RHLG_PSEAE
ID RHLG_PSEAE Reviewed; 256 AA.
AC Q9RPT1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100;
DE AltName: Full=3-ketoacyl-acyl carrier protein reductase;
GN Name=rhlG; OrderedLocusNames=PA3387;
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].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9721281; DOI=10.1128/jb.180.17.4442-4451.1998;
RA Campos-Garcia J., Caro A.D., Najera R., Miller-Maier R.M., Al-Tahhan R.A.,
RA Soberon-Chavez G.;
RT "The Pseudomonas aeruginosa rhlG gene encodes an NADPH-dependent beta-
RT ketoacyl reductase which is specifically involved in rhamnolipid
RT synthesis.";
RL J. Bacteriol. 180:4442-4451(1998).
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).
CC -!- FUNCTION: Required for the synthesis of the beta-hydroxy acid moiety of
CC rhamnolipids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC -!- PATHWAY: Lipid metabolism; rhamnolipid biosynthesis.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF148964; AAD53514.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06775.1; -; Genomic_DNA.
DR PIR; F83221; F83221.
DR RefSeq; NP_252077.1; NC_002516.2.
DR RefSeq; WP_003113116.1; NZ_QZGE01000017.1.
DR PDB; 2B4Q; X-ray; 2.30 A; A/B=1-256.
DR PDBsum; 2B4Q; -.
DR AlphaFoldDB; Q9RPT1; -.
DR SMR; Q9RPT1; -.
DR STRING; 287.DR97_4535; -.
DR PaxDb; Q9RPT1; -.
DR PRIDE; Q9RPT1; -.
DR EnsemblBacteria; AAG06775; AAG06775; PA3387.
DR GeneID; 880033; -.
DR KEGG; pae:PA3387; -.
DR PATRIC; fig|208964.12.peg.3546; -.
DR PseudoCAP; PA3387; -.
DR HOGENOM; CLU_010194_1_1_6; -.
DR InParanoid; Q9RPT1; -.
DR OMA; VGQRAWP; -.
DR PhylomeDB; Q9RPT1; -.
DR BioCyc; MetaCyc:MON-15945; -.
DR BioCyc; PAER208964:G1FZ6-3453-MON; -.
DR UniPathway; UPA00657; -.
DR EvolutionaryTrace; Q9RPT1; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0008709; F:cholate 7-alpha-dehydrogenase activity; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..256
FT /note="Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-
FT protein] reductase"
FT /id="PRO_0000054755"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 14..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2B4Q"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 162..180
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:2B4Q"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:2B4Q"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2B4Q"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2B4Q"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:2B4Q"
SQ SEQUENCE 256 AA; 26831 MW; 3DB7B481F34C89A3 CRC64;
MHPYFSLAGR IALVTGGSRG IGQMIAQGLL EAGARVFICA RDAEACADTA TRLSAYGDCQ
AIPADLSSEA GARRLAQALG ELSARLDILV NNAGTSWGAA LESYPVSGWE KVMQLNVTSV
FSCIQQLLPL LRRSASAENP ARVINIGSVA GISAMGEQAY AYGPSKAALH QLSRMLAKEL
VGEHINVNVI APGRFPSRMT RHIANDPQAL EADSASIPMG RWGRPEEMAA LAISLAGTAG
AYMTGNVIPI DGGFHL
