ID A0A098VW48_9MICR Unreviewed; 371 AA.
AC A0A098VW48;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013920};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188};
DE AltName: Full=Pentose-5-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00030599};
DE AltName: Full=RPE {ECO:0000256|ARBA:ARBA00029933};
GN ORFNames=DI09_23p210 {ECO:0000313|EMBL:KGG51946.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG51946.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG51946.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG51946.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG51946.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001782};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC xylulose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage):
CC step 1/1. {ECO:0000256|ARBA:ARBA00005016}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|ARBA:ARBA00009541}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC {ECO:0000256|ARBA:ARBA00008080}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGG51946.1}.
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DR EMBL; JMKJ01000155; KGG51946.1; -; Genomic_DNA.
DR RefSeq; XP_013238373.1; XM_013382919.1.
DR AlphaFoldDB; A0A098VW48; -.
DR GeneID; 25259175; -.
DR VEuPathDB; MicrosporidiaDB:DI09_23p210; -.
DR HOGENOM; CLU_746147_0_0_1; -.
DR OrthoDB; 5480189at2759; -.
DR UniPathway; UPA00115; UER00411.
DR Proteomes; UP000029725; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 4.10.910.10; 30s ribosomal protein s13, domain 2; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR027437; Rbsml_uS13_C.
DR InterPro; IPR001892; Ribosomal_uS13.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR InterPro; IPR018269; Ribosomal_uS13_CS.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR01163; rpe; 1.
DR PANTHER; PTHR11749; RIBULOSE-5-PHOSPHATE-3-EPIMERASE; 1.
DR PANTHER; PTHR11749:SF3; RIBULOSE-PHOSPHATE 3-EPIMERASE; 1.
DR Pfam; PF00416; Ribosomal_S13; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Reference proteome {ECO:0000313|Proteomes:UP000029725};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
SQ SEQUENCE 371 AA; 40848 MW; C129828D1DEE85BA CRC64;
MTAGPIIIAP SILSSDFANL AADCQRVIDA GADALHVDIM DGHFVPNLTI GPAVVKCLRE
KVQHKIFDCH LMVSDPKMWV KPLAAAGATI FTFHLESEIE NIFNLIAEIK QTGMKAGIAI
KPNTPVSDVI PYLQSIDMVL VMSVEPGFGG QKFMPSIIPK AIRNITPHLD IEVDGGVTLE
NVGDIIKAGA NVIVAGSAIF NSADPRAPSF DFLSEMSLVV SDKSNFQHII RLLNTNVDGK
QKVMYAITAI KGVGRCFSNI VCKKADVDLN KRAGELSNEE LERLVTIIQN PRQYGIPDWF
LNRQKDIKDG SYSQVVSNAL DNKLREDLDY LKKIRCHRGL RHHWNLRVRG QHTKTTGRFG
RTMGVSKKKG A
//
