ID N0BID8_9EURY Unreviewed; 313 AA.
AC N0BID8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Ribose 1,5-bisphosphate isomerase {ECO:0000256|HAMAP-Rule:MF_02230};
DE Short=R15P isomerase {ECO:0000256|HAMAP-Rule:MF_02230};
DE Short=R15Pi {ECO:0000256|HAMAP-Rule:MF_02230};
DE EC=5.3.1.29 {ECO:0000256|HAMAP-Rule:MF_02230};
DE AltName: Full=Ribulose 1,5-bisphosphate synthase {ECO:0000256|HAMAP-Rule:MF_02230};
DE Short=RuBP synthase {ECO:0000256|HAMAP-Rule:MF_02230};
GN ORFNames=Asulf_00197 {ECO:0000313|EMBL:AGK60231.1};
OS Archaeoglobus sulfaticallidus PM70-1.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK60231.1, ECO:0000313|Proteomes:UP000013307};
RN [1] {ECO:0000313|EMBL:AGK60231.1, ECO:0000313|Proteomes:UP000013307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM70-1 {ECO:0000313|EMBL:AGK60231.1};
RX PubMed=23833130;
RA Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT "Complete Genome Sequence of the Thermophilic and Facultatively
RT Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus Strain
RT PM70-1T.";
RL Genome Announc. 1:e00406-13(2013).
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:0000256|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:0000256|HAMAP-Rule:MF_02230};
CC -!- MISCELLANEOUS: Reaction proceeds via a cis-phosphoenolate intermediate.
CC {ECO:0000256|HAMAP-Rule:MF_02230}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC R15P isomerase subfamily. {ECO:0000256|ARBA:ARBA00009229,
CC ECO:0000256|HAMAP-Rule:MF_02230}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02230}.
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DR EMBL; CP005290; AGK60231.1; -; Genomic_DNA.
DR RefSeq; WP_015589830.1; NC_021169.1.
DR AlphaFoldDB; N0BID8; -.
DR STRING; 387631.Asulf_00197; -.
DR GeneID; 15391843; -.
DR KEGG; ast:Asulf_00197; -.
DR eggNOG; arCOG01124; Archaea.
DR HOGENOM; CLU_016218_2_1_2; -.
DR OrthoDB; 27639at2157; -.
DR Proteomes; UP000013307; 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; translation initiation factor eif-2b, domain 1; 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; R15Pi.
DR NCBIfam; TIGR00524; eIF-2B_rel; 1.
DR NCBIfam; TIGR00511; ribulose_e2b2; 1.
DR PANTHER; PTHR43475; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR43475:SF2; RIBOSE 1,5-BISPHOSPHATE ISOMERASE; 1.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02230};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02230};
KW Reference proteome {ECO:0000313|Proteomes:UP000013307}.
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 19..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 201..202
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
SQ SEQUENCE 313 AA; 35245 MW; DBBCCFA0369FB4AC CRC64;
MSIDYVVKSA EKIKNMEVRG AGRIAKFCAK VLMEYAMEIK KNFDEEMKKA AEILLNTRPT
AVSLYNSIYY VMDYSGESDE EKRESLVKRA KEFIEWVDTA QKEIGRIGSR RIKSGSTILT
HCNSASALSV IKEAYRKGKD IEVFATESRP RYQGHLTAKE LSAEGIPVTL IVDSAVRYFI
REIDYVIVGA DAITVNGSLV NKIGTSQIAL IAKEARVPFM VAAETYKFSP KTLLGESIVI
EERDPAEVAP EELRSLVKIR NPAFDITPRH YIDLIITEIG AIPPEMAYLV IKERLGYRLL
GEDELKLSVH HYD
//
