KDUI2_RHIME
ID KDUI2_RHIME Reviewed; 282 AA.
AC Q92V09;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=RB0925; ORFNames=SMb21349;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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}.
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DR EMBL; AL591985; CAC49325.1; -; Genomic_DNA.
DR PIR; E95957; E95957.
DR RefSeq; NP_437465.1; NC_003078.1.
DR RefSeq; WP_010975773.1; NC_003078.1.
DR AlphaFoldDB; Q92V09; -.
DR SMR; Q92V09; -.
DR STRING; 266834.SM_b21349; -.
DR PRIDE; Q92V09; -.
DR EnsemblBacteria; CAC49325; CAC49325; SM_b21349.
DR GeneID; 25013751; -.
DR GeneID; 61600894; -.
DR KEGG; sme:SM_b21349; -.
DR PATRIC; fig|266834.11.peg.5854; -.
DR eggNOG; COG3717; Bacteria.
DR HOGENOM; CLU_062609_0_0_5; -.
DR OMA; TFIWAMA; -.
DR UniPathway; UPA00545; UER00826.
DR PRO; PR:Q92V09; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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; Plasmid; Reference proteome; Zinc.
FT CHAIN 1..282
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
FT 2"
FT /id="PRO_0000215494"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 282 AA; 31441 MW; E3FF77AEFF6BEDE3 CRC64;
MTASHIDYTI RYAVDPAAAA RMDTDALRAN FHIGDLFRQG RISLTYSHYD RMIVGGAMPV
DKPLALETIR PTGTARFLER RELIAVNIGG PGRIEMNGES FRLEPRDMAY AGMGEDVTFS
SEDPAVPAKF YLLSAPAHQA LPRRHIRIGD AKRLDLGSAA TSNERSIFQF IHPEGVKTCQ
LVVGMTQLAP GSVWNTMPCH VHDRRMEAYL YFDLDDSARV LHLMGEPSET RHIVMAREEA
VLSPPWSIHS GCGTANYAFI WAMAGDNIDY TDVEMVPMET LR
