ID   ASCD_YERPS              Reviewed;         329 AA.
AC   Q66DP5; P37911; Q8GJ93;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, entry version 114.
DE   RecName: Full=CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase;
DE            EC=1.17.1.-;
DE   AltName: Full=CDP-6-deoxy-delta-3,4-glucoseen reductase;
DE            Short=E3;
GN   Name=ascD; Synonyms=ddhD, rfbI; OrderedLocusNames=YPTB0998;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=V;
RX   PubMed=8288541; DOI=10.1128/jb.176.2.460-468.1994;
RA   Lo S.F., Miller V.P., Lei Y., Thorson J.S., Liu H.-W., Schottel J.L.;
RT   "CDP-6-deoxy-delta 3,4-glucoseen reductase from Yersinia
RT   pseudotuberculosis: enzyme purification and characterization of the cloned
RT   gene.";
RL   J. Bacteriol. 176:460-468(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M85 / Serotype IIA;
RX   PubMed=8444803; DOI=10.1128/jb.175.5.1412-1422.1993;
RA   Kessler A.C., Haase A., Reeves P.R.;
RT   "Molecular analysis of the 3,6-dideoxyhexose pathway genes of Yersinia
RT   pseudotuberculosis serogroup IIA.";
RL   J. Bacteriol. 175:1412-1422(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype VA;
RX   PubMed=8071227; DOI=10.1128/jb.176.17.5483-5493.1994;
RA   Thorson J.S., Lo S.F., Ploux O., He X., Liu H.-W.;
RT   "Studies of the biosynthesis of 3,6-dideoxyhexoses: molecular cloning and
RT   characterization of the asc (ascarylose) region from Yersinia
RT   pseudotuberculosis serogroup VA.";
RL   J. Bacteriol. 176:5483-5493(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype IVB;
RA   Pacinelli E., Wang L., Reeves P.R.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=8961949; DOI=10.1021/bi961370w;
RA   Johnson D.A., Gassner G.T., Bandarian V., Ruzicka F.J., Ballou D.P.,
RA   Reed G.H., Liu H.-W.;
RT   "Kinetic characterization of an organic radical in the ascarylose
RT   biosynthetic pathway.";
RL   Biochemistry 35:15846-15856(1996).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=8672475; DOI=10.1021/bi960217z;
RA   Gassner G.T., Johnson D.A., Liu H.-W., Ballou D.P.;
RT   "Kinetics of the reductive half-reaction of the iron-sulfur flavoenzyme
RT   CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase.";
RL   Biochemistry 35:7752-7761(1996).
CC   -!- FUNCTION: Participates in the conversion of CDP-6-deoxy-D-glycero-L-
CC       threo-4-hexulose to 3,6-dideoxy-D-glycero-D-glycero-4-hexulose together
CC       with CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) in two
CC       consecutive steps. The detailed mechanism of E3 is not yet resolved.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; CDP-ascarylose biosynthesis.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SUBUNIT: Monomer.
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DR   EMBL; L25594; AAA16760.1; -; Unassigned_DNA.
DR   EMBL; AF461770; AAB49398.1; -; Genomic_DNA.
DR   EMBL; L33181; AAA88698.1; -; Genomic_DNA.
DR   EMBL; AF461769; AAN23052.1; -; Genomic_DNA.
DR   EMBL; BX936398; CAH20238.1; -; Genomic_DNA.
DR   PIR; A36952; A36952.
DR   RefSeq; WP_011191878.1; NC_006155.1.
DR   AlphaFoldDB; Q66DP5; -.
DR   SMR; Q66DP5; -.
DR   TCDB; 5.B.1.3.1; the phagocyte (gp91(phox)) nadph oxidase family.
DR   GeneID; 49786946; -.
DR   KEGG; ag:AAA88698; -.
DR   KEGG; ypo:BZ17_1550; -.
DR   KEGG; yps:YPTB0998; -.
DR   PATRIC; fig|273123.14.peg.1643; -.
DR   OMA; AAQCGMH; -.
DR   BioCyc; MetaCyc:MONOMER-13782; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00818; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06189; flavin_oxioreductase; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR050415; MRET.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; NAD; Oxidoreductase; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..329
FT                   /note="CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase
FT                   reductase"
FT                   /id="PRO_0000189394"
FT   DOMAIN          2..93
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          98..197
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         37
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         42
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         75
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   CONFLICT        111
FT                   /note="V -> I (in Ref. 1, 2 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  36033 MW;  8B1B98EE473704FF CRC64;
     MSLNVKLHPS GIIFTSDGTS TILDAALDSN IHIEYSCKDG TCGSCKAILI SGEVDSAENT
     FLTEEDVAKG AILTCCSKAK SDIELDVNYY PELSHIQKKT YPCKLDSIEF VGEDIAILSL
     RLPPTAKIQY LAGQYIDLII NGQRRSYSIA NAPGGNGNIE LHVRKVVNGV FSNIIFNELK
     LQQLLRIEGP QGTFFVREDN LPIVFLAGGT GFAPVKSMVE ALINKNDQRQ VHIYWGMPAG
     HNFYSDIANE WAIKHPNIHY VPVVSGDDST WTGATGFVHQ AVLEDIPDLS LFNVYACGSL
     AMITAARNDF INHGLAENKF FSDAFVPSK
//