ID   RPIB_MYCPA              Reviewed;         159 AA.
AC   Q73XM4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=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}; Synonyms=rpi;
GN   OrderedLocusNames=MAP_2285c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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   -!- MISCELLANEOUS: In mycobacterial enzymes, the usual proton acceptor is
CC       not a cysteine, but is remplaced by a glutamate.
CC       {ECO:0000250|UniProtKB:P9WKD7}.
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
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DR   EMBL; AE016958; AAS04602.1; -; Genomic_DNA.
DR   RefSeq; WP_003875844.1; NC_002944.2.
DR   AlphaFoldDB; Q73XM4; -.
DR   SMR; Q73XM4; -.
DR   STRING; 262316.MAP_2285c; -.
DR   EnsemblBacteria; AAS04602; AAS04602; MAP_2285c.
DR   KEGG; mpa:MAP_2285c; -.
DR   eggNOG; COG0698; Bacteria.
DR   HOGENOM; CLU_091396_4_0_11; -.
DR   OMA; DYPPFCL; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000000580; 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; IPR011860; Rib-5-P_Isoase_Actino.
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; TIGR02133; RPI_actino; 1.
DR   TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..159
FT                   /note="Ribose-5-phosphate isomerase B"
FT                   /id="PRO_0000251149"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         8..9
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         67..71
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         100
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         110
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         134
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         138
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
SQ   SEQUENCE   159 AA;  16939 MW;  159BBB97275006E0 CRC64;
     MRVYLGSDHA GFELKQQIIA HLEQSGHQPI DCGAFSYDAD DDYPAFCIAA ATRTVADPDS
     LGIVLGGSGN GEQIAANKVP GARCALAWSV ETAQLAREHN NAQLIGIGGR MHTVAEALAI
     VDAFVTTPWS KAPRHQRRID ILAEYERTHQ APPVPGAVG