ASCD_YERPE
ID ASCD_YERPE Reviewed; 329 AA.
AC P68641; P37911; Q7B0V7;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
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=YPO3116, y1067, YP_0814;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EV 76;
RX PubMed=10931327; DOI=10.1046/j.1365-2958.2000.01993.x;
RA Skurnik M., Peippo A., Ervela E.;
RT "Characterization of the O-antigen gene clusters of Yersinia
RT pseudotuberculosis and the cryptic O-antigen gene cluster of Yersinia
RT pestis shows that the plague bacillus is most closely related to and has
RT evolved from Y. pseudotuberculosis serotype O:1b.";
RL Mol. Microbiol. 37:316-330(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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 (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; CDP-ascarylose biosynthesis.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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DR EMBL; AJ251713; CAB63270.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL21712.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84648.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61079.1; -; Genomic_DNA.
DR PIR; AE0378; AE0378.
DR RefSeq; WP_002208598.1; NZ_WUCM01000009.1.
DR RefSeq; YP_002348024.1; NC_003143.1.
DR AlphaFoldDB; P68641; -.
DR SMR; P68641; -.
DR STRING; 214092.YPO3116; -.
DR PaxDb; P68641; -.
DR DNASU; 1146014; -.
DR EnsemblBacteria; AAM84648; AAM84648; y1067.
DR EnsemblBacteria; AAS61079; AAS61079; YP_0814.
DR GeneID; 57975595; -.
DR KEGG; ype:YPO3116; -.
DR KEGG; ypk:y1067; -.
DR KEGG; ypm:YP_0814; -.
DR PATRIC; fig|214092.21.peg.3571; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_7_0_6; -.
DR OMA; IGLPYGC; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00818; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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 3: Inferred from homology;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..329
FT /note="CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase
FT reductase"
FT /id="PRO_0000189393"
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"
SQ SEQUENCE 329 AA; 36047 MW; 7930BD82FF126503 CRC64;
MSLNVKLHPS GIIFTSDGTS TILDAALDSN IHIEYSCKDG TCGSCKAILI SGEVDSAENT
FLTEEDVAKG AILTCCSKAK SDIELDVNYY PELSHIQKKT YPCKLDSIEF IGEDIAILSL
RLPPTAKIQY LAGQYIDLII NGQRRSYSIA NAPGGNGNIE LHVRKVVNGV FSNIIFNELK
LQQLLRIEGP QGTFFVREDN LPIVFLAGGT GFAPVKSMVE ALINKNDQRQ VHIYWGMPAG
HNFYSDIANE WAIKHPNIHY VPVVSGDDST WTGATGFVHQ AVLEDIPDLS LFNVYACGSL
AMITAARNDF INHGLAENKF FSDAFVPSK
