ID D2RDV0_ARCPA Unreviewed; 314 AA.
AC D2RDV0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=Arcpr_1242 {ECO:0000313|EMBL:ADB58294.1};
OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB58294.1, ECO:0000313|Proteomes:UP000001901};
RN [1] {ECO:0000313|EMBL:ADB58294.1, ECO:0000313|Proteomes:UP000001901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18
RC {ECO:0000313|Proteomes:UP000001901};
RX PubMed=21304717;
RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL Stand. Genomic Sci. 2:327-346(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: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; CP001857; ADB58294.1; -; Genomic_DNA.
DR RefSeq; WP_012940630.1; NC_013741.1.
DR AlphaFoldDB; D2RDV0; -.
DR STRING; 572546.Arcpr_1242; -.
DR PaxDb; 572546-Arcpr_1242; -.
DR GeneID; 8739927; -.
DR KEGG; apo:Arcpr_1242; -.
DR eggNOG; arCOG01124; Archaea.
DR HOGENOM; CLU_016218_2_1_2; -.
DR OrthoDB; 27639at2157; -.
DR Proteomes; UP000001901; Chromosome.
DR GO; GO:0043917; F:ribose 1,5-bisphosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 Initiation factor {ECO:0000313|EMBL:ADB58294.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02230};
KW Protein biosynthesis {ECO:0000313|EMBL:ADB58294.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001901}.
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 202..203
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
SQ SEQUENCE 314 AA; 35218 MW; BF1ECA9C7D5AF4E1 CRC64;
MPNFKLVEES AKKIINMEVR GASRIARFAA ETLKEFAKTV EKDFDENMRK ASEILMNTRP
TAVSLFNAIN YVMMYKGEND EEKKADAIRR AEEFIRWVDT AKQKIGEIGA KRIKDGWTIL
THCNSSTALM VIKTAFRQGK NIEVIATESR PRYQGHLTVK ELAGEGIPTT LIVDSAVRYF
MKDVDCVIVG ADTITVNGAL INKIGTSQIA LCARESRVPF MVCAETYKFS PATLFGELVV
IEERDAREVA PEEILNLGVK VRNPAFDVTP REYIDLIVTE IGAIPPEMAY VIIRERLGYG
LEMGELKVSA KHFD
//
