KDSD_ECOL6
ID KDSD_ECOL6 Reviewed; 328 AA.
AC Q8FD73;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=c3957;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAN82397.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN82397.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001305135.1; NC_004431.1.
DR AlphaFoldDB; Q8FD73; -.
DR SMR; Q8FD73; -.
DR STRING; 199310.c3957; -.
DR DNASU; 1040318; -.
DR EnsemblBacteria; AAN82397; AAN82397; c3957.
DR KEGG; ecc:c3957; -.
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; UP000001410; 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_0000136577"
FT DOMAIN 42..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 222
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; 35171 MW; A7A2327A95EA7D04 CRC64;
MSHVELQPGF DFQQAGKEVL AIERECLAEL DQYINQNFTL ACEKMFWCKG KVVVMGMGKS
GHIGRKMAAT FASTGTPSFF VHPGEAAHGD LGMVTPQDVV IAISNSGESS EITALIPVLK
RLHVPLICIT GCPESSMARA ADVHLCVKVA KEACPLGLAP TSSTTATLVM GDALAVALLK
ARGFTAEDFA LSHPGGALGR KLLLRVNDIM HTGDEIPHVK KTASLRDALL EVTRKNLGMT
VICDDNMMIE GIFTDGDLRR VFDMGVDVRR LSIADVMTPG GIRVRPGILA VEALNLMQSR
HITSVMVADG DHLLGVLHMH DLLRAGVV
