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 27-MAR-2024, entry version 116.
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; Pseudomonadota; 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 RefSeq; WP_000737354.1; NZ_CP123365.1.
DR AlphaFoldDB; Q83RK8; -.
DR SMR; Q83RK8; -.
DR STRING; 198214.SF1319; -.
DR PaxDb; 198214-SF1319; -.
DR DNASU; 1077776; -.
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 CDD; cd08255; 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43350:SF22; D-GULOSIDE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
