RPIB_LISIN
ID RPIB_LISIN Reviewed; 148 AA.
AC Q92EU5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ribose-5-P isomerase B {ECO:0000303|PubMed:22773791};
DE EC=5.3.1.6 {ECO:0000269|PubMed:22773791};
DE AltName: Full=RpiB-type ribose-5-P isomerase {ECO:0000303|PubMed:22773791};
GN Name=rpiB {ECO:0000303|PubMed:22773791};
GN OrderedLocusNames=lin0363 {ECO:0000312|EMBL:CAC95596.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND PATHWAY.
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=22773791; DOI=10.1128/jb.00801-12;
RA Monniot C., Zebre A.C., Ake F.M., Deutscher J., Milohanic E.;
RT "Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent
RT dihydroxyacetone kinase system connected to the pentose phosphate
RT pathway.";
RL J. Bacteriol. 194:4972-4982(2012).
CC -!- FUNCTION: Catalyzes the interconversion of ribulose-5-P and ribose-5-P.
CC {ECO:0000269|PubMed:22773791}.
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:0000269|PubMed:22773791};
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:0000305|PubMed:22773791}.
CC -!- INDUCTION: Repressed by GolR. {ECO:0000269|PubMed:22773791}.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
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DR EMBL; AL596164; CAC95596.1; -; Genomic_DNA.
DR PIR; AD1478; AD1478.
DR RefSeq; WP_003724276.1; NC_003212.1.
DR AlphaFoldDB; Q92EU5; -.
DR SMR; Q92EU5; -.
DR STRING; 272626.lin0363; -.
DR EnsemblBacteria; CAC95596; CAC95596; CAC95596.
DR GeneID; 61169370; -.
DR KEGG; lin:lin0363; -.
DR eggNOG; COG0698; Bacteria.
DR HOGENOM; CLU_091396_4_1_9; -.
DR OMA; VTAHDVY; -.
DR OrthoDB; 1346802at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Isomerase.
FT CHAIN 1..148
FT /note="Ribose-5-P isomerase B"
FT /id="PRO_0000439509"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P37351"
FT BINDING 8..9
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 66..70
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 99
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 132
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"
SQ SEQUENCE 148 AA; 16383 MW; 7DBA4F4F670398D8 CRC64;
MKIAIGCDEM GYELKQTLIT RLKEKNIEFT DFGSFENEKV LYPSIAEKVA LEVKNNDYDR
GILICGTGIG MAITANKIHG IRAAQIHDSY SAERARKSND AHIMTMGALV IGPSLAVSLL
DTWLDSDFSG GRSQAKVDLM EEIDQKNR
