ID   SORD_KLEPN              Reviewed;         267 AA.
AC   P37079;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Sorbitol-6-phosphate 2-dehydrogenase;
DE            EC=1.1.1.140;
DE   AltName: Full=Glucitol-6-phosphate dehydrogenase;
DE   AltName: Full=Ketosephosphate reductase;
GN   Name=sorD;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=7947968; DOI=10.1016/0167-4838(94)90124-4;
RA   Wehmeier U.F., Lengeler J.W.;
RT   "Sequence of the sor-operon for L-sorbose utilization from Klebsiella
RT   pneumoniae KAY2026.";
RL   Biochim. Biophys. Acta 1208:348-351(1994).
RN   [2]
RP   SIMILARITY.
RX   PubMed=7652212; DOI=10.1016/0923-2508(96)80896-5;
RA   Reizer J., Reizer A., Saier M.H. Jr.;
RT   "Sorbose-1-P reductase (SorE) and the glucitol-6-P dehydrogenase (SorD) of
RT   the Klebsiella pneumoniae L-sorbose operon belong to the zinc-dependent
RT   dehydrogenase family and the short chain alcohol dehydrogenase family,
RT   respectively.";
RL   Res. Microbiol. 146:183-184(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sorbitol 6-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:19837, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:60084; EC=1.1.1.140;
CC   -!- PATHWAY: Carbohydrate metabolism; D-sorbitol degradation; D-fructose 6-
CC       phosphate from D-sorbitol 6-phosphate: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; X66059; CAA46856.1; -; Genomic_DNA.
DR   PIR; S50186; S50186.
DR   RefSeq; WP_004177862.1; NZ_WULI01000005.1.
DR   AlphaFoldDB; P37079; -.
DR   SMR; P37079; -.
DR   PATRIC; fig|573.1555.peg.3683; -.
DR   UniPathway; UPA00812; UER00783.
DR   GO; GO:0009010; F:sorbitol-6-phosphate 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006062; P:sorbitol catabolic process; IEA:UniProtKB-UniPathway.
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   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..267
FT                   /note="Sorbitol-6-phosphate 2-dehydrogenase"
FT                   /id="PRO_0000054775"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  29005 MW;  44A9C31964384DEC CRC64;
     MNTWLNLKDN VIIVTGGASG IGLAIVDELL SQGAHVQMID IHGGDRHHNG DNYHFWSTDI
     SSATEVQQTI DAIIQRWSRI DGLVNNAGVN FPRLLVDEKA PAGRYELNEA AFEKMVNINQ
     KGVFFMSQAV ARQMVKQRAG VIVNVSSESG LEGSEGQSCY AATKAALNSF TRSWSKELGK
     YGIRVVGVAP GILEKTGLRT PEYEEALAWT RNITVEQLRE GYTKNAIPIG RAGKLSEVAD
     FVCYLLSARA SYITGVTTNI AGGKTRG