RPIA_PSEAE
ID RPIA_PSEAE Reviewed; 223 AA.
AC Q9I6G1;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PA0330;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG03719.1; -; Genomic_DNA.
DR PIR; E83603; E83603.
DR RefSeq; NP_249021.1; NC_002516.2.
DR RefSeq; WP_003084386.1; NZ_QZGE01000016.1.
DR PDB; 4X84; X-ray; 1.25 A; A/B/C/D=1-223.
DR PDBsum; 4X84; -.
DR AlphaFoldDB; Q9I6G1; -.
DR SMR; Q9I6G1; -.
DR STRING; 287.DR97_3295; -.
DR PaxDb; Q9I6G1; -.
DR PRIDE; Q9I6G1; -.
DR DNASU; 882171; -.
DR EnsemblBacteria; AAG03719; AAG03719; PA0330.
DR GeneID; 882171; -.
DR KEGG; pae:PA0330; -.
DR PATRIC; fig|208964.12.peg.346; -.
DR PseudoCAP; PA0330; -.
DR HOGENOM; CLU_056590_1_1_6; -.
DR InParanoid; Q9I6G1; -.
DR OMA; YDWDEVN; -.
DR PhylomeDB; Q9I6G1; -.
DR BioCyc; PAER208964:G1FZ6-333-MON; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0006014; P:D-ribose metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
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..223
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158450"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 32..35
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:4X84"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4X84"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:4X84"
SQ SEQUENCE 223 AA; 23721 MW; ED096E8EB6AF5E37 CRC64;
MNQDQLKQAV AQAAVDHILP HLDSKSIVGV GTGSTANFFI DALARHKAEF DGAVASSEAT
AKRLKEHGIP VYELNTVSEL EFYVDGADES NERLELIKGG GAALTREKIV AAVAKTFICI
ADASKLVPIL GQFPLPVEVI PMARSHVARQ LVKLGGDPVY REGVLTDNGN IILDVHNLRI
DSPVELEEKI NAIVGVVTNG LFAARPADLL LLGTADGVKT LKA
