RPIB_MYCLE
ID RPIB_MYCLE Reviewed; 162 AA.
AC Q9CBY1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=ML1484;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583922; CAC30434.1; -; Genomic_DNA.
DR PIR; E87094; E87094.
DR RefSeq; NP_302043.1; NC_002677.1.
DR RefSeq; WP_010908364.1; NC_002677.1.
DR AlphaFoldDB; Q9CBY1; -.
DR SMR; Q9CBY1; -.
DR STRING; 272631.ML1484; -.
DR EnsemblBacteria; CAC30434; CAC30434; CAC30434.
DR KEGG; mle:ML1484; -.
DR PATRIC; fig|272631.5.peg.2781; -.
DR Leproma; ML1484; -.
DR eggNOG; COG0698; Bacteria.
DR HOGENOM; CLU_091396_4_0_11; -.
DR OMA; DYPPFCL; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000000806; 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..162
FT /note="Ribose-5-phosphate isomerase B"
FT /id="PRO_0000251147"
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; 17433 MW; 984E8A2CF74E9D4D CRC64;
MSGMRVYLGA DHAGYELKRQ IIEHLKQSGH QPIDCGAFSY DVDDEYPAFC ITAATRTVAD
PGSLGIVLGG SGNGEQIAAN KVVGARCALA WSVETARLAR EHNNAQLIGI GGRMHTVAEA
LTIVDAFVTT PWSEAQRHQR RIDILAEFER THQAPPVPGA QA
