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Database: UniProt
Entry: Q8X4N5_ECO57
LinkDB: Q8X4N5_ECO57
Original site: Q8X4N5_ECO57 
ID   Q8X4N5_ECO57            Unreviewed;       253 AA.
AC   Q8X4N5; A0A0H3JJX4; A0A6M0JEI8; Q7AB45;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 3.
DT   27-MAR-2024, entry version 139.
DE   SubName: Full=2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase {ECO:0000313|EMBL:BAB37122.1};
GN   Name=kduD {ECO:0000313|EMBL:BAB37122.1};
GN   ORFNames=ECs_3699 {ECO:0000313|EMBL:BAB37122.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB37122.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB37122.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR   EMBL; BA000007; BAB37122.1; -; Genomic_DNA.
DR   RefSeq; NP_311726.1; NC_002695.1.
DR   RefSeq; WP_000603526.1; NZ_VOAI01000003.1.
DR   AlphaFoldDB; Q8X4N5; -.
DR   STRING; 155864.Z4162; -.
DR   GeneID; 66673291; -.
DR   GeneID; 916482; -.
DR   KEGG; ecs:ECs_3699; -.
DR   PATRIC; fig|386585.9.peg.3866; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_1_6; -.
DR   OMA; WEVANVI; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0008678; F:2-deoxy-D-gluconate 3-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd05347; Ga5DH-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011286; 2-deoxy-D-gluc_3_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01832; kduD; 1.
DR   PANTHER; PTHR42760:SF140; 2-DEHYDRO-3-DEOXY-D-GLUCONATE 5-DEHYDROGENASE; 1.
DR   PANTHER; PTHR42760; SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
SQ   SEQUENCE   253 AA;  27041 MW;  85018928430EBFFA CRC64;
     MILSAFSLEG KVAVVTGCDT GLGQGMALGL AQAGCDIVGI NIVEPTETIK QVTALGRRFL
     SLTADLRKID GIPGLLDRAV AEFGHIDILV NNAGLIRRED ALEFSEKDWD DVMNLNIKSV
     FFMSQAAAKH FIAQGNGGKI INIASMLSFQ GGIRVPSYTA SKSGVMGVTR LMANEWAKHN
     INVNAIAPGY MATNNTQQLR ADEQRSAEIL DRIPAGRWGL PSDLMGPVVF LASSASDYVN
     GYTIAVDGGW LAR
//
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