RPE_SYNY3
ID RPE_SYNY3 Reviewed; 230 AA.
AC P74061;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000255|HAMAP-Rule:MF_02227};
DE EC=5.1.3.1 {ECO:0000255|HAMAP-Rule:MF_02227};
GN Name=rpe {ECO:0000255|HAMAP-Rule:MF_02227}; OrderedLocusNames=sll0807;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=15333955; DOI=10.1107/s0907444904015896;
RA Wise E.L., Akana J., Gerlt J.A., Rayment I.;
RT "Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6
RT A resolution.";
RL Acta Crystallogr. D 60:1687-1690(2004).
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02227};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02227};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_02227};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02227}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:15333955}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_02227}.
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DR EMBL; BA000022; BAA18137.1; -; Genomic_DNA.
DR PIR; S75576; S75576.
DR PDB; 1TQJ; X-ray; 1.60 A; A/B/C/D/E/F=1-230.
DR PDBsum; 1TQJ; -.
DR AlphaFoldDB; P74061; -.
DR SMR; P74061; -.
DR IntAct; P74061; 1.
DR STRING; 1148.1653221; -.
DR PaxDb; P74061; -.
DR EnsemblBacteria; BAA18137; BAA18137; BAA18137.
DR KEGG; syn:sll0807; -.
DR eggNOG; COG0036; Bacteria.
DR InParanoid; P74061; -.
DR OMA; CDLILIM; -.
DR PhylomeDB; P74061; -.
DR BRENDA; 5.1.3.1; 6192.
DR EvolutionaryTrace; P74061; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; -; 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 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Isomerase; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..230
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171582"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 146..149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 179..181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 179
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 201..202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1TQJ"
FT STRAND 32..45
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1TQJ"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1TQJ"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1TQJ"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1TQJ"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1TQJ"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1TQJ"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:1TQJ"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:1TQJ"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:1TQJ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1TQJ"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1TQJ"
SQ SEQUENCE 230 AA; 24971 MW; 6BE4D0930084B96B CRC64;
MSKNIVVAPS ILSADFSRLG EEIKAVDEAG ADWIHVDVMD GRFVPNITIG PLIVDAIRPL
TKKTLDVHLM IVEPEKYVED FAKAGADIIS VHVEHNASPH LHRTLCQIRE LGKKAGAVLN
PSTPLDFLEY VLPVCDLILI MSVNPGFGGQ SFIPEVLPKI RALRQMCDER GLDPWIEVDG
GLKPNNTWQV LEAGANAIVA GSAVFNAPNY AEAIAGVRNS KRPEPQLATV
