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ID D3UY27_XENBS Unreviewed; 224 AA.
AC D3UY27;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 08-MAY-2019, entry version 50.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|PIRNR:PIRNR001461};
DE EC=5.1.3.1 {ECO:0000256|PIRNR:PIRNR001461};
GN Name=rpe {ECO:0000313|EMBL:CBJ79205.1};
GN OrderedLocusNames=XBJ1_0054 {ECO:0000313|EMBL:CBJ79205.1};
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79205.1, ECO:0000313|Proteomes:UP000002045};
RN [1] {ECO:0000313|EMBL:CBJ79205.1, ECO:0000313|Proteomes:UP000002045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79205.1,
RC ECO:0000313|Proteomes:UP000002045};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT photorhabdus: convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:e27909-e27909(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000256|PIRNR:PIRNR001461};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001461-2};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000256|PIRSR:PIRSR001461-2};
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|PIRNR:PIRNR001461}.
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DR EMBL; FN667741; CBJ79205.1; -; Genomic_DNA.
DR RefSeq; WP_012986678.1; NC_013892.1.
DR STRING; 406818.XBJ1_0054; -.
DR EnsemblBacteria; CBJ79205; CBJ79205; XBJ1_0054.
DR GeneID; 8829682; -.
DR KEGG; xbo:XBJ1_0054; -.
DR PATRIC; fig|406818.4.peg.47; -.
DR eggNOG; ENOG4105DJV; Bacteria.
DR eggNOG; COG0036; LUCA.
DR HOGENOM; HOG000259347; -.
DR KO; K01783; -.
DR OMA; CHLMIED; -.
DR BioCyc; XBOV406818:XBJ1_RS00250-MONOMER; -.
DR Proteomes; UP000002045; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01163; rpe; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 3: Inferred from homology;
DR PRODOM; D3UY27.
DR SWISS-2DPAGE; D3UY27.
KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW Isomerase {ECO:0000256|PIRNR:PIRNR001461,
KW ECO:0000313|EMBL:CBJ79205.1};
KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT REGION 145 148 Substrate binding. {ECO:0000256|PIRSR:
FT PIRSR001461-3}.
FT REGION 200 201 Substrate binding. {ECO:0000256|PIRSR:
FT PIRSR001461-3}.
FT ACT_SITE 37 37 Proton acceptor. {ECO:0000256|PIRSR:
FT PIRSR001461-1}.
FT ACT_SITE 178 178 Proton donor. {ECO:0000256|PIRSR:
FT PIRSR001461-1}.
FT METAL 35 35 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR001461-2}.
FT METAL 37 37 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR001461-2}.
FT METAL 69 69 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR001461-2}.
FT METAL 178 178 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR001461-2}.
FT BINDING 10 10 Substrate. {ECO:0000256|PIRSR:
FT PIRSR001461-3}.
FT BINDING 69 69 Substrate. {ECO:0000256|PIRSR:
FT PIRSR001461-3}.
FT BINDING 180 180 Substrate; via amide nitrogen.
FT {ECO:0000256|PIRSR:PIRSR001461-3}.
SQ SEQUENCE 224 AA; 24565 MW; C889EF392D094323 CRC64;
MKKDFLIAPS ILSADFARLG EDTAKVLAAG ADVVHFDVMD NHYVPNLTIG PMVCQALCDY
GITAPIDVHL MVKPVDRIIP DFAKAGATYI TFHPEASEHV DRTLQLIKEH GCKAGLVFNP
ATPLSYLDYV LDKLDVILLM SVNPGFSGQS FIPETLNKLR QVRKIIDESG YDIRLEVDGG
IKANNIREAA QAGADMFVAG SAIFSQPDYK TVIDEMRREL SKVA
//
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