(data stored in ACNUC9543 zone)

SWISSPROT: A0A0H2Y4F7_YERPA

ID   A0A0H2Y4F7_YERPA        Unreviewed;       357 AA.
AC   A0A0H2Y4F7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 16.
DE   RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|RuleBase:RU004473};
DE            EC=4.2.1.46 {ECO:0000256|RuleBase:RU004473};
GN   OrderedLocusNames=YPA_0156 {ECO:0000313|EMBL:ABG12125.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12125.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12125.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12125.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-
CC         glucose + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57477, ChEBI:CHEBI:57649; EC=4.2.1.46;
CC         Evidence={ECO:0000256|RuleBase:RU004473};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU004473};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. dTDP-glucose dehydratase subfamily.
CC       {ECO:0000256|RuleBase:RU004473}.
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DR   EMBL; CP000308; ABG12125.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12125; ABG12125; YPA_0156.
DR   KEGG; ypa:YPA_0156; -.
DR   KO; K01710; -.
DR   OMA; KLIPLMC; -.
DR   BioCyc; YPES360102:GHZU-171-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR   CDD; cd05246; dTDP_GD_SDR_e; 1.
DR   InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2Y4F7.
DR   SWISS-2DPAGE; A0A0H2Y4F7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Lyase {ECO:0000256|RuleBase:RU004473, ECO:0000313|EMBL:ABG12125.1}.
FT   DOMAIN        7    329       NAD(P)-bd_dom. {ECO:0000259|Pfam:
FT                                PF16363}.
SQ   SEQUENCE   357 AA;  39820 MW;  FF3AB062F92D1AEB CRC64;
     MALRRILVTG GAGFIGSAVV RHIIDGTSDS VVVVDKLTYA GNLESLSVVA GSERYAFEQV
     DICDSSELDR VFAQYQPNVV MHLAAESHVD RSIDGPAAFI ETNVVGTYTL LEAARHYWQQ
     LSVEAKQAFR FHHISTDEVY GDLHGTDDLF TETTPYAPSS PYSASKASSD HLVRAWLRTY
     GLPTLVTNCS NNYGPYHFPE KLIPLVILNA LAGKPLPVYG NGAQVRDWLY VEDHARALYQ
     VVTEGVVGET YNIGGHNERK NIEVVETICA LLDELVPAKP AGIAHYRDLI TYVKDRPGHD
     MRYAIDAGKI ERELGWRPQE TFESGIRKTV LWYLNNESWW RRVQDGSYAG ERLGLSD
//

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