ID   YCJQ_SHIFL              Reviewed;         350 AA.
AC   Q83RK8;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=D-guloside 3-dehydrogenase {ECO:0000250|UniProtKB:P76043};
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:P76043};
GN   Name=ycjQ; OrderedLocusNames=SF1318.1, S1402;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of the hydroxyl
CC       group at C3 of D-gulosides leading to 3-dehydro-D-gulosides. Probably
CC       functions in a metabolic pathway that transforms D-gulosides to D-
CC       glucosides. Is also able to catalyze the reverse reactions, i.e. the
CC       NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-
CC       gulosides leading to D-gulosides. In vitro, can oxidize D-gulose and
CC       methyl beta-D-guloside, and reduce methyl alpha-3-dehydro-D-guloside
CC       and methyl beta-3-dehydro-D-guloside. However, the actual specific
CC       physiological substrates for this metabolic pathway are unknown.
CC       {ECO:0000250|UniProtKB:P76043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-guloside + NAD(+) = a 3-dehydro-D-guloside + H(+) + NADH;
CC         Xref=Rhea:RHEA:61720, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:145014, ChEBI:CHEBI:145016;
CC         Evidence={ECO:0000250|UniProtKB:P76043};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P76043};
CC       Note=Binds 1 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P76043};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN42928.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16811.1; -; Genomic_DNA.
DR   RefSeq; NP_707221.1; NC_004337.2.
DR   AlphaFoldDB; Q83RK8; -.
DR   SMR; Q83RK8; -.
DR   STRING; 198214.SF1319; -.
DR   DNASU; 1077776; -.
DR   EnsemblBacteria; AAN42928; AAN42928; SF1319.
DR   EnsemblBacteria; AAP16811; AAP16811; S1402.
DR   GeneID; 1023364; -.
DR   KEGG; sfl:SF1319; -.
DR   KEGG; sfx:S1402; -.
DR   PATRIC; fig|198214.7.peg.1549; -.
DR   HOGENOM; CLU_026673_9_0_6; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..350
FT                   /note="D-guloside 3-dehydrogenase"
FT                   /id="PRO_0000160891"
FT   CONFLICT        141
FT                   /note="N -> D (in Ref. 2; AAP16811)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  38216 MW;  F59EFE9A50C48610 CRC64;
     MKKLVATAPR VAALVEYEDR AILANEVKIR VRFGAPKHGT EVVDFRAASP FIDEDFNGEW
     QMFTPRPADA PRGIEFGKFQ LGNMVVGDII ECGSDVTDYA VGDSVCGYGP LSETVIINAV
     NNYKLRKMPQ GSSWKNAVCY NPAQFAMSGV RDANVRVGDF VVVVGLGAIG QIAIQLAKRA
     GASVVIGVDP IAHRCDIARR HGADFCLNPI GTDVGKEIKT LTGKQGADVI IETSGYADAL
     QSALRGLAYG GTISYVAFAK PFAEGFNLGR EAHFNNAKIV FSRACSEPNP DYPRWSRKRI
     EETCWELLMN GYLNCEDLID PVVTFANSPE SYMQYVDQHP EQSIKMGVTF