ID   SORE_KLEPN              Reviewed;         410 AA.
AC   P37084;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=L-sorbose 1-phosphate reductase;
DE            EC=1.1.1.-;
GN   Name=sorE;
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   -!- FUNCTION: Reduces L-sorbose 1-phosphate to D-glucitol 6-phosphate.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O58389};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X66059; CAA46861.1; -; Genomic_DNA.
DR   PIR; S50191; S50191.
DR   RefSeq; WP_002884587.1; NZ_WYAL01000049.1.
DR   AlphaFoldDB; P37084; -.
DR   SMR; P37084; -.
DR   OrthoDB; 972769at2; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..410
FT                   /note="L-sorbose 1-phosphate reductase"
FT                   /id="PRO_0000160925"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         221
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         309..310
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
SQ   SEQUENCE   410 AA;  44797 MW;  26C630CF620F04E6 CRC64;
     MQTTTALRLY GKRDLRLETF TLPAMQDDEI LARVVTDSLC LSSWKEANQG ADHKKVPDDV
     ATRPIIIGHE FCGEILAVGK KWQHKFQPGQ RYVIQANLQL PDRPDCPGYS FPWIGGEATH
     VVIPNEVMAQ DCLLTWEGDT WFEGSLVEPL SCVIGAFNAN YHLQEGSYNH VMGIRPQGHT
     LILGGTGPMG LLAIDYALHG PINPSLLVVT DTNKPKLSYA RRHYPSEPQT LIHYLDGHEA
     SRDTLLALSG GHGFDDIFVF VPNEQLITLA SSLLAPDGCL NFFAGPQDKQ FSAPINFYDV
     HYAFTHYVGT SGGNTDDMRA AVALMQAKKV QTAKVVTHIL GLNAAGETTL DLPAVGGGKK
     LVYTGKAFPL TPLGEIADPE LAAIVARHHG IWSQEAEAYL LAHAEDITHD