ID   R15PI_METJA             Reviewed;         308 AA.
AC   Q57586;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ribose 1,5-bisphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_02230};
DE            Short=R15P isomerase {ECO:0000255|HAMAP-Rule:MF_02230};
DE            Short=R15Pi {ECO:0000255|HAMAP-Rule:MF_02230};
DE            EC=5.3.1.29 {ECO:0000255|HAMAP-Rule:MF_02230};
DE   AltName: Full=Ribulose 1,5-bisphosphate synthase {ECO:0000255|HAMAP-Rule:MF_02230};
DE            Short=RuBP synthase {ECO:0000255|HAMAP-Rule:MF_02230};
GN   OrderedLocusNames=MJ0122;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P)
CC       to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate
CC       for RubisCO. Functions in an archaeal AMP degradation pathway, together
CC       with AMP phosphorylase and RubisCO. {ECO:0000255|HAMAP-Rule:MF_02230}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate;
CC         Xref=Rhea:RHEA:32243, ChEBI:CHEBI:57870, ChEBI:CHEBI:68688;
CC         EC=5.3.1.29; Evidence={ECO:0000255|HAMAP-Rule:MF_02230};
CC   -!- MISCELLANEOUS: Reaction proceeds via a cis-phosphoenolate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_02230}.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       R15P isomerase subfamily. {ECO:0000255|HAMAP-Rule:MF_02230,
CC       ECO:0000305}.
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DR   EMBL; L77117; AAB98103.1; -; Genomic_DNA.
DR   PIR; B64315; B64315.
DR   AlphaFoldDB; Q57586; -.
DR   SMR; Q57586; -.
DR   STRING; 243232.MJ_0122; -.
DR   EnsemblBacteria; AAB98103; AAB98103; MJ_0122.
DR   KEGG; mja:MJ_0122; -.
DR   eggNOG; arCOG01124; Archaea.
DR   HOGENOM; CLU_016218_2_1_2; -.
DR   InParanoid; Q57586; -.
DR   OMA; GDVIMTH; -.
DR   PhylomeDB; Q57586; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0043917; F:ribose 1,5-bisphosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.420; -; 1.
DR   Gene3D; 3.40.50.10470; -; 1.
DR   HAMAP; MF_02230; R15P_isomerase; 1.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   InterPro; IPR027363; M1Pi_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR005250; Ribulose_e2b2.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00511; ribulose_e2b2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..308
FT                   /note="Ribose 1,5-bisphosphate isomerase"
FT                   /id="PRO_0000156103"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT   BINDING         24..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT   BINDING         208..209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
SQ   SEQUENCE   308 AA;  34518 MW;  EC2BAE3E061E4FCE CRC64;
     MVFKMSEMDI IKETYEKIKN MEIRGAGRIG RAAAKALKEY ALKISHLNEE EFKNKMREAG
     NILISARPTA VSLPNVVKYV LKGLNEENPK ERVIERADEF INSSLKAIEN IGKFGANRIK
     DGDTILTHCN SEAAISVIKT AYDEGKDIKV FCTETRPRNQ GYLTAKTLYD YGIDVTLIVD
     SAVRYFIKEI DIVVVGADAI TANGCLVNKI GTSQIALIAN ESRVPFLTAA ETYKFHPKTI
     VGELIEIEER SPEEVAVFED KYKGIKIRNP AFDVTPAKYI DAIITEVGLI PPQGAWYIIE
     KYFGWLEK