RPE_MYCTU
ID RPE_MYCTU Reviewed; 229 AA.
AC P9WI51; L0T6S4; P65760; P71676;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
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=Rv1408;
GN ORFNames=MTCY21B4.25;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP44167.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP44167.1; ALT_INIT; Genomic_DNA.
DR PIR; E70901; E70901.
DR RefSeq; NP_215924.1; NC_000962.3.
DR AlphaFoldDB; P9WI51; -.
DR SMR; P9WI51; -.
DR STRING; 83332.Rv1408; -.
DR PaxDb; P9WI51; -.
DR DNASU; 886702; -.
DR GeneID; 886702; -.
DR KEGG; mtu:Rv1408; -.
DR PATRIC; fig|83332.12.peg.1573; -.
DR TubercuList; Rv1408; -.
DR eggNOG; COG0036; Bacteria.
DR OMA; WLQVDGG; -.
DR Proteomes; UP000001584; 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 Carbohydrate metabolism; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..229
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171578"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 69
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 145..148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 178..180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 178
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
SQ SEQUENCE 229 AA; 23774 MW; 5C2E39D098490302 CRC64;
MAGSTGGPLI APSILAADFA RLADEAAAVN GADWLHVDVM DGHFVPNLTI GLPVVESLLA
VTDIPMDCHL MIDNPDRWAP PYAEAGAYNV TFHAEATDNP VGVARDIRAA GAKAGISVKP
GTPLEPYLDI LPHFDTLLVM SVEPGFGGQR FIPEVLSKVR AVRKMVDAGE LTILVEIDGG
INDDTIEQAA EAGVDCFVAG SAVYGADDPA AAVAALRRQA GAASLHLSL