(data stored in SCRATCH zone)

SWISSPROT: C1E106_MICCC

ID   C1E106_MICCC            Unreviewed;       268 AA.
AC   C1E106;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 37.
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:ACO62093.1};
GN   ORFNames=MICPUN_104768 {ECO:0000313|EMBL:ACO62093.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO62093.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO62093.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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}.
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DR   EMBL; CP001324; ACO62093.1; -; Genomic_DNA.
DR   RefSeq; XP_002500835.1; XM_002500789.1.
DR   ProteinModelPortal; C1E106; -.
DR   GeneID; 8241582; -.
DR   KEGG; mis:MICPUN_104768; -.
DR   HOGENOM; HOG000259347; -.
DR   InParanoid; C1E106; -.
DR   KO; K01783; -.
DR   Proteomes; UP000002009; Chromosome 3.
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; C1E106.
DR   SWISS-2DPAGE; C1E106.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR001461};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   REGION      190    193       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   REGION      245    246       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   ACT_SITE     81     81       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR001461-1}.
FT   ACT_SITE    223    223       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001461-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL       112    112       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL       223    223       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   BINDING      54     54       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING     112    112       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING     225    225       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001461-3}.
SQ   SEQUENCE   268 AA;  28029 MW;  28ACCD5336F8DA68 CRC64;
     MSAVTNSAVF ARKSLAGKAI ANKRVATKAR AAFNVSANAK VDACDKNSVI VSPSILSANF
     ATLGAEVKAV DEAGAEWIHI DVMDGRFVPN ITIGPLVVDA LRPVTDKVLD THLMIVEPEL
     RVADFAKAGS DIISVHAEGA STIHLHRTIN QIKDLGCKAG VVLNPGTHPD CLEYILDCVD
     LILVMSVNPG FGGQSFIESQ VDKIKKIKAM CDAKGVNPWI EVDGGVSPAN AYKVIDAGAN
     ALVAGSAVFN SDDYAKAIAG IKASKAPK
//

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