ID A0A077DDU6_9BURK Unreviewed; 232 AA.
AC A0A077DDU6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE EC=5.3.1.6 {ECO:0000256|HAMAP-Rule:MF_00170};
DE AltName: Full=Phosphoriboisomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE Short=PRI {ECO:0000256|HAMAP-Rule:MF_00170};
GN Name=rpiA {ECO:0000256|HAMAP-Rule:MF_00170};
GN ORFNames=IX83_05180 {ECO:0000313|EMBL:AIL32784.1};
OS Basilea psittacipulmonis DSM 24701.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Basilea.
OX NCBI_TaxID=1072685 {ECO:0000313|EMBL:AIL32784.1, ECO:0000313|Proteomes:UP000028945};
RN [1] {ECO:0000313|EMBL:AIL32784.1, ECO:0000313|Proteomes:UP000028945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24701 {ECO:0000313|EMBL:AIL32784.1,
RC ECO:0000313|Proteomes:UP000028945};
RX PubMed=24581117; DOI=10.1186/1471-2164-15-169;
RA Whiteson K.L., Hernandez D., Lazarevic V., Gaia N., Farinelli L.,
RA Francois P., Pilo P., Frey J., Schrenzel J.;
RT "A genomic perspective on a new bacterial genus and species from the
RT Alcaligenaceae family, Basilea psittacipulmonis.";
RL BMC Genomics 15:169-169(2014).
CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC ribulose 5-phosphate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00170}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00170}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000256|HAMAP-Rule:MF_00170}.
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DR EMBL; CP009238; AIL32784.1; -; Genomic_DNA.
DR RefSeq; WP_038499868.1; NZ_CP009238.1.
DR AlphaFoldDB; A0A077DDU6; -.
DR STRING; 1072685.IX83_05180; -.
DR KEGG; bpsi:IX83_05180; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_4; -.
DR OrthoDB; 5870696at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000028945; 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 Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.1360; -; 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 NCBIfam; TIGR00021; rpiA; 1.
DR PANTHER; PTHR11934; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11934:SF0; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF75445; D-ribose-5-phosphate isomerase (RpiA), lid domain; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00170};
KW Reference proteome {ECO:0000313|Proteomes:UP000028945}.
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 33..36
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 99..102
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ SEQUENCE 232 AA; 24997 MW; 455251C7D06DF2EC CRC64;
MLTQDQLKQA VAKQALSHIR QHLIQDAIIG IGTGSTADFF IDALAEHRHA FRGAVASSER
SAKRLAMHGI RVFDLNEVDE LAVYVDGADE INAKLEMIKG GGGALTREKI VASASHHFVC
IVDESKVVDN LGAFPLPIEV LAISKEVVSR QLYQLGATEV IERKDFLTDN GHPILDVKGL
KIEDAARLEA QINDIPGVVT CGLFAIRPAT VALVGTQEGV KIIGQTADPR YA
//
