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 27-MAR-2024, entry version 119.
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; Pseudomonadota; 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 KEGG; mlo:mlr4915; -.
DR PATRIC; fig|266835.9.peg.3881; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_5_5; -.
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 Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
