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RPIA_STRP4
ID   RPIA_STRP4              Reviewed;         227 AA.
AC   B5E3K1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE            EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE   AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE            Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170};
GN   Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; OrderedLocusNames=SPG_0749;
OS   Streptococcus pneumoniae serotype 19F (strain G54).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=512566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RX   PubMed=11442348; DOI=10.1089/10766290152044995;
RA   Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA   Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA   Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT   "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT   clinical isolate.";
RL   Microb. Drug Resist. 7:99-125(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RA   Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA   Tettelin H., Oggioni M.;
RT   "Pneumococcal beta glucoside metabolism investigated by whole genome
RT   comparison.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC       ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.
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:0000255|HAMAP-Rule:MF_00170};
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:0000255|HAMAP-Rule:MF_00170}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR   EMBL; CP001015; ACF55342.1; -; Genomic_DNA.
DR   RefSeq; WP_000429299.1; NC_011072.1.
DR   AlphaFoldDB; B5E3K1; -.
DR   SMR; B5E3K1; -.
DR   GeneID; 60234174; -.
DR   KEGG; spx:SPG_0749; -.
DR   HOGENOM; CLU_056590_1_0_9; -.
DR   OMA; YDWDEVN; -.
DR   UniPathway; UPA00115; UER00412.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
DR   CDD; cd01398; RPI_A; 1.
DR   HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR   InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00021; rpiA; 1.
PE   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..227
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_1000097698"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         26..29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         82..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         95..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   227 AA;  24792 MW;  E08B6341DF2D7412 CRC64;
     MENLKKMAGI KAAEFVSDGM VVGLGTGSTA YYFVEEIGRR IKEEGLQITA VTTSSVTTKQ
     AEGLNIPLKS IDQVDFVDVT VDGADEVDSQ FNGIKGGGGA LLMEKVVATP SKEYIWVVDE
     SKLVEKLGAF KLPVEVVQYG AEQVFRHFER AGYKPSFREK DGQRFVTDMQ NFIIDLALDV
     IENPIAFGQE LDHVVGVVEH GLFNQMVDKV IVAGRDGVQI STSKKGK
 
 
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