(data stored in SCRATCH zone)

SWISSPROT: D6XXE1_BACIE

ID   D6XXE1_BACIE            Unreviewed;       276 AA.
AC   D6XXE1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase {ECO:0000256|HAMAP-Rule:MF_00687};
DE            EC=5.3.1.17 {ECO:0000256|HAMAP-Rule:MF_00687};
DE   AltName: Full=5-keto-4-deoxyuronate isomerase {ECO:0000256|HAMAP-Rule:MF_00687};
DE   AltName: Full=DKI isomerase {ECO:0000256|HAMAP-Rule:MF_00687};
GN   Name=kduI {ECO:0000256|HAMAP-Rule:MF_00687};
GN   OrderedLocusNames=Bsel_0460 {ECO:0000313|EMBL:ADH97998.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97998.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97998.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-
CC       glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
CC       {ECO:0000256|HAMAP-Rule:MF_00687, ECO:0000256|SAAS:SAAS00959317}.
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:0000256|HAMAP-
CC         Rule:MF_00687, ECO:0000256|SAAS:SAAS01117303};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00687};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00687};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-
CC       D-gluconate from pectin: step 4/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00687, ECO:0000256|SAAS:SAAS00959316}.
CC   -!- SIMILARITY: Belongs to the KduI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00687, ECO:0000256|SAAS:SAAS00959314}.
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DR   EMBL; CP001791; ADH97998.1; -; Genomic_DNA.
DR   RefSeq; WP_013171427.1; NC_014219.1.
DR   STRING; 439292.Bsel_0460; -.
DR   EnsemblBacteria; ADH97998; ADH97998; Bsel_0460.
DR   KEGG; bse:Bsel_0460; -.
DR   eggNOG; ENOG4105D50; Bacteria.
DR   eggNOG; COG3717; LUCA.
DR   HOGENOM; HOG000124379; -.
DR   KO; K01815; -.
DR   OMA; CQLQMGM; -.
DR   OrthoDB; 1047507at2; -.
DR   BioCyc; BSEL439292:G1GLR-490-MONOMER; -.
DR   UniPathway; UPA00545; UER00826.
DR   Proteomes; UP000000271; 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;
DR   PRODOM; D6XXE1.
DR   SWISS-2DPAGE; D6XXE1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00687,
KW   ECO:0000256|SAAS:SAAS00425504, ECO:0000313|EMBL:ADH97998.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00687,
KW   ECO:0000256|SAAS:SAAS00959321};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00687, ECO:0000256|SAAS:SAAS00959320}.
FT   METAL       194    194       Zinc. {ECO:0000256|HAMAP-Rule:MF_00687}.
FT   METAL       196    196       Zinc. {ECO:0000256|HAMAP-Rule:MF_00687}.
FT   METAL       201    201       Zinc. {ECO:0000256|HAMAP-Rule:MF_00687}.
FT   METAL       243    243       Zinc. {ECO:0000256|HAMAP-Rule:MF_00687}.
SQ   SEQUENCE   276 AA;  31958 MW;  6551DBBEE6F2091C CRC64;
     MEIRHATNPT DFKLYTTDRL RSDFLMENLF IEGELNLVYS HYDRVITGGV VPKEEEIKLP
     IIEQMKTEYF LERREMGIVN IGEPALVNVE GETYELNKRD CLYIGKGNQH VSFKSKNPDN
     PSKLYFVSVN AHTPYPVTLM PIKDATPVKL GSNAESNSRT IYKYIHSDGI QSCQLMMGMT
     LLEPNNMWNT MPAHLHDRRM EVYLYFDMDA SSRVFHFMGQ PHETRHLVVQ NEQVVLSPPW
     SIHSGVGTNN YTFIWAMAGD NYTFTDMDFI PMEDLR
//

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