ID   RPIB_MYCTO              Reviewed;         162 AA.
AC   P9WKD6; L0TCF4; Q79FD7; Q7D737;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
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}; OrderedLocusNames=MT2540;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46840.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46840.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003899332.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKD6; -.
DR   SMR; P9WKD6; -.
DR   EnsemblBacteria; AAK46840; AAK46840; MT2540.
DR   KEGG; mtc:MT2540; -.
DR   PATRIC; fig|83331.31.peg.2741; -.
DR   HOGENOM; CLU_091396_4_0_11; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..162
FT                   /note="Ribose-5-phosphate isomerase B"
FT                   /id="PRO_0000427672"
FT   ACT_SITE        75
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT   BINDING         11..12
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         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   162 AA;  17278 MW;  31EF834F28783E00 CRC64;
     MSGMRVYLGA DHAGYELKQR IIEHLKQTGH EPIDCGALRY DADDDYPAFC IAAATRTVAD
     PGSLGIVLGG SGNGEQIAAN KVPGARCALA WSVQTAALAR EHNNAQLIGI GGRMHTVAEA
     LAIVDAFVTT PWSKAQRHQR RIDILAEYER THEAPPVPGA PA