RPIA_PYRHO
ID RPIA_PYRHO Reviewed; 229 AA.
AC O50083;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170, ECO:0000269|PubMed:12057201};
DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170};
GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; OrderedLocusNames=PH1375;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-85; ARG-100; GLU-107;
RP LYS-125 AND ASP-168, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=12057201; DOI=10.1016/s0969-2126(02)00779-7;
RA Ishikawa K., Matsui I., Payan F., Cambillau C., Ishida H., Kawarabayasi Y.,
RA Kikuchi H., Roussel A.;
RT "A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus
RT horikoshii characterization and three-dimensional structure.";
RL Structure 10:877-886(2002).
CC -!- FUNCTION: Involved in the first step of the non-oxidative branch of the
CC pentose phosphate pathway. It catalyzes the reversible conversion of
CC ribose-5-phosphate to ribulose 5-phosphate.
CC {ECO:0000269|PubMed:12057201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170,
CC ECO:0000269|PubMed:12057201};
CC -!- ACTIVITY REGULATION: Inhibited by D-4-phosphoerythronic acid.
CC {ECO:0000269|PubMed:12057201}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.17 mM for ribose 5-P {ECO:0000269|PubMed:12057201};
CC pH dependence:
CC Optimum pH is 6 (at 50 degrees Celsius).
CC {ECO:0000269|PubMed:12057201};
CC Temperature dependence:
CC Optimum temperature is over 95 degrees Celsius.
CC {ECO:0000269|PubMed:12057201};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12057201}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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; BA000001; BAA30481.1; -; Genomic_DNA.
DR PIR; A71010; A71010.
DR RefSeq; WP_010885464.1; NC_000961.1.
DR PDB; 1LK5; X-ray; 1.75 A; A/B/C/D=1-229.
DR PDB; 1LK7; X-ray; 2.00 A; A/B/C/D=1-229.
DR PDBsum; 1LK5; -.
DR PDBsum; 1LK7; -.
DR AlphaFoldDB; O50083; -.
DR SMR; O50083; -.
DR IntAct; O50083; 1.
DR MINT; O50083; -.
DR STRING; 70601.3257798; -.
DR EnsemblBacteria; BAA30481; BAA30481; BAA30481.
DR GeneID; 1443702; -.
DR KEGG; pho:PH1375; -.
DR eggNOG; arCOG01122; Archaea.
DR OMA; YDWDEVN; -.
DR OrthoDB; 98657at2157; -.
DR BRENDA; 5.3.1.6; 5244.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; O50083; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IDA:UniProtKB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IDA:UniProtKB.
DR CDD; cd01398; RPI_A; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR PANTHER; PTHR11934; PTHR11934; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase.
FT CHAIN 1..229
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158517"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:12057201"
FT BINDING 28..31
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12057201,
FT ECO:0007744|PDB:1LK7"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12057201,
FT ECO:0007744|PDB:1LK7"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12057201,
FT ECO:0007744|PDB:1LK7"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12057201,
FT ECO:0007744|PDB:1LK7"
FT SITE 85
FT /note="Plays a direct or indirect catalytic role"
FT MUTAGEN 85
FT /note="D->N: Strong decrease in the catalytic efficiency
FT and increase in the binding affinity."
FT /evidence="ECO:0000269|PubMed:12057201"
FT MUTAGEN 100
FT /note="R->A: 2-fold decrease in the catalytic efficiency
FT and strong decrease in the binding affinity."
FT /evidence="ECO:0000269|PubMed:12057201"
FT MUTAGEN 107
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12057201"
FT MUTAGEN 125
FT /note="K->A: 2-fold decrease in the catalytic efficiency
FT and strong decrease in the binding affinity."
FT /evidence="ECO:0000269|PubMed:12057201"
FT MUTAGEN 168
FT /note="D->N: Almost the same catalytic efficiency and
FT binding affinity than wild-type."
FT /evidence="ECO:0000269|PubMed:12057201"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:1LK5"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1LK5"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1LK5"
SQ SEQUENCE 229 AA; 25162 MW; 0E35BCB9F608D93C CRC64;
MNVEEMKKIA AKEALKFIED DMVIGLGTGS TTAYFIKLLG EKLKRGEISD IVGVPTSYQA
KLLAIEHDIP IASLDQVDAI DVAVDGADEV DPNLNLIKGR GAALTMEKII EYRAGTFIVL
VDERKLVDYL CQKMPVPIEV IPQAWKAIIE ELSIFNAKAE LRMGVNKDGP VITDNGNFII
DAKFPRIDDP LDMEIELNTI PGVIENGIFA DIADIVIVGT REGVKKLER
