ID   M1SCN7_MORMO            Unreviewed;       345 AA.
AC   M1SCN7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Xylitol dehydrogenase {ECO:0000313|EMBL:AGG32174.1};
GN   ORFNames=MU9_3130 {ECO:0000313|EMBL:AGG32174.1};
OS   Morganella morganii subsp. morganii KT.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG32174.1, ECO:0000313|Proteomes:UP000011834};
RN   [1] {ECO:0000313|EMBL:AGG32174.1, ECO:0000313|Proteomes:UP000011834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT {ECO:0000313|EMBL:AGG32174.1,
RC   ECO:0000313|Proteomes:UP000011834};
RX   PubMed=23282187;
RA   Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA   Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT   "Whole-genome sequencing and identification of Morganella morganii KT
RT   pathogenicity-related genes.";
RL   BMC Genomics 13:S4-S4(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP004345; AGG32174.1; -; Genomic_DNA.
DR   RefSeq; WP_015422928.1; NC_020418.1.
DR   AlphaFoldDB; M1SCN7; -.
DR   GeneID; 69677835; -.
DR   KEGG; mmk:MU9_3130; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_5_6; -.
DR   Proteomes; UP000011834; Chromosome.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05285; sorbitol_DH; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR045306; SDH-like.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011834};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   345 AA;  36615 MW;  5F30717CA3A09D6E CRC64;
     MKALVLEKAG KIAIQDWQSN EVLGDDDVEI KIHTVGICGS DVHYYQHGRI GPFVVEAPMV
     LGHEASGVIT AAGKNVKHLK VGDRVCMEPG IPDLQSPQSR AGIYNLDPAV RFWATPPIDG
     CLRESVIHPA AFTFKLPDNV SFAQGAMVEP LAIGMQSATK AGIKPGDIGL VIGAGTIGII
     TALCALAGGC SDVIICDVFD EKLKVAEKYQ GLHAVNSKDQ QALADKVREL TGGEGVNVLF
     ECSGAKPVIA SISDHIAPGG TAVLVGMPID PAPLDIVAAQ AKEVTFKTIF RYANMYPRTI
     RLLSSGKLNV APLLSATYKF KDSVEAYERA AEGRATDVKI VLEME
//