R15PI_ARCFU
ID R15PI_ARCFU Reviewed; 313 AA.
AC O28242;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=AF_2037;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB89217.1; -; Genomic_DNA.
DR PIR; D69504; D69504.
DR RefSeq; WP_010879529.1; NC_000917.1.
DR AlphaFoldDB; O28242; -.
DR SMR; O28242; -.
DR STRING; 224325.AF_2037; -.
DR DNASU; 1485263; -.
DR EnsemblBacteria; AAB89217; AAB89217; AF_2037.
DR GeneID; 1485263; -.
DR KEGG; afu:AF_2037; -.
DR eggNOG; arCOG01124; Archaea.
DR HOGENOM; CLU_016218_2_1_2; -.
DR OMA; GDVIMTH; -.
DR OrthoDB; 36100at2157; -.
DR PhylomeDB; O28242; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0043917; F:ribose 1,5-bisphosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:InterPro.
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..313
FT /note="Ribose 1,5-bisphosphate isomerase"
FT /id="PRO_0000156102"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 17..20
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
SQ SEQUENCE 313 AA; 35144 MW; B054D0189EEED729 CRC64;
MEEVLEAAEK IRSMEVRGAA RIARFAAETL MKFAEKASDE KFDEEMRFAA ETLLNTRPTA
VSLYNAINYV MRYSGESVEE KRQSVIRRAR EFINWVETAQ RKIGEIGEKR IKDGYTVMTH
CNSSAALSVI KKAHENGKRV EVIATESRPR WQGHLTVKQL REAGIEVTLI VDSAVRYFIN
EVDCVVVGAD TITANGALIN KIGTSQIALA AKEARVPFMV AAETYKFSPK TLFGELVVIE
ERDAREVAPE EILKLGVKVR NPAFDVTPRD YIDVIITEIG AIPPEMAYIV ITERLGYAGI
EEEEITLNSR HFD
