(data stored in ACNUC7421 zone)

SWISSPROT: D4YXK3_SPHJU

ID   D4YXK3_SPHJU            Unreviewed;       220 AA.
AC   D4YXK3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 44.
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:BAI95085.1};
GN   OrderedLocusNames=SJA_C1-02510 {ECO:0000313|EMBL:BAI95085.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95085.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95085.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5-
CC       phosphate. {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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010803; BAI95085.1; -; Genomic_DNA.
DR   RefSeq; WP_007686706.1; NC_014006.1.
DR   ProteinModelPortal; D4YXK3; -.
DR   STRING; 452662.SJA_C1-02510; -.
DR   EnsemblBacteria; BAI95085; BAI95085; SJA_C1-02510.
DR   GeneID; 29271954; -.
DR   KEGG; sjp:SJA_C1-02510; -.
DR   eggNOG; ENOG4105DJV; Bacteria.
DR   eggNOG; COG0036; LUCA.
DR   HOGENOM; HOG000259347; -.
DR   KO; K01783; -.
DR   OMA; CHLMIED; -.
DR   OrthoDB; POG091H01TC; -.
DR   Proteomes; UP000007753; Chromosome 1.
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; D4YXK3.
DR   SWISS-2DPAGE; D4YXK3.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR001461,
KW   ECO:0000313|EMBL:BAI95085.1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   REGION      144    147       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   REGION      199    200       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   ACT_SITE     37     37       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR001461-1}.
FT   ACT_SITE    177    177       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        68     68       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL       177    177       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   BINDING      10     10       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING      68     68       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING     179    179       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001461-3}.
SQ   SEQUENCE   220 AA;  23459 MW;  6CF7FE3FC0BD43B5 CRC64;
     MTSPILISPS ILSADFARLG EEVRAIDEAG ADWIHIDVMD GHFVPNITIG PGVVKALRPH
     TKKPFDVHLM ISPVDQYLNA FAEAGADILT VHPEAGPHIH RSIQHIKSLG VQAGVVLNPG
     TPAKMLDYLI DDVDLILVMS VNPGFGGQSF IANQLRKIEA IRKMIEKSGR DIRLQVDGGI
     DFTTAPLAIE AGADVLVAGT ATFRGGASAY ADNIRTLRGG
//

If you have problems or comments...

PBIL Back to PBIL home page