R15PI_PYRAB
ID R15PI_PYRAB Reviewed; 324 AA.
AC Q9V281; G8ZG28;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=PYRAB01930; ORFNames=PAB2402;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB49117.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69569.1; -; Genomic_DNA.
DR PIR; F75208; F75208.
DR AlphaFoldDB; Q9V281; -.
DR SMR; Q9V281; -.
DR STRING; 272844.PAB2402; -.
DR EnsemblBacteria; CAB49117; CAB49117; PAB2402.
DR KEGG; pab:PAB2402; -.
DR PATRIC; fig|272844.11.peg.207; -.
DR eggNOG; arCOG01124; Archaea.
DR HOGENOM; CLU_016218_2_1_2; -.
DR OMA; GDVIMTH; -.
DR PhylomeDB; Q9V281; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..324
FT /note="Ribose 1,5-bisphosphate isomerase"
FT /id="PRO_0000156104"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 22..25
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 137..139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
SQ SEQUENCE 324 AA; 36418 MW; D4483ACE4234A6EA CRC64;
MGAMIVREVY EIAEKIKSME IRGAGKIARS VAQALMIQAE KSTAKSPEEL WTELKEAAKI
LYKTRPTAVS LPNALRYVMH RAKIAYSSGA DLETLRFTVI NSAKEFIHNS EKAIERIGEI
GAKRIEDGDV IMTHCHSKAA ISVMKTAFDQ GKDIKVIVTE TRPRWQGKIT AKELASYGIP
VIYVVDSAAR HYMKMTDKVV MGADSITANG AVINKIGTSL IALTAKEHRV WVMIAAETYK
FHPETMLGQL VEIEMRDPTE VIPEEELKTW PKNIEVWNPA FDVTPPEYID VIITEKGIIP
PYAAIDILKE EFGWALKYRE PWED
