RPIB_MYCGE
ID RPIB_MYCGE Reviewed; 152 AA.
AC P47636;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable ribose-5-phosphate isomerase B {ECO:0000250|UniProtKB:P9WKD7};
DE EC=5.3.1.6 {ECO:0000250|UniProtKB:P9WKD7};
DE AltName: Full=Phosphoriboisomerase B {ECO:0000250|UniProtKB:P9WKD7};
GN Name=rpiB {ECO:0000250|UniProtKB:P9WKD7}; OrderedLocusNames=MG396;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
CC -!- FUNCTION: Catalyzes the interconversion of ribulose-5-P and ribose-5-P.
CC {ECO:0000250|UniProtKB:P9WKD7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC EC=5.3.1.6; Evidence={ECO:0000250|UniProtKB:P9WKD7};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000250|UniProtKB:P9WKD7}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WKD7}.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L43967; AAC71624.1; -; Genomic_DNA.
DR PIR; H64243; H64243.
DR RefSeq; WP_009885626.1; NZ_AAGX01000001.1.
DR AlphaFoldDB; P47636; -.
DR SMR; P47636; -.
DR STRING; 243273.MG_396; -.
DR PRIDE; P47636; -.
DR EnsemblBacteria; AAC71624; AAC71624; MG_396.
DR KEGG; mge:MG_396; -.
DR eggNOG; COG0698; Bacteria.
DR HOGENOM; CLU_091396_4_1_14; -.
DR OMA; DYPPFCL; -.
DR OrthoDB; 1346802at2; -.
DR BioCyc; MGEN243273:G1GJ2-493-MON; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IBA:GO_Central.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; ISS:UniProtKB.
DR GO; GO:0019316; P:D-allose catabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; ISS:UniProtKB.
DR Gene3D; 3.40.1400.10; -; 1.
DR InterPro; IPR004785; RpiB.
DR InterPro; IPR003500; RpiB_LacA_LacB.
DR InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR PANTHER; PTHR30345; PTHR30345; 1.
DR Pfam; PF02502; LacAB_rpiB; 1.
DR PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR SUPFAM; SSF89623; SSF89623; 1.
DR TIGRFAMs; TIGR01120; rpiB; 1.
DR TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..152
FT /note="Probable ribose-5-phosphate isomerase B"
FT /id="PRO_0000208165"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P37351"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 10..11
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 70..74
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 103
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 113
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 136
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 140
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
SQ SEQUENCE 152 AA; 16893 MW; 1D5A15E5C14F74DB CRC64;
MSFNIFIASD HTGLTLKKII SEHLKTKQFN VVDLGPNYFD ANDDYPDFAF LVADKVKKNS
DKDLGILICG TGVGVCMAAN KVKGVLAALV VSEKTAALAR QHDNANVLCL SSRFVTDSEN
IKIVDDFLKA NFEGGRHQRR IDKIIRYEKE TE
