RPE_HELPY
ID RPE_HELPY Reviewed; 217 AA.
AC P56188;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=HP_1386;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_02227}.
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DR EMBL; AE000511; AAD08425.1; -; Genomic_DNA.
DR PIR; B64693; B64693.
DR RefSeq; NP_208177.1; NC_000915.1.
DR RefSeq; WP_000861474.1; NC_018939.1.
DR AlphaFoldDB; P56188; -.
DR SMR; P56188; -.
DR IntAct; P56188; 1.
DR STRING; 85962.C694_07155; -.
DR PaxDb; P56188; -.
DR EnsemblBacteria; AAD08425; AAD08425; HP_1386.
DR KEGG; hpy:HP_1386; -.
DR PATRIC; fig|85962.47.peg.1484; -.
DR eggNOG; COG0036; Bacteria.
DR OMA; CDLILIM; -.
DR PhylomeDB; P56188; -.
DR Proteomes; UP000000429; 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 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..217
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171572"
FT ACT_SITE 31
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 6
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 29
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 31
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 138..141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 171..173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 193..194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
SQ SEQUENCE 217 AA; 24045 MW; 7CAA9E1E5DC9006F CRC64;
MKVAPSLLSA DFMHLAKEIE SVSNADFLHV DVMDGHYVPN LTMGPVVLEN VTQMSQVPLD
VHLMVENASF FAELFAPLKP QIISIHAENE KHPHRVLQLI KNLGITPGIV LNPHTHEESI
KYLLESVGLV LLMSVNPGFG GQKFLDLVLE KCLKVKELIK RYNPSCLLEV DGGVNDKNIF
ELQQAGVDVV VSGSYIFKSK DRKLAIEGLQ NVRQSLA
