KDUI_CERSK
ID KDUI_CERSK Reviewed; 274 AA.
AC B9KKM8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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};
GN OrderedLocusNames=RSKD131_1815;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACM01675.1; -; Genomic_DNA.
DR RefSeq; WP_002720646.1; NC_011963.1.
DR AlphaFoldDB; B9KKM8; -.
DR SMR; B9KKM8; -.
DR EnsemblBacteria; ACM01675; ACM01675; RSKD131_1815.
DR GeneID; 57470802; -.
DR GeneID; 67447214; -.
DR KEGG; rsk:RSKD131_1815; -.
DR HOGENOM; CLU_062609_0_0_5; -.
DR OMA; TFIWAMA; -.
DR UniPathway; UPA00545; UER00826.
DR Proteomes; UP000001597; Chromosome 1.
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..274
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT isomerase"
FT /id="PRO_1000147781"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
SQ SEQUENCE 274 AA; 30263 MW; 9363E16BED39983B CRC64;
MTHVEIRHAM DPVSARQLDT AGLREAFHMG DLFRSGEIRL VYTHYDRMIV GGAVPAGEPL
VLDEVKPTGT ASILDRREMG VVNVGAAGTV SAGGESWEMG RGDVLYLPMG AGPVTFAGEG
RFYILSAPAH TAHPARLVKL EDAKKVKLGS PETANERTIN QFIHPEVMQS CQLVVGYTQF
HGGSVWNTMP AHVHDRRMEA YLYFDLAEEA RVFHFMGEPS ETRHLVMRNE EAVVSPPWSI
HCGCGTGSYT FVWAMAGDNV DYRDVEMVAM EDLR
