R15PI_HALVD
ID R15PI_HALVD Reviewed; 323 AA.
AC D4GV73;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=HVO_0966;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP SAMPYLATION AT LYS-210, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20054389; DOI=10.1038/nature08659;
RA Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., Zhou G.,
RA Chen S., Wells L., Maupin-Furlow J.A.;
RT "Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax
RT volcanii.";
RL Nature 463:54-60(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001956; ADE03061.1; -; Genomic_DNA.
DR RefSeq; WP_004043979.1; NZ_AOHU01000094.1.
DR AlphaFoldDB; D4GV73; -.
DR SMR; D4GV73; -.
DR STRING; 309800.C498_13946; -.
DR EnsemblBacteria; ADE03061; ADE03061; HVO_0966.
DR GeneID; 8925565; -.
DR KEGG; hvo:HVO_0966; -.
DR eggNOG; arCOG01124; Archaea.
DR HOGENOM; CLU_016218_2_1_2; -.
DR OMA; GDVIMTH; -.
DR OrthoDB; 36100at2157; -.
DR Proteomes; UP000008243; 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Isomerase; Isopeptide bond; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..323
FT /note="Ribose 1,5-bisphosphate isomerase"
FT /id="PRO_0000397103"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT ACT_SITE 199
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 209..210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02230"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SAMP2)"
FT /evidence="ECO:0000269|PubMed:20054389"
SQ SEQUENCE 323 AA; 34876 MW; 27BA4853C01818A9 CRC64;
MDDRVHPEVR RTATEIDTME IRGAATIADA AARALRTQAT ESDAADAEAF RAELRATART
LHETRPTAVS LPNALRYVLR DMSSTTVEGL RQSVVDSADE FCARLERAQA DLGQVGANRL
RDGDTIMTHC HSTDALACVE AAVEQGKHIE AVVKETRPRN QGHITAKRLH ELGVPVTLIV
DSAARRYLND VDHVLVGADA VAADGSVINK IGTSGLAVNA RERGTPIMVA AQTLKLHPGT
MTGHTVDIEM RDTAEVVDDD TLADLGNPTV KNPAFDVTPP RYVDAIVTER GQFPPESIVI
LMRELFGEGT SEPWAEPSPR AEP
