KDSD_PSEAE
ID KDSD_PSEAE Reviewed; 326 AA.
AC Q9HVW0;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Arabinose 5-phosphate isomerase KdsD;
DE Short=API;
DE EC=5.3.1.13;
DE AltName: Full=Pa-KdsD;
GN Name=kdsD; OrderedLocusNames=PA4457;
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, NMR
RP SPECTROSCOPY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF LYS-56; HIS-85 AND HIS-190.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21337483; DOI=10.1002/cbic.201000754;
RA Airoldi C., Sommaruga S., Merlo S., Sperandeo P., Cipolla L., Polissi A.,
RA Nicotra F.;
RT "Targeting bacterial membranes: identification of Pseudomonas aeruginosa D-
RT arabinose-5P isomerase and NMR characterisation of its substrate
RT recognition and binding properties.";
RL ChemBioChem 12:719-727(2011).
CC -!- FUNCTION: Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate
CC (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs).
CC Catalyzes the reversible aldol-ketol isomerization between D-ribulose
CC 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).
CC {ECO:0000269|PubMed:21337483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:23104, ChEBI:CHEBI:57693, ChEBI:CHEBI:58121;
CC EC=5.3.1.13; Evidence={ECO:0000269|PubMed:21337483};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Specific activity decreases significantly at 5 degrees Celsius
CC compared to specific activity at 37 degrees Celsius.
CC {ECO:0000269|PubMed:21337483};
CC -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC step 1/3.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells are not viable.
CC {ECO:0000269|PubMed:21337483}.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG07845.1; -; Genomic_DNA.
DR PIR; A83087; A83087.
DR RefSeq; NP_253147.1; NC_002516.2.
DR RefSeq; WP_003134758.1; NZ_CP053028.1.
DR AlphaFoldDB; Q9HVW0; -.
DR SMR; Q9HVW0; -.
DR STRING; 287.DR97_1636; -.
DR PaxDb; Q9HVW0; -.
DR PRIDE; Q9HVW0; -.
DR DNASU; 881001; -.
DR EnsemblBacteria; AAG07845; AAG07845; PA4457.
DR GeneID; 881001; -.
DR KEGG; pae:PA4457; -.
DR PATRIC; fig|208964.12.peg.4667; -.
DR PseudoCAP; PA4457; -.
DR HOGENOM; CLU_040681_13_1_6; -.
DR InParanoid; Q9HVW0; -.
DR OMA; LMACLMR; -.
DR PhylomeDB; Q9HVW0; -.
DR BioCyc; PAER208964:G1FZ6-4546-MON; -.
DR BRENDA; 5.3.1.13; 5087.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00473.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR004800; KdsD/KpsF-type.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035474; SIS_Kpsf.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00393; kpsF; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; CBS domain; Isomerase;
KW Lipopolysaccharide biosynthesis; Metal-binding; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..326
FT /note="Arabinose 5-phosphate isomerase KdsD"
FT /id="PRO_0000417165"
FT DOMAIN 38..181
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 207..265
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 274..326
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 111..120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 56
FT /note="Catalytically relevant"
FT SITE 108
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 149
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 190
FT /note="Catalytically relevant"
FT MUTAGEN 56
FT /note="K->A: 100-fold reduction in catalytic activity
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:21337483"
FT MUTAGEN 85
FT /note="H->A: 200-fold reduction in catalytic activity
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:21337483"
FT MUTAGEN 190
FT /note="H->A: 400-fold reduction in catalytic activity
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:21337483"
SQ SEQUENCE 326 AA; 34198 MW; 510B3190C0F92C51 CRC64;
MNMSQNLDFI HSAQRTIGLE RDAVDSLLAR IGDDFVKACE LLLAGKGRVV VVGMGKSGHV
GKKIAATLAS TGTPSFFVHP AEASHGDMGM ITKDDVVLAL SNSGSTAEIV TLLPLIKRLG
ITLISMTGNP ESPLAKAAEV NLDASVGQEA CPLNLAPTSS TTVTLVLGDA LAIALLEARG
FTAEDFAFSH PGGALGRRLL LKVEDVMHVG EGLPQVLLGT SLTGALMEMT RKGLGMTVVL
DEHGKLAGIF TDGDLRRALD RGIDVRQVTI DQVMTVHGKT VRAEILAAEA LKIMEDNKIG
ALVVVDADDR PVGALNMHDL LRAGVM
