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KDUI_SALTY
ID   KDUI_SALTY              Reviewed;         278 AA.
AC   Q8ZM98;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=STM3018;
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: 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; AE006468; AAL21894.1; -; Genomic_DNA.
DR   RefSeq; NP_461935.1; NC_003197.2.
DR   RefSeq; WP_000383271.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZM98; -.
DR   SMR; Q8ZM98; -.
DR   STRING; 99287.STM3018; -.
DR   PaxDb; Q8ZM98; -.
DR   EnsemblBacteria; AAL21894; AAL21894; STM3018.
DR   GeneID; 1254541; -.
DR   KEGG; stm:STM3018; -.
DR   PATRIC; fig|99287.12.peg.3194; -.
DR   HOGENOM; CLU_062609_0_0_6; -.
DR   OMA; TFIWAMA; -.
DR   PhylomeDB; Q8ZM98; -.
DR   BioCyc; SENT99287:STM3018-MON; -.
DR   UniPathway; UPA00545; UER00826.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0008697; F:4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019698; P:D-galacturonate catabolic process; IBA:GO_Central.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; IBA:GO_Central.
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; Reference proteome; Zinc.
FT   CHAIN           1..278
FT                   /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT                   isomerase"
FT                   /id="PRO_0000215496"
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;  31201 MW;  5B80B519414D2C61 CRC64;
     MDVRQSIHSE HAKTLDTQAL RREFLIENIF VADEYTMVYS HIDRIIVGGI MPVSHPVEIG
     GEVGKQLGVS RLLDRRELGV INIGGAGAII VDGQRHDIGH RDALYIGKGA KELVFVSNEA
     SRPAKFYYNC APAHTAYPTK KVSPADVAPV TLGDNLTSNR RTINKYFVPD VLETCQLSMG
     LTELAPGNLW NTMPCHTHER RMEVYLYFNM EEDSCVFHMM GQPQETRHIV MRNEQAVISP
     SWSIHSGVGT KAYTFVWGMV GENQVFDDMD HVAVQDLR
 
 
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