KDUI_LACE2
ID KDUI_LACE2 Reviewed; 280 AA.
AC C4Z0J8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=EUBELI_01111;
OS Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS (Eubacterium eligens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnospira.
OX NCBI_TaxID=515620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(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; CP001104; ACR72111.1; -; Genomic_DNA.
DR RefSeq; WP_012739346.1; NC_012778.1.
DR AlphaFoldDB; C4Z0J8; -.
DR SMR; C4Z0J8; -.
DR STRING; 515620.EUBELI_01111; -.
DR EnsemblBacteria; ACR72111; ACR72111; EUBELI_01111.
DR GeneID; 41355837; -.
DR KEGG; eel:EUBELI_01111; -.
DR eggNOG; COG3717; Bacteria.
DR HOGENOM; CLU_062609_0_0_9; -.
DR OMA; TFIWAMA; -.
DR OrthoDB; 1047507at2; -.
DR UniPathway; UPA00545; UER00826.
DR Proteomes; UP000001476; 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; Reference proteome; Zinc.
FT CHAIN 1..280
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT isomerase"
FT /id="PRO_1000212562"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
SQ SEQUENCE 280 AA; 32155 MW; F76FF3AC4490DCCE CRC64;
MEVRQGANAR DVKGYDTERL RNDFLIQNLF PADDFKLVYS QIDRIIVGGC MPVNKELTLE
AGSELKAAYF LERREMGIFN VGGNGSVIVD GTEYKFKYRD GLYIGMGSKE IKFKSEDSSK
PAKFYFNSTP AHKTYPTVFI DPEKDIKDEF KLQLGSVEGC NKRLNRKYIL PGQVETCQLE
MGITTLEPGS VWNTMPCHTH DRRMEVYFYF EIPEEDIVVH YMGEPTETRH IIMRSEEAVI
SPSWSIHSAS ATHAYAFIWG MAGENQDFDD MDWVDMKDLK