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Database: UniProt
Entry: A0A2H9L1Q2_9ARCH
LinkDB: A0A2H9L1Q2_9ARCH
Original site: A0A2H9L1Q2_9ARCH 
ID   A0A2H9L1Q2_9ARCH        Unreviewed;       217 AA.
AC   A0A2H9L1Q2;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
DE            EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
GN   Name=rpe {ECO:0000256|HAMAP-Rule:MF_02227,
GN   ECO:0000313|EMBL:PIT85449.1};
GN   ORFNames=COU36_03230 {ECO:0000313|EMBL:PIT85449.1};
OS   Candidatus Micrarchaeota archaeon CG10_big_fil_rev_8_21_14_0_10_59_7.
OC   Archaea; Candidatus Micrarchaeota.
OX   NCBI_TaxID=1974419 {ECO:0000313|EMBL:PIT85449.1, ECO:0000313|Proteomes:UP000228973};
RN   [1] {ECO:0000313|EMBL:PIT85449.1, ECO:0000313|Proteomes:UP000228973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG10_big_fil_rev_8_21_14_0_10_59_7
RC   {ECO:0000313|EMBL:PIT85449.1};
RA   Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA   Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA   Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-hosted
RT   aquifers and enrichment of novel symbionts in the deep terrestrial
RT   subsurface.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC       phosphate to D-xylulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_02227}.
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         ECO:0000256|HAMAP-Rule:MF_02227, ECO:0000256|PIRNR:PIRNR001461};
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02227,
CC         ECO:0000256|PIRSR:PIRSR001461-2};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02227, ECO:0000256|PIRSR:PIRSR001461-2};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|HAMAP-Rule:MF_02227}.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00009541, ECO:0000256|HAMAP-Rule:MF_02227,
CC       ECO:0000256|PIRNR:PIRNR001461}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02227}.
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:PIT85449.1}.
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DR   EMBL; PFCC01000108; PIT85449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H9L1Q2; -.
DR   Proteomes; UP000228973; Unassembled WGS sequence.
DR   GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR   CDD; cd00429; RPE; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_02227; RPE; 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   NCBIfam; TIGR01163; rpe; 1.
DR   PANTHER; PTHR11749; RIBULOSE-5-PHOSPHATE-3-EPIMERASE; 1.
DR   PANTHER; PTHR11749:SF3; RIBULOSE-PHOSPHATE 3-EPIMERASE-RELATED; 1.
DR   Pfam; PF00834; Ribul_P_3_epim; 1.
DR   PIRSF; PIRSF001461; RPE; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02227,
KW   ECO:0000256|PIRNR:PIRNR001461}; Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02227};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02227}; Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   ACT_SITE        33
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-1"
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-1"
FT   BINDING         6
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         31
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         33
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         65
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         142..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         171..173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT   BINDING         171
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         193..194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
SQ   SEQUENCE   217 AA;  23517 MW;  2E273D9056998C96 CRC64;
     MIVAPSLLSA DFSDIEEEAR RCEKAGADWL HVDVMDGRFV PNATEFSPDV VARIRKASKL
     FLDVHLMVET PEKLVEEYAK AGADLISFHL EAVENPAALV RKIHSLGKKA GISIKPATAV
     GKIPRQLLRE CDLFMVMTVE PGKGGQAFLP QMLPKVKLLR MLCPDARIEV DGGINADTAK
     KCAAAGADVL VAGTYLFKAP DMAKAIASLR VPMPRLL
//
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