., Zhu K., Mayasundari A., Rock C.O. J. Biol. Chem. 283:28788-28794(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004091 Genomic DNA. Translation: AAG04385.1.
PIR	G83521.
RefSeq	NP_249687.1. NC_002516.2.
3D structure databases
ProteinModelPortal	Q9I4X3.
SMR	Q9I4X3. Positions 5-506.
ModBase	Search...
Protein-protein interaction databases
STRING	208964.PA0996.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	880760.
KEGG	pae:PA0996.
PATRIC	19836282. VBIPseAer58763_1028.
Organism-specific databases
PseudoCAP	PA0996.
Phylogenomic databases
HOGENOM	HOG000229998.
OMA	PRNDNGK.
ProtClustDB	CLSK866268.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16009.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PQSA_PSEAE

Accession

Primary (citable) accession number: Q9I4X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program