RPIA_CHLAA
ID RPIA_CHLAA Reviewed; 239 AA.
AC A9WIA0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Caur_3198;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY36392.1; -; Genomic_DNA.
DR RefSeq; WP_012259045.1; NC_010175.1.
DR RefSeq; YP_001636781.1; NC_010175.1.
DR AlphaFoldDB; A9WIA0; -.
DR SMR; A9WIA0; -.
DR STRING; 324602.Caur_3198; -.
DR EnsemblBacteria; ABY36392; ABY36392; Caur_3198.
DR KEGG; cau:Caur_3198; -.
DR PATRIC; fig|324602.8.peg.3610; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_0; -.
DR InParanoid; A9WIA0; -.
DR OMA; YDWDEVN; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000002008; 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 3: Inferred from homology;
KW Isomerase; Reference proteome.
FT CHAIN 1..239
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_1000194697"
FT ACT_SITE 110
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 31..34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 101..104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ SEQUENCE 239 AA; 24996 MW; 8A50CABD0A4FCE34 CRC64;
MNTTSTETRK AMAAAAAVAL VRPGMVIGLG FGSTAAYATR MIAERLHQGD LNDIVGVPCA
EGTAQLAREL GIPLTTLDEV AAVDLTIDGA DEVDPQLSLI KGGGGALLRE KMVAQASRRV
AIIVDDSKLS PALGTRFALP LEVVDFGWRA TARWLEAQGG TVQLRLRADG QPFRTDQGNL
ILDWKCGPLN DPAALAAQLS ARAGIVEHGL FIGLATDLFV AGPDGVQHVT TSDCGTIAW