ID   RIDH_KLEAE              Reviewed;         249 AA.
AC   P00335;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Ribitol 2-dehydrogenase;
DE            Short=RDH;
DE            EC=1.1.1.56;
GN   Name=rbtD;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=A, and D;
RX   PubMed=3904726; DOI=10.1042/bj2300569;
RA   Dothie J.M., Giglio J.R., Moore C.H., Taylor S.S., Hartley B.S.;
RT   "Ribitol dehydrogenase of Klebsiella aerogenes. Sequence and properties of
RT   wild-type and mutant strains.";
RL   Biochem. J. 230:569-578(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2933028; DOI=10.1042/bj2300579;
RA   Loviny T., Norton P.M., Hartley B.S.;
RT   "Ribitol dehydrogenase of Klebsiella aerogenes. Sequence of the structural
RT   gene.";
RL   Biochem. J. 230:579-585(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RX   PubMed=3891331; DOI=10.1002/j.1460-2075.1985.tb03782.x;
RA   Wu J.C., Anderton-Loviny T., Smith C.A., Hartley B.S.;
RT   "Structure of wild-type and mutant repressors and of the control region of
RT   the rbt operon of Klebsiella aerogenes.";
RL   EMBO J. 4:1339-1344(1985).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + ribitol = D-ribulose + H(+) + NADH;
CC         Xref=Rhea:RHEA:20053, ChEBI:CHEBI:15378, ChEBI:CHEBI:15963,
CC         ChEBI:CHEBI:17173, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.56;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: The sequence shown is that of strain A.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; M25606; AAA25140.1; -; Genomic_DNA.
DR   EMBL; X02448; CAA26292.1; -; Genomic_DNA.
DR   PIR; A94585; DEKBR.
DR   PIR; S07134; S07134.
DR   AlphaFoldDB; P00335; -.
DR   SMR; P00335; -.
DR   STRING; 548.EAG7_00524; -.
DR   PRIDE; P00335; -.
DR   BioCyc; MetaCyc:MON-12237; -.
DR   GO; GO:0050255; F:ribitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..249
FT                   /note="Ribitol 2-dehydrogenase"
FT                   /id="PRO_0000054756"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         20..43
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   VARIANT         196
FT                   /note="A -> P (in strain: D)"
FT   CONFLICT        146..147
FT                   /note="AV -> SS (in Ref. 2; AAA25140)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="N -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  26514 MW;  C34896C276CC8FBC CRC64;
     MKHSVSSMNT SLSGKVAAIT GAASGIGLEC ARTLLGAGAK VVLIDREGEK LNKLVAELGE
     NAFALQVDLM QADQVDNLLQ GILQLTGRLD IFHANAGAYI GGPVAEGDPD VWDRVLHLNI
     NAAFRCVRSV LPHLIAQKSG DIIFTAVIAG VVPVIWEPVY TASKFAVQAF VHTTRRQVAQ
     YGVRVGAVLP GPVVTALLDD WPKAKMDEAL ANGSLMQPIE VAESVLFMVT RSKNVTVRDI
     VILPNSVDL