(data stored in ACNUC1104 zone)

SWISSPROT: D3VG56_XENNA

ID   D3VG56_XENNA            Unreviewed;       224 AA.
AC   D3VG56;
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:CBJ88146.1};
GN   OrderedLocusNames=XNC1_0058 {ECO:0000313|EMBL:CBJ88146.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88146.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88146.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
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; FN667742; CBJ88146.1; -; Genomic_DNA.
DR   RefSeq; WP_010847519.1; NC_014228.1.
DR   STRING; 406817.XNC1_0058; -.
DR   EnsemblBacteria; CBJ88146; CBJ88146; XNC1_0058.
DR   KEGG; xne:XNC1_0058; -.
DR   eggNOG; ENOG4105DJV; Bacteria.
DR   eggNOG; COG0036; LUCA.
DR   HOGENOM; HOG000259347; -.
DR   KO; K01783; -.
DR   OMA; CHLMIED; -.
DR   Proteomes; UP000008075; 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; D3VG56.
DR   SWISS-2DPAGE; D3VG56.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR001461,
KW   ECO:0000313|EMBL:CBJ88146.1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
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;  24536 MW;  D54C485C05E24DBE CRC64;
     MKQDFLIAPS ILSADFARLG EDTAKVLAAG ADVVHFDVMD NHYVPNLTIG PMVCQALRHY
     GITAPIDVHL MVKPVDRIIP DFAKAGATYI TFHPEASEHI DRTLQLIREH GCKAGLVFNP
     ATPLRYLDYV LDKLDVILLM SVNPGFGGQS FIPETLKKLR QVRKIIDDSG YDIRLEVDGG
     IKPSNIAEAA QAGADMFVAG SAIFSQPDYK AVIDEMRGEL SKVT
//

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