ID G7WQJ0_METH6 Unreviewed; 307 AA.
AC G7WQJ0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=Mhar_2272 {ECO:0000313|EMBL:AET65624.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65624.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET65624.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET65624.1,
RC ECO:0000313|Proteomes:UP000005877};
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
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; CP003117; AET65624.1; -; Genomic_DNA.
DR RefSeq; WP_014587800.1; NC_017527.1.
DR AlphaFoldDB; G7WQJ0; -.
DR STRING; 1110509.Mhar_2272; -.
DR GeneID; 12511450; -.
DR KEGG; mhi:Mhar_2272; -.
DR PATRIC; fig|1110509.7.peg.2513; -.
DR HOGENOM; CLU_016218_2_1_2; -.
DR OrthoDB; 27639at2157; -.
DR Proteomes; UP000005877; 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:UP000005877}.
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 17..20
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 203..204
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02230"
SQ SEQUENCE 307 AA; 33285 MW; 27C78E4FD28CD63F CRC64;
MDQLLDTAEK IRSMEIRGAA LIGRAAAGAL KEFALAIDPS GIEEFNAQVD MAADILLNTR
PTAVSLSNAI RMVMRYRGDE VESARTSLAK NADGFVERSL MAVERIGEIG SRRVRDGDVI
LTHCNSSVAL SIIKTAFDAG KDVKVIATES RPRYQGHLTV KTLDGWGIET ELVVDSAVRS
VINEVDEVIV GADVVTASGS LVNKIGTAAI ALAAHEARTS FMVAAETYKF SPETLMGELV
PIEERAAEEV YPGISELKHV RVRNPAFDVT PHQYIDVICT EVGAIPPEMS YLVIKEMLGW
EMEGRVP
//
