ID   KDUI2_BACTN             Reviewed;         292 AA.
AC   Q8A0B5;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase 2;
DE            EC=5.3.1.17;
DE   AltName: Full=5-keto-4-deoxyuronate isomerase 2;
DE   AltName: Full=DKI isomerase 2;
GN   Name=kduI2; OrderedLocusNames=BT_4106;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
CC   -!- FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-
CC       glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 4/5.
CC   -!- SIMILARITY: Belongs to the KduI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO79211.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE015928; AAO79211.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_813017.1; NC_004663.1.
DR   AlphaFoldDB; Q8A0B5; -.
DR   SMR; Q8A0B5; -.
DR   STRING; 226186.BT_4106; -.
DR   PaxDb; Q8A0B5; -.
DR   PRIDE; Q8A0B5; -.
DR   EnsemblBacteria; AAO79211; AAO79211; BT_4106.
DR   KEGG; bth:BT_4106; -.
DR   PATRIC; fig|226186.12.peg.4171; -.
DR   eggNOG; COG3717; Bacteria.
DR   HOGENOM; CLU_062609_0_0_10; -.
DR   InParanoid; Q8A0B5; -.
DR   OMA; TFIWAMA; -.
DR   UniPathway; UPA00545; UER00826.
DR   Proteomes; UP000001414; 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..292
FT                   /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
FT                   2"
FT                   /id="PRO_0000215483"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  33051 MW;  18B129469B7A5E52 CRC64;
     MSASAQVNYK MQVACNPQDV KTYNTNRLRS SFLMEKVMVP DQINVTYSMY DRLIFGGAVP
     ATKELVLETI DPLKAKYFLE RRELGVINIG GEGIVTVDGK EYTLNFKDAL YVGRGKQKVT
     FKSKDASKPA KFYINSATAH KEYKTQLITI DGRKGSLKAN SFAAGKMEES NDRVINQLIV
     NNVLEEGPCQ LQMGLTELKP GSVWNTMPAH THSRRVEAYF YFNVPEGNSI CHFMGEPQEE
     RIVWMQNEQA IMSPEWSIHA AAGTSNYMFI WGMAGENLDY GDMDKIKYTE MR