RPIA_STRMK
ID RPIA_STRMK Reviewed; 215 AA.
AC B2FT30;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Smlt3868;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR EMBL; AM743169; CAQ47272.1; -; Genomic_DNA.
DR RefSeq; WP_005410902.1; NC_010943.1.
DR PDB; 7LDA; X-ray; 1.45 A; A/B=1-215.
DR PDBsum; 7LDA; -.
DR AlphaFoldDB; B2FT30; -.
DR SMR; B2FT30; -.
DR STRING; 522373.Smlt3868; -.
DR EnsemblBacteria; CAQ47272; CAQ47272; Smlt3868.
DR KEGG; sml:Smlt3868; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_6; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1681738at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000008840; 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..215
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_1000097697"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 26..29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 79..82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:7LDA"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:7LDA"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:7LDA"
SQ SEQUENCE 215 AA; 23275 MW; 1674036640EF6414 CRC64;
MSEAKRLAAE KAIEYVEDGM IVGVGTGSTV AYFIDALARI QHRIKGAVSS SEQSTARLKQ
HGIEVIELNH SGNLSLYVDG ADECDANKCL IKGGGAALTR EKIIAEASER FICIIDPSKQ
VPVLGRFPLP VEVIPMARSL VARQIRDMTG GQPTWREGVV TDNGNQILDI HNLQITDPEK
LERELNQLPG VVCVGLFARR RADVVIVGGE PPVVL
