RPIA_THET2
ID RPIA_THET2 Reviewed; 227 AA.
AC Q72J47;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
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=TT_C0932;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM,
RP AND SUBUNIT.
RX PubMed=13679361; DOI=10.1074/jbc.m309272200;
RA Hamada K., Ago H., Sugahara M., Nodake Y., Kuramitsu S., Miyano M.;
RT "Oxyanion hole-stabilized stereospecific isomerization in ribose-5-
RT phosphate isomerase (Rpi).";
RL J. Biol. Chem. 278:49183-49190(2003).
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. Can also act on D-ribose-5-
CC diphosphate and D-ribose-5-triphosphate as substrate.
CC {ECO:0000269|PubMed:13679361}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.63 mM for ribose-5-phosphate (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:13679361};
CC Note=kcat is 1072 sec(-1) for ribose-5-phosphate.;
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: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170,
CC ECO:0000269|PubMed:13679361}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR EMBL; AE017221; AAS81276.1; -; Genomic_DNA.
DR RefSeq; WP_011173356.1; NC_005835.1.
DR PDB; 1UJ4; X-ray; 1.80 A; A=1-227.
DR PDB; 1UJ5; X-ray; 2.00 A; A=1-227.
DR PDB; 1UJ6; X-ray; 1.74 A; A=1-227.
DR PDBsum; 1UJ4; -.
DR PDBsum; 1UJ5; -.
DR PDBsum; 1UJ6; -.
DR AlphaFoldDB; Q72J47; -.
DR SMR; Q72J47; -.
DR STRING; 262724.TT_C0932; -.
DR EnsemblBacteria; AAS81276; AAS81276; TT_C0932.
DR KEGG; tth:TT_C0932; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_0_0; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1681738at2; -.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; Q72J47; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
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 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..227
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158486"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170,
FT ECO:0000269|PubMed:13679361"
FT BINDING 30..33
FT /ligand="substrate"
FT BINDING 86..89
FT /ligand="substrate"
FT BINDING 99..104
FT /ligand="substrate"
FT BINDING 126
FT /ligand="substrate"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1UJ6"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1UJ6"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1UJ6"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1UJ6"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:1UJ6"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1UJ6"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:1UJ6"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1UJ6"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1UJ6"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1UJ6"
SQ SEQUENCE 227 AA; 24039 MW; 47CD743AEAC126C7 CRC64;
MERPLESYKK EAAHAAIAYV QDGMVVGLGT GSTARYAVLE LARRLREGEL KGVVGVPTSR
ATEELAKREG IPLVDLPPEG VDLAIDGADE IAPGLALIKG MGGALLREKI VERAAKEFIV
IADHTKKVPV LGRGPVPVEI VPFGYRATLK AIADLGGEPE LRMDGDEFYF TDGGHLIADC
RFGPIGDPLG LHRALLEIPG VVETGLFVGM ATRALVAGPF GVEELLP
