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   16-JUN-2009, entry version 67.
DE   RecName: Full=Ribitol 2-dehydrogenase;
DE            Short=RDH;
DE            EC=1.1.1.56;
GN   Name=rbtD;
OS   Klebsiella aerogenes.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=28451;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=A, and D;
RX   MEDLINE=86050423; PubMed=3904726;
RA   Dothie J.M., Giglio J.R., Moore C.H., Taylor S.S., Hartley B.S.;
RT   "Ribitol dehydrogenase of Klebsiella aerogenes. Sequence and
RT   properties of wild-type and mutant strains.";
RL   Biochem. J. 230:569-578(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86050424; PubMed=2933028;
RA   Loviny T., Norton P.M., Hartley B.S.;
RT   "Ribitol dehydrogenase of Klebsiella aerogenes. Sequence of the
RT   structural gene.";
RL   Biochem. J. 230:579-585(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RX   MEDLINE=85230591; PubMed=3891331;
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
RT   region of the rbt operon of Klebsiella aerogenes.";
RL   EMBO J. 4:1339-1344(1985).
CC   -!- CATALYTIC ACTIVITY: Ribitol + NAD(+) = D-ribulose + NADH.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: The sequence shown is that of strain A.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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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   HSSP; Q9HFV6; 1JA9.
DR   BioCyc; MetaCyc:MON-12237; -.
DR   BRENDA; 1.1.1.56; 366.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0050255; F:ribitol 2-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN         1    249       Ribitol 2-dehydrogenase.
FT                                /FTId=PRO_0000054756.
FT   NP_BIND      20     43       NAD (By similarity).
FT   ACT_SITE    160    160       Proton acceptor (By similarity).
FT   VARIANT     196    196       A -> P (in strain: D).
FT   CONFLICT    146    147       AV -> SS (in Ref. 2; AAA25140).
FT   CONFLICT    212    212       N -> D (in Ref. 1; AA sequence).
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
//