KDSD_SALTI
ID KDSD_SALTI Reviewed; 328 AA.
AC Q8Z3G6;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Arabinose 5-phosphate isomerase KdsD;
DE Short=API;
DE Short=L-API;
DE EC=5.3.1.13;
GN Name=kdsD; OrderedLocusNames=STY3494, t3232;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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) (By similarity).
CC {ECO:0000250}.
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;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL513382; CAD07832.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70768.1; -; Genomic_DNA.
DR RefSeq; NP_457694.1; NC_003198.1.
DR RefSeq; WP_000018616.1; NZ_WSUR01000003.1.
DR AlphaFoldDB; Q8Z3G6; -.
DR SMR; Q8Z3G6; -.
DR STRING; 220341.16504380; -.
DR EnsemblBacteria; AAO70768; AAO70768; t3232.
DR KEGG; stt:t3232; -.
DR KEGG; sty:STY3494; -.
DR PATRIC; fig|220341.7.peg.3558; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_6; -.
DR OMA; LMACLMR; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00473.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00393; kpsF; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; CBS domain; Isomerase;
KW Lipopolysaccharide biosynthesis; Metal-binding; Repeat; Zinc.
FT CHAIN 1..328
FT /note="Arabinose 5-phosphate isomerase KdsD"
FT /id="PRO_0000136578"
FT DOMAIN 41..184
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 210..268
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 277..328
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 75..76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114..123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148..150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 111
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 152
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 35032 MW; B89E3B3BC2D59BCA CRC64;
MSHLALQPGF DFQQAGKEVL EIEREGLAEL DQYINQHFTL ACEKMFNCTG KVVVMGMGKS
GHIGRKMAAT FASTGTSSFF VHPGEAAHGD LGMVTPQDVV IAISNSGESS EIAALIPVLK
RLHVPLICIT GRPESSMARA ADVHLCVKVP KEACPLGLAP TSSTTATLVM GDALAVALLK
ARGFTAEDFA LSHPGGALGR KLLLRVSDIM HTGDEIPHVN KHATLRDALL EITRKNLGMT
VICDESMKID GIFTDGDLRR MFDMGGDMRQ LGIAEVMTPG GIRVRPGILA VDALNLMQSR
HITSVLVADG DQLLGVLHMH DLLRAGVV
