ID   XYLD_RHILO              Reviewed;         348 AA.
AC   Q98D10;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Putative D-xylulose reductase;
DE            EC=1.1.1.9;
DE   AltName: Full=Xylitol dehydrogenase;
DE            Short=XDH;
GN   OrderedLocusNames=mlr4915;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH;
CC         Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC         ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; BA000012; BAB51461.1; -; Genomic_DNA.
DR   RefSeq; WP_010912802.1; NC_002678.2.
DR   AlphaFoldDB; Q98D10; -.
DR   SMR; Q98D10; -.
DR   STRING; 266835.14024859; -.
DR   EnsemblBacteria; BAB51461; BAB51461; BAB51461.
DR   KEGG; mlo:mlr4915; -.
DR   PATRIC; fig|266835.9.peg.3881; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_5_5; -.
DR   OMA; FWKAGRI; -.
DR   OrthoDB; 972769at2; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05285; sorbitol_DH; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR045306; SDH-like.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..348
FT                   /note="Putative D-xylulose reductase"
FT                   /id="PRO_0000160886"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  36355 MW;  5323000209211076 CRC64;
     MRALVLEKKG ELSLREIALP LDVGPDDVKI AIHTVGVCGS DVHYYTHGAI GSYVVRAPMV
     LGHEAAGTVV ETGANVETFK AGDRVCMEPG VPNLSSRATK LGIYNVDPDV SFWATPPVHG
     VLAPYAVHPA AFTYKLPDNV SFAEGAMVEP FAIGMQAASR ARIVPGDVAV VVGCGPIGIM
     IALAALAGGC SKVLISDFSA PKLKIAAQYA GIVPVNIGER SLVDAVAAAT DKWGADIVFE
     ASGSPKAFAD LFDVVRPGGA VVLVGLPVEP VALNVPAAIS KEVRIETVFR YANIFDRALQ
     LIASGKVDLK PLITGTYDFA DSIKAFERAA QGNPEDVKLQ ILLTGEKG