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 27-MAR-2024, entry version 119. 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; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. 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 PDB; 6MU0; X-ray; 1.10 A; A=1-152. DR PDBsum; 6MU0; -. DR AlphaFoldDB; P47636; -. DR SMR; P47636; -. DR STRING; 243273.MG_396; -. DR KEGG; mge:MG_396; -. DR eggNOG; COG0698; Bacteria. DR HOGENOM; CLU_091396_4_1_14; -. DR InParanoid; P47636; -. DR OrthoDB; 1778624at2; -. DR BioCyc; MGEN243273:G1GJ2-493-MONOMER; -. DR UniPathway; UPA00115; UER00412. DR Proteomes; UP000000807; Chromosome. 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; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1. DR InterPro; IPR004785; RpiB. DR InterPro; IPR003500; RpiB_LacA_LacB. DR InterPro; IPR036569; RpiB_LacA_LacB_sf. DR NCBIfam; TIGR01120; rpiB; 1. DR NCBIfam; TIGR00689; rpiB_lacA_lacB; 1. DR PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1. DR PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1. DR Pfam; PF02502; LacAB_rpiB; 1. DR PIRSF; PIRSF005384; RpiB_LacA_B; 1. DR SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1. PE 1: Evidence at protein level; KW 3D-structure; 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" FT STRAND 3..9 FT /evidence="ECO:0007829|PDB:6MU0" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:6MU0" FT HELIX 14..26 FT /evidence="ECO:0007829|PDB:6MU0" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:6MU0" FT HELIX 45..58 FT /evidence="ECO:0007829|PDB:6MU0" FT TURN 59..62 FT /evidence="ECO:0007829|PDB:6MU0" FT STRAND 64..72 FT /evidence="ECO:0007829|PDB:6MU0" FT HELIX 73..80 FT /evidence="ECO:0007829|PDB:6MU0" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:6MU0" FT HELIX 93..101 FT /evidence="ECO:0007829|PDB:6MU0" FT STRAND 106..115 FT /evidence="ECO:0007829|PDB:6MU0" FT HELIX 117..129 FT /evidence="ECO:0007829|PDB:6MU0" FT HELIX 136..150 FT /evidence="ECO:0007829|PDB:6MU0" SQ SEQUENCE 152 AA; 16893 MW; 1D5A15E5C14F74DB CRC64; MSFNIFIASD HTGLTLKKII SEHLKTKQFN VVDLGPNYFD ANDDYPDFAF LVADKVKKNS DKDLGILICG TGVGVCMAAN KVKGVLAALV VSEKTAALAR QHDNANVLCL SSRFVTDSEN IKIVDDFLKA NFEGGRHQRR IDKIIRYEKE TE //