R15PI_PYRHO
ID R15PI_PYRHO Reviewed; 324 AA.
AC O57947;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=PH0208;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29277.1; -; Genomic_DNA.
DR PIR; F71243; F71243.
DR PDB; 5YFJ; X-ray; 2.20 A; A/B/C=1-324.
DR PDB; 5YFS; X-ray; 2.30 A; A/B/C=1-324.
DR PDB; 5YFT; X-ray; 2.21 A; A/B/C=1-324.
DR PDB; 5YFU; X-ray; 2.35 A; A/B/C=1-324.
DR PDB; 5YFV; X-ray; 2.75 A; A/B/C=1-324.
DR PDB; 5YFW; X-ray; 2.35 A; A/B/C=1-324.
DR PDB; 5YFX; X-ray; 2.70 A; A=1-324.
DR PDB; 5YG5; X-ray; 2.75 A; A/B/C=1-324.
DR PDB; 5YG6; X-ray; 2.35 A; A/B/C=1-324.
DR PDB; 5YG7; X-ray; 2.50 A; A/B/C=1-324.
DR PDB; 5YG8; X-ray; 2.80 A; A/B/C=1-324.
DR PDB; 5YG9; X-ray; 2.80 A; A/B/C=1-324.
DR PDB; 5YGA; X-ray; 2.45 A; A/B/C=1-324.
DR PDBsum; 5YFJ; -.
DR PDBsum; 5YFS; -.
DR PDBsum; 5YFT; -.
DR PDBsum; 5YFU; -.
DR PDBsum; 5YFV; -.
DR PDBsum; 5YFW; -.
DR PDBsum; 5YFX; -.
DR PDBsum; 5YG5; -.
DR PDBsum; 5YG6; -.
DR PDBsum; 5YG7; -.
DR PDBsum; 5YG8; -.
DR PDBsum; 5YG9; -.
DR PDBsum; 5YGA; -.
DR AlphaFoldDB; O57947; -.
DR SMR; O57947; -.
DR STRING; 70601.3256594; -.
DR EnsemblBacteria; BAA29277; BAA29277; BAA29277.
DR KEGG; pho:PH0208; -.
DR eggNOG; arCOG01124; Archaea.
DR OMA; GDVIMTH; -.
DR BRENDA; 5.3.1.29; 5244.
DR Proteomes; UP000000752; 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 3D-structure; Carbohydrate metabolism; Isomerase.
FT CHAIN 1..324
FT /note="Ribose 1,5-bisphosphate isomerase"
FT /id="PRO_0000156106"
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"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 24..41
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 92..122
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5YFJ"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5YFJ"
FT TURN 189..195
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:5YFJ"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:5YFJ"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:5YFJ"
SQ SEQUENCE 324 AA; 36406 MW; A78FCC28ACD5D2AB CRC64;
MGAMIVKEVY ETAEKIKSME IRGAGRIARA AAQALMIQAE KSKAKEPEEL WNELKVASKI
LYNTRPTAVS LPNALRYVMH RVKAAYLGGA DLETLRFTAI NSAKEFIYNS EKAIERIGEI
GAKRIEDGDI IMTHCHSKAA ISVMKKAFEQ GKNIKVIVTE TRPKWQGKIT AKELASYGIP
VIYIVDSAAR HYMKMTDKVV MGADSITANG AVINKIGTSL IALTAKEHRV WVMIAAETYK
FHPATMLGQL VEIEMRDPTE VIPEEELRTW PKNIEVWNPA FDVTPPEYID VIITERGIIP
PYAAIDILKE EFGWALKYKE PWED
