KDUI_SALEP
ID KDUI_SALEP Reviewed; 278 AA.
AC B5QWV0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
DE EC=5.3.1.17 {ECO:0000255|HAMAP-Rule:MF_00687};
DE AltName: Full=5-keto-4-deoxyuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
DE AltName: Full=DKI isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
GN Name=kduI {ECO:0000255|HAMAP-Rule:MF_00687}; OrderedLocusNames=SEN2861;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
CC -!- FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-
CC glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
CC {ECO:0000255|HAMAP-Rule:MF_00687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-
CC hexodiulosonate; Xref=Rhea:RHEA:23896, ChEBI:CHEBI:17117,
CC ChEBI:CHEBI:29071; EC=5.3.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00687};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00687};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00687};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00687}.
CC -!- SIMILARITY: Belongs to the KduI family. {ECO:0000255|HAMAP-
CC Rule:MF_00687}.
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DR EMBL; AM933172; CAR34439.1; -; Genomic_DNA.
DR RefSeq; WP_000383274.1; NC_011294.1.
DR AlphaFoldDB; B5QWV0; -.
DR SMR; B5QWV0; -.
DR KEGG; set:SEN2861; -.
DR HOGENOM; CLU_062609_0_0_6; -.
DR OMA; TFIWAMA; -.
DR UniPathway; UPA00545; UER00826.
DR Proteomes; UP000000613; Chromosome.
DR GO; GO:0008697; F:4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 2.60.120.520; -; 1.
DR HAMAP; MF_00687; KduI; 1.
DR InterPro; IPR007045; KduI.
DR InterPro; IPR021120; KduI/IolB_isomerase.
DR InterPro; IPR027449; KduI_N.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR38461; PTHR38461; 1.
DR Pfam; PF04962; KduI; 1.
DR PIRSF; PIRSF006625; KduI; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 3: Inferred from homology;
KW Isomerase; Metal-binding; Zinc.
FT CHAIN 1..278
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT isomerase"
FT /id="PRO_1000131890"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
SQ SEQUENCE 278 AA; 31205 MW; 674D7735638F16EC CRC64;
MDVRQSIHSE HAKTLDTQAL RREFLIENIF VADEYTMVYS HIDRIIVGGI MPVSHSVEIG
GEVGKQLGVS RLLDRRELGV INIGGAGAII VDGQRHDIGH RDALYIGKGA KELVFVSNEA
SRPAKFYYNC APAHTAYPTK KVSPADVAPV TLGDNLTSNR RTINKYFVPD VLETCQLSMG
LTELAPGNLW NTMPCHTHER RMEVYLYFNM EEDSCVFHMM GQPQETRHIV MRNEQAVISP
SWSIHSGVGT KAYTFIWGMV GENQVFDDMD HVAVQDLR