ID A0A3N6LPI8_9EURY Unreviewed; 326 AA.
AC A0A3N6LPI8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=EA462_05320 {ECO:0000313|EMBL:RQG91393.1};
OS Natrarchaeobius halalkaliphilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobius.
OX NCBI_TaxID=1679091 {ECO:0000313|EMBL:RQG91393.1, ECO:0000313|Proteomes:UP000273828};
RN [1] {ECO:0000313|EMBL:RQG91393.1, ECO:0000313|Proteomes:UP000273828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArcht-Sl {ECO:0000313|EMBL:RQG91393.1,
RC ECO:0000313|Proteomes:UP000273828};
RA Sorokin D.Y., Elcheninov A.G., Kostrikina N.A., Bale N.J.,
RA Sinninghe Damste J.S., Khijniak T.V., Kublanov I.V., Toshchakov S.V.;
RT "Natrarchaeobius chitinivorans gen. nov., sp. nov., and Natrarchaeobius
RT haloalkaliphilus sp. nov., alkaliphilic, chitin-utilizing haloarchaea from
RT hypersaline alkaline lakes.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQG91393.1}.
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DR EMBL; REFY01000002; RQG91393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6LPI8; -.
DR OrthoDB; 27639at2157; -.
DR Proteomes; UP000273828; Unassembled WGS sequence.
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:UP000273828}.
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 25..28
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
SQ SEQUENCE 326 AA; 34972 MW; B86A25A1F4521F57 CRC64;
MGNEAPAVDP VVESTAADIA AMRIRGAAAI ADAAAAALAI QAERSDAVTP GAFRTQLRVA
ARTLYETRPT AVSLPNALRY VLRGTDGDSV DELRSSTIDR AETFREDLED AQTTLGKIGS
NRLRDGDVVM THCHSTDALA CIEAALDDGK RIEAIVTETR PRKQGHITAR ELREWGVPVT
LIVDNAARRY LDDADHVLVG ADSIAADGGV INKIGTSGLA VNARERGVPV MVAAQTIKLH
PGTMTGHTVA IEMRDETEVL TSSERSEITD LEDGDDGFTV ENPAFDVTPP RHVDAIVTEH
GQFPPESVVT LMRELFGETT TEPWET
//
