RPIA_LEGPH
ID RPIA_LEGPH Reviewed; 216 AA.
AC Q5ZZB7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=lpg0094;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU26201.1; -; Genomic_DNA.
DR RefSeq; WP_010945855.1; NC_002942.5.
DR RefSeq; YP_094148.1; NC_002942.5.
DR PDB; 6EEP; X-ray; 1.85 A; A/B=1-216.
DR PDB; 6MC0; X-ray; 2.00 A; A/B=1-216.
DR PDBsum; 6EEP; -.
DR PDBsum; 6MC0; -.
DR AlphaFoldDB; Q5ZZB7; -.
DR SMR; Q5ZZB7; -.
DR STRING; 272624.lpg0094; -.
DR PaxDb; Q5ZZB7; -.
DR PRIDE; Q5ZZB7; -.
DR EnsemblBacteria; AAU26201; AAU26201; lpg0094.
DR GeneID; 66489300; -.
DR KEGG; lpn:lpg0094; -.
DR PATRIC; fig|272624.6.peg.100; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_6; -.
DR OMA; YDWDEVN; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000000609; 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..216
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158430"
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 1..13
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6EEP"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:6EEP"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:6EEP"
SQ SEQUENCE 216 AA; 23022 MW; 07BE7A675CAA5824 CRC64;
MSELKIKAAK AAIAYIEDDM VIGVGTGSTV NFFIKELAAI KHKIEACVAS SKATEALLRA
EGIPVIDLNS VQDLPIYVDG ADEVNERGEM IKGGGGALTR EKIVANVATQ FICIVDESKV
VKRLGEFPVA VEVIPMARSF VARQIVKLGG DPEYREGFVT DNGNIILDVF NLSFSTPMAL
EDSLNVIPGV VENGVFAKRL ADKVLVASAS GVNNLK
