KDSD_FRATT
ID KDSD_FRATT Reviewed; 327 AA.
AC Q5NGP7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Arabinose 5-phosphate isomerase KdsD;
DE Short=API;
DE EC=5.3.1.13;
GN Name=kdsD; OrderedLocusNames=FTT_0788c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=21236668; DOI=10.1016/j.bmcl.2010.12.066;
RA Yep A., Sorenson R.J., Wilson M.R., Showalter H.D., Larsen S.D.,
RA Keller P.R., Woodard R.W.;
RT "Enediol mimics as inhibitors of the D-arabinose 5-phosphate isomerase
RT (KdsD) from Francisella tularensis.";
RL Bioorg. Med. Chem. Lett. 21:2679-2682(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:21236668}.
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:21236668};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxamates, mimicking the putative
CC enediol reaction intermediate. Most potent inhibition, with an IC(50)
CC of 0.7 uM, is obtained with the 4 carbon-based hydroxamate containing
CC acetyl moieties. {ECO:0000269|PubMed:21236668}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for A5P (at pH 8.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:21236668};
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 -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ749949; CAG45421.1; -; Genomic_DNA.
DR RefSeq; YP_169795.1; NC_006570.2.
DR AlphaFoldDB; Q5NGP7; -.
DR SMR; Q5NGP7; -.
DR STRING; 177416.FTT_0788c; -.
DR BindingDB; Q5NGP7; -.
DR ChEMBL; CHEMBL1770042; -.
DR DNASU; 3192129; -.
DR EnsemblBacteria; CAG45421; CAG45421; FTT_0788c.
DR KEGG; ftu:FTT_0788c; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR OMA; LMACLMR; -.
DR SABIO-RK; Q5NGP7; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00473.
DR PHI-base; PHI:7067; -.
DR Proteomes; UP000001174; 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..327
FT /note="Arabinose 5-phosphate isomerase KdsD"
FT /id="PRO_0000417166"
FT DOMAIN 41..183
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 209..268
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 275..327
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113..122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147..149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 110
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 151
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 192
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 35691 MW; 21D9D0564BAF1831 CRC64;
MEISMTSHIN NAVETFRLEI ETLEKLKNSI DENFEKACEI ILENNRDKSR VIITGMGKSG
HIGKKMAATF ASTGTPAFFV HPGEAGHGDF GMITKNDVLI AISNSGTSSE IMGLLPMIKH
LDIPIIAITS NPKSILARNS NVTLNLHVDK EACPLNLAPT SSTTATLVLG DALAIALLKA
KNFSEKDFAF SHPNGALGRK LILKVENIMR KGNEIPIVKP TDNIRKAILE ISDKGVGNTL
VAENNTLLGI FTDGDLRRMF EAESFNSQRA ISEVMTKNPK SISKEEMAIT ALEKMEKYEI
TSLAVVDNGH NILGIVTMHD LIKLELR
