KDUI_SALHS
ID KDUI_SALHS Reviewed; 278 AA.
AC B4TGS4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=SeHA_C3234;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001120; ACF66969.1; -; Genomic_DNA.
DR RefSeq; WP_000383279.1; NC_011083.1.
DR AlphaFoldDB; B4TGS4; -.
DR SMR; B4TGS4; -.
DR KEGG; seh:SeHA_C3234; -.
DR HOGENOM; CLU_062609_0_0_6; -.
DR OMA; TFIWAMA; -.
DR UniPathway; UPA00545; UER00826.
DR Proteomes; UP000001866; 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_1000131892"
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; 31235 MW; 27FD7732123F16E0 CRC64;
MDVRQSIHSE HAKTLDTQTL 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