(data stored in SCRATCH zone)

SWISSPROT: D1CE53_THET1

ID   D1CE53_THET1            Unreviewed;       232 AA.
AC   D1CE53;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|PIRNR:PIRNR001461};
DE            EC=5.1.3.1 {ECO:0000256|PIRNR:PIRNR001461};
GN   OrderedLocusNames=Tter_0287 {ECO:0000313|EMBL:ACZ41209.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41209.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41209.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41209.1; -; Genomic_DNA.
DR   RefSeq; WP_012874244.1; NC_013525.1.
DR   STRING; 525904.Tter_0287; -.
DR   EnsemblBacteria; ACZ41209; ACZ41209; Tter_0287.
DR   KEGG; ttr:Tter_0287; -.
DR   eggNOG; ENOG4105DJV; Bacteria.
DR   eggNOG; COG0036; LUCA.
DR   HOGENOM; HOG000259347; -.
DR   KO; K01783; -.
DR   OMA; CHLMIED; -.
DR   OrthoDB; 1697639at2; -.
DR   BioCyc; TTER525904:G1GGS-290-MONOMER; -.
DR   Proteomes; UP000000323; 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; D1CE53.
DR   SWISS-2DPAGE; D1CE53.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR001461,
KW   ECO:0000313|EMBL:ACZ41209.1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   REGION      148    151       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   REGION      203    204       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   ACT_SITE     41     41       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR001461-1}.
FT   ACT_SITE    181    181       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001461-1}.
FT   METAL        39     39       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL        41     41       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL        72     72       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL       181    181       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   BINDING      14     14       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING      72     72       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING     183    183       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001461-3}.
SQ   SEQUENCE   232 AA;  25446 MW;  616B4281A6CFC767 CRC64;
     MFHVKQGKLK IAPSILSADF TRLGEQVQEA EAAGADYIHY DVMDGHFVPN ISMGPYIAEA
     VKRSTSLPLD VHLMIEDPDR YIPDFVSAGA DIITVHYEAV VHLHRTVMRI RDLGAKAGVA
     INPSTPPFML DEILPFVNLI LVMSVNPGFG GQHFIPTSLQ KLKRLRMMID DRRYDIELEV
     DGGIDPNTAE PVAASGARVL VAGSAIFGQG SIEENIRAIR ESAERGLARQ AF
//

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