KDSD_SALTY
ID KDSD_SALTY Reviewed; 328 AA.
AC Q8ZLS1;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=STM3315;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
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DR EMBL; AE006468; AAL22184.1; -; Genomic_DNA.
DR RefSeq; NP_462225.1; NC_003197.2.
DR RefSeq; WP_000018617.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLS1; -.
DR SMR; Q8ZLS1; -.
DR STRING; 99287.STM3315; -.
DR BindingDB; Q8ZLS1; -.
DR ChEMBL; CHEMBL3110; -.
DR PaxDb; Q8ZLS1; -.
DR PRIDE; Q8ZLS1; -.
DR DNASU; 1254838; -.
DR EnsemblBacteria; AAL22184; AAL22184; STM3315.
DR GeneID; 1254838; -.
DR KEGG; stm:STM3315; -.
DR PATRIC; fig|99287.12.peg.3516; -.
DR HOGENOM; CLU_040681_13_1_6; -.
DR OMA; LMACLMR; -.
DR PhylomeDB; Q8ZLS1; -.
DR BioCyc; SENT99287:STM3315-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00473.
DR Proteomes; UP000001014; 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; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..328
FT /note="Arabinose 5-phosphate isomerase KdsD"
FT /id="PRO_0000136579"
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; 35000 MW; CF9E3B2F86858F8E 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 VFDMGGDMRQ LGIAEVMTPG GIRVRPGILA VDALNLMQSR
HITSVLVADG DQLLGVLHMH DLLRAGVV
