ID   RPIA_RUEPO              Reviewed;         262 AA.
AC   Q5LTT5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=SPO1327;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV94616.1; -; Genomic_DNA.
DR   RefSeq; WP_011047066.1; NC_003911.12.
DR   AlphaFoldDB; Q5LTT5; -.
DR   SMR; Q5LTT5; -.
DR   STRING; 246200.SPO1327; -.
DR   EnsemblBacteria; AAV94616; AAV94616; SPO1327.
DR   KEGG; sil:SPO1327; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_0_5; -.
DR   OMA; FIDICDT; -.
DR   OrthoDB; 1681738at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001023; Chromosome.
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; Reference proteome.
FT   CHAIN           1..262
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_0000158462"
FT   ACT_SITE        111
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         33..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         89..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         102..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   262 AA;  28300 MW;  394E6348C4096BCB CRC64;
     MTGELSPIDK AKFVAAKRAA DLVEDGMRVG LGTGSTAAWL VRCLGDMVRK EGLKMRGVPT
     STRTAQLARE VGIEVITLDE ARWLDITIDG ADEFDGDLNL IKGGGGALLQ EKIVATASDQ
     MVVIADLGKE VSRLGAFPLP VEVIPFGWQT TQALLEETLI SMDVLGRTAT LRMNGDTPFV
     TDEGNHILDL HLQRIGNARQ LALVLNQIPG VVENGLFIDI CDTVVVGHGD GRVEIRDINQ
     GTVEHDRLDF VESDNLFTDL AD