RHLA_PSEAE
ID RHLA_PSEAE Reviewed; 295 AA.
AC Q51559; Q9HYD0;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=3-(3-hydroxydecanoyloxy)decanoate synthase {ECO:0000305|PubMed:18326581};
DE EC=2.3.1.- {ECO:0000269|PubMed:18326581};
GN Name=rhlA; OrderedLocusNames=PA3479;
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], AND INDUCTION.
RC STRAIN=DSM 2659 / PG201;
RX PubMed=8051059; DOI=10.1016/s0021-9258(17)32089-6;
RA Ochsner U.A., Fiechter A., Reiser J.;
RT "Isolation, characterization, and expression in Escherichia coli of the
RT Pseudomonas aeruginosa rhlAB genes encoding a rhamnosyltransferase involved
RT in rhamnolipid biosurfactant synthesis.";
RL J. Biol. Chem. 269:19787-19795(1994).
RN [2]
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 [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15126453; DOI=10.1128/jb.186.10.2936-2945.2004;
RA Heurlier K., Williams F., Heeb S., Dormond C., Pessi G., Singer D.,
RA Camara M., Williams P., Haas D.;
RT "Positive control of swarming, rhamnolipid synthesis, and lipase production
RT by the posttranscriptional RsmA/RsmZ system in Pseudomonas aeruginosa
RT PAO1.";
RL J. Bacteriol. 186:2936-2945(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, and PA14;
RX PubMed=18326581; DOI=10.1128/jb.00080-08;
RA Zhu K., Rock C.O.;
RT "RhlA converts beta-hydroxyacyl-acyl carrier protein intermediates in fatty
RT acid synthesis to the beta-hydroxydecanoyl-beta-hydroxydecanoate component
RT of rhamnolipids in Pseudomonas aeruginosa.";
RL J. Bacteriol. 190:3147-3154(2008).
CC -!- FUNCTION: Required for rhamnolipid surfactant production
CC (PubMed:15126453). Supplies the acyl moieties for rhamnolipid
CC biosynthesis by competing with the enzymes of the type II fatty acid
CC synthase (FASII) cycle for the beta-hydroxyacyl-acyl carrier protein
CC (ACP) pathway intermediates. Catalyzes the formation of one molecule of
CC beta-hydroxydecanoyl-beta-hydroxydecanoate from two molecules of beta-
CC hydroxydecanoyl-ACP. Is the only enzyme required to generate the lipid
CC component of rhamnolipid. In vitro results establish that RhlA is
CC highly selective for 10-carbon acyl-ACP intermediates and thus
CC functions as the molecular ruler that controls the acyl chain
CC composition of rhamnolipids. Cannot use beta-hydroxydecanoyl-CoA as
CC substrate (PubMed:18326581). Rhamnolipid production plays an important
CC role in swarming motility (PubMed:15126453).
CC {ECO:0000269|PubMed:15126453, ECO:0000269|PubMed:18326581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (3R)-hydroxydecanoyl-[ACP] + H2O = (3R)-3-[(3R)-3-
CC hydroxydecanoyloxy]decanoate + H(+) + 2 holo-[ACP];
CC Xref=Rhea:RHEA:55592, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78466, ChEBI:CHEBI:139104;
CC Evidence={ECO:0000269|PubMed:18326581};
CC -!- PATHWAY: Lipid metabolism; rhamnolipid biosynthesis.
CC {ECO:0000269|PubMed:18326581}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18326581}.
CC -!- INDUCTION: By nitrogen starvation (PubMed:8051059). Expression is about
CC 20-fold higher in stationary phase (PubMed:8051059). Positively
CC regulated by the translational regulator CsrA (RsmA) (PubMed:15126453).
CC {ECO:0000269|PubMed:15126453, ECO:0000269|PubMed:8051059}.
CC -!- DISRUPTION PHENOTYPE: Loss of rhamnolipid production and of swarming
CC mobility (PubMed:15126453). {ECO:0000269|PubMed:15126453}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; L28170; AAA62128.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06867.1; -; Genomic_DNA.
DR PIR; A53652; A53652.
DR PIR; D83212; D83212.
DR RefSeq; NP_252169.1; NC_002516.2.
DR RefSeq; WP_003113897.1; NZ_QZGE01000039.1.
DR AlphaFoldDB; Q51559; -.
DR SMR; Q51559; -.
DR STRING; 287.DR97_4442; -.
DR ChEMBL; CHEMBL1795159; -.
DR ESTHER; pseae-rhla; 6_AlphaBeta_hydrolase.
DR PaxDb; Q51559; -.
DR PRIDE; Q51559; -.
DR DNASU; 878955; -.
DR EnsemblBacteria; AAG06867; AAG06867; PA3479.
DR GeneID; 878955; -.
DR KEGG; pae:PA3479; -.
DR PATRIC; fig|208964.12.peg.3642; -.
DR PseudoCAP; PA3479; -.
DR HOGENOM; CLU_062012_0_0_6; -.
DR InParanoid; Q51559; -.
DR OMA; LESKAAW; -.
DR PhylomeDB; Q51559; -.
DR BioCyc; MetaCyc:MON-15954; -.
DR BioCyc; PAER208964:G1FZ6-3547-MON; -.
DR UniPathway; UPA00657; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0106236; P:rhamnolipid biosynthesis; IMP:PHI-base.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..295
FT /note="3-(3-hydroxydecanoyloxy)decanoate synthase"
FT /id="PRO_0000097327"
FT DOMAIN 30..252
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT CONFLICT 168
FT /note="Q -> P (in Ref. 1; AAA62128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32963 MW; 6E66805F003B85EB CRC64;
MRRESLLVSV CKGLRVHVER VGQDPGRSTV MLVNGAMATT ASFARTCKCL AEHFNVVLFD
LPFAGQSRQH NPQRGLITKD DEVEILLALI ERFEVNHLVS ASWGGISTLL ALSRNPRGIR
SSVVMAFAPG LNQAMLDYVG RAQALIELDD KSAIGHLLNE TVGKYLPQRL KASNHQHMAS
LATGEYEQAR FHIDQVLALN DRGYLACLER IQSHVHFING SWDEYTTAED ARQFRDYLPH
CSFSRVEGTG HFLDLESKLA AVRVHRALLE HLLKQPEPQR AERAAGFHEM AIGYA
