ID   IOLB_GEOKA              Reviewed;         276 AA.
AC   Q5KYR2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=5-deoxy-glucuronate isomerase {ECO:0000255|HAMAP-Rule:MF_01673};
DE            Short=5DG isomerase {ECO:0000255|HAMAP-Rule:MF_01673};
DE            EC=5.3.1.30 {ECO:0000255|HAMAP-Rule:MF_01673};
GN   Name=iolB {ECO:0000255|HAMAP-Rule:MF_01673}; OrderedLocusNames=GK1889;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
CC   -!- FUNCTION: Involved in the isomerization of 5-deoxy-glucuronate (5DG) to
CC       5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate).
CC       {ECO:0000255|HAMAP-Rule:MF_01673}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate;
CC         Xref=Rhea:RHEA:25840, ChEBI:CHEBI:16669, ChEBI:CHEBI:58852;
CC         EC=5.3.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_01673};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 4/7. {ECO:0000255|HAMAP-
CC       Rule:MF_01673}.
CC   -!- SIMILARITY: Belongs to the isomerase IolB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01673}.
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DR   EMBL; BA000043; BAD76174.1; -; Genomic_DNA.
DR   RefSeq; WP_011231379.1; NC_006510.1.
DR   AlphaFoldDB; Q5KYR2; -.
DR   SMR; Q5KYR2; -.
DR   STRING; 235909.GK1889; -.
DR   EnsemblBacteria; BAD76174; BAD76174; GK1889.
DR   KEGG; gka:GK1889; -.
DR   eggNOG; COG3718; Bacteria.
DR   HOGENOM; CLU_066438_1_0_9; -.
DR   OMA; HGYDLYY; -.
DR   UniPathway; UPA00076; UER00920.
DR   Proteomes; UP000001172; Chromosome.
DR   GO; GO:0102482; F:5-deoxy-D-glucuronate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008880; F:glucuronate isomerase activity; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.10; -; 2.
DR   HAMAP; MF_01673; IolB; 1.
DR   InterPro; IPR024203; Deoxy-glucuronate_isom_IolB.
DR   InterPro; IPR023770; IolB_Bacilli.
DR   InterPro; IPR021120; KduI/IolB_isomerase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR39193; PTHR39193; 1.
DR   Pfam; PF04962; KduI; 1.
DR   PIRSF; PIRSF036628; IolB; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   TIGRFAMs; TIGR04378; myo_inos_iolB; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..276
FT                   /note="5-deoxy-glucuronate isomerase"
FT                   /id="PRO_0000352387"
SQ   SEQUENCE   276 AA;  31186 MW;  FBAE1F509E4445B8 CRC64;
     MSRLIIPSHS PNEEGNVVRV TPESVGWEYV GFEVYVLAKG QTLRKETKDQ EACLVLLKGK
     ANISTKLERW EQIGLRMDVF EKVPPYSVYV PANDVYEVEA MTDVEVAVCL APGKGTYPAR
     LIPPSEVGVE IRGAGNIERR VHNILPESQP ADSLLVVEVF TPEGNWSSYP PHKHDQDNLP
     HESYLEETYY HKINPGHGFM VQRVYTDDRS IDETMVVKNG DVVLVPKGYH PVSAPPGYEG
     YYLNVMAGPV RTWKFHNDPD HDWVMESKLA AKQKEK