ASCD_YERPS
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 03-AUG-2022, entry version 100.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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; NZ_CP009712.1.
DR AlphaFoldDB; Q66DP5; -.
DR SMR; Q66DP5; -.
DR TCDB; 5.B.1.3.1; the phagocyte (gp91(phox)) nadph oxidase family.
DR EnsemblBacteria; CAH20238; CAH20238; YPTB0998.
DR GeneID; 66842576; -.
DR KEGG; ypo:BZ17_1550; -.
DR KEGG; yps:YPTB0998; -.
DR PATRIC; fig|273123.14.peg.1643; -.
DR OMA; IGLPYGC; -.
DR BioCyc; MetaCyc:MON-13782; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00818; -.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 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; 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
