ID   B7UTC5_ECO27            Unreviewed;       455 AA.
AC   B7UTC5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   04-NOV-2026, entry version 74.
DE   SubName: Full=D-arabitol dehydrogenase {ECO:0000313|EMBL:CAS09778.1};
GN   Name=atlD {ECO:0000313|EMBL:CAS09778.1};
GN   OrderedLocusNames=E2348C_2230 {ECO:0000313|EMBL:CAS09778.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS09778.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS09778.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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DR   EMBL; FM180568; CAS09778.1; -; Genomic_DNA.
DR   RefSeq; WP_000660943.1; NC_011601.1.
DR   AlphaFoldDB; B7UTC5; -.
DR   KEGG; ecg:E2348C_2230; -.
DR   HOGENOM; CLU_027324_0_2_6; -.
DR   OMA; AACWHDR; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0008866; F:fructuronate reductase activity; IEA:TreeGrafter.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; IEA:TreeGrafter.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR050025; DalD.
DR   InterPro; IPR000669; Mannitol_DH.
DR   InterPro; IPR050988; Mannitol_DH/Oxidoreductase.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF043014; DArabDhDalD; 1.
DR   PANTHER; PTHR43362:SF7; D-MANNONATE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43362; MANNITOL DEHYDROGENASE DSF1-RELATED; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008205}.
FT   DOMAIN          8..253
FT                   /note="Mannitol dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01232"
FT   DOMAIN          263..447
FT                   /note="Mannitol dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08125"
SQ   SEQUENCE   455 AA;  50998 MW;  9904B4E6CE1BC30F CRC64;
     MKEKYTWLHI GLGSFHRAHQ AWYLHRLLVG GDARWSIAAG NIRNDAEHVV QALMTQKGRY
     VLETVSPEGE SVYEEITSIQ KLLPWQVDLQ PLIAEGADPK TKVIAFTVTE GGYYLNTSHK
     LEVTNPDLAA DLKGECKTIY GVITRILEAR MANNAGPLTL LNCDNVRHNG ERFHDGLVEF
     LQLTGKQTVI DWLSANATCP NTMVDRITPR PSTELPERIK AQTGMSDKAP VMGETFIQWV
     VEDNFRDVRP ALENVGVELV ESVIPYEEAK IRILNSSHSC IAWAGTLVGQ KYIHESTLTD
     FIYQIADRYV TEDVIPCLGD NGIDLETYRD VVLRRFTNPH IQDTNQRVAA DGFSKIPAMI
     APTLRECYQR GVRPNATAML PALFYVFMQQ WHLGKLPYEY QDGILDAPAV HAMFESADPI
     AVYASDKALF GDLTDCADFA ALLREKIADV YALIN
//