ID   RPIB_MYCPN              Reviewed;         152 AA.
AC   P53527;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=MPN_595;
GN   ORFNames=MP247;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8604303; DOI=10.1093/nar/24.4.628;
RA   Hilbert H., Himmelreich R., Plagens H., Herrmann R.;
RT   "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma
RT   pneumoniae comprising the dnaA region, the atp operon and a cluster of
RT   ribosomal protein genes.";
RL   Nucleic Acids Res. 24:628-639(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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}.
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DR   EMBL; U43738; AAC43662.1; -; Genomic_DNA.
DR   EMBL; U00089; AAB95895.1; -; Genomic_DNA.
DR   PIR; S62852; S62852.
DR   RefSeq; NP_110284.1; NC_000912.1.
DR   RefSeq; WP_010874952.1; NC_000912.1.
DR   AlphaFoldDB; P53527; -.
DR   SMR; P53527; -.
DR   IntAct; P53527; 2.
DR   STRING; 272634.MPN_595; -.
DR   PRIDE; P53527; -.
DR   EnsemblBacteria; AAB95895; AAB95895; MPN_595.
DR   GeneID; 66608720; -.
DR   KEGG; mpn:MPN_595; -.
DR   PATRIC; fig|272634.6.peg.658; -.
DR   HOGENOM; CLU_091396_4_1_14; -.
DR   OMA; DYPPFCL; -.
DR   BioCyc; MPNE272634:G1GJ3-969-MON; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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_0000208166"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P37351"
FT   ACT_SITE        103
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         12..13
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         71..75
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         104
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         114
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         137
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         141
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
SQ   SEQUENCE   152 AA;  16699 MW;  0A7244F0C1ABE363 CRC64;
     MQMNHPIYIA SDHTGLELKS LVIKHLEQQK LQVIDLGPTE LDPLDDYPDY AFLLAQTMQA
     NPNSLGILIC GTGVGVCMAA NKAKGILAAL VVDSKTAALA RQHDDANVLC LSSRFVVPEE
     NIKIVDEFLQ AQFEGGRHSK RVGKIIAYER EK