RPIA_FRATT
ID RPIA_FRATT Reviewed; 224 AA.
AC Q5NFM5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=FTT_1208;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Orlikowska M., Rostankowski R., Nakka C., Hattne J., Grimshaw S., Borek D.,
RA Otwinowski Z.;
RT "Crystal structure of ribose-5-isomerase A.";
RL Submitted (DEC-2009) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Rostankowski R., Orlikowska M., Nakka C., Grimshaw S., Borek D.,
RA Otwinowski Z.;
RT "Structural and biophysical studies of Ribose-5-Phosphate Isomerase A from
RT Francisella tularensis.";
RL Submitted (JAN-2013) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.
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 -!- 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 and homotetramer. {ECO:0000255|HAMAP-Rule:MF_00170,
CC ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR EMBL; AJ749949; CAG45841.1; -; Genomic_DNA.
DR RefSeq; WP_003015241.1; NZ_CP010290.1.
DR RefSeq; YP_170167.1; NC_006570.2.
DR PDB; 3KWM; X-ray; 2.32 A; A/B/C/D=1-224.
DR PDB; 4IO1; X-ray; 1.65 A; A/B=1-224.
DR PDBsum; 3KWM; -.
DR PDBsum; 4IO1; -.
DR AlphaFoldDB; Q5NFM5; -.
DR SMR; Q5NFM5; -.
DR STRING; 177416.FTT_1208; -.
DR DNASU; 3192024; -.
DR EnsemblBacteria; CAG45841; CAG45841; FTT_1208.
DR KEGG; ftu:FTT_1208; -.
DR eggNOG; COG0120; Bacteria.
DR OMA; YDWDEVN; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000001174; 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 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; Reference proteome.
FT CHAIN 1..224
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158419"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 34..37
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 100..103
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:4IO1"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3KWM"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:4IO1"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:4IO1"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4IO1"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:4IO1"
SQ SEQUENCE 224 AA; 24466 MW; 46ACC58D7487CC2B CRC64;
MFFNKKNNQD ELKKLAATEA AKSITTEITL GVGTGSTVGF LIEELVNYRD KIKTVVSSSE
DSTRKLKALG FDVVDLNYAG EIDLYIDGAD ECNNHKELIK GGGAALTREK ICVAAAKKFI
CIIDESKKVN TLGNFPLPIE VIPMARSYIA RQIVKLGGQP VYREQTITDN GNVILDVYNL
KIDNPLKLET ELNQITGVVT NGIFALKPAD TVIMATKDSN IVVL
