ID A0A0C4WP49_9GAMM Unreviewed; 226 AA.
AC A0A0C4WP49;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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-2 {ECO:0000313|EMBL:AJE19887.1};
GN Synonyms=rpiA {ECO:0000256|HAMAP-Rule:MF_00170};
GN ORFNames=Achr_3810 {ECO:0000313|EMBL:AJE19887.1};
OS Azotobacter chroococcum NCIMB 8003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE19887.1, ECO:0000313|Proteomes:UP000068210};
RN [1] {ECO:0000313|EMBL:AJE19887.1, ECO:0000313|Proteomes:UP000068210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE19887.1,
RC ECO:0000313|Proteomes:UP000068210};
RX PubMed=26061173;
RA Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT (ATCC 4412).";
RL PLoS ONE 10:E0127997-E0127997(2015).
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; CP010415; AJE19887.1; -; Genomic_DNA.
DR RefSeq; WP_039801335.1; NZ_CP010415.1.
DR AlphaFoldDB; A0A0C4WP49; -.
DR STRING; 1328314.Achr_3810; -.
DR KEGG; acx:Achr_3810; -.
DR HOGENOM; CLU_056590_1_1_6; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000068210; 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:UP000068210}.
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 32..35
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ SEQUENCE 226 AA; 24443 MW; C1B5E27B73A4A35C CRC64;
MTQDQLKQAV AQAALDHILP QLTSKSVVGV GTGSTANFFI DLLARHRLDF DGAVASSEAT
AARLKGHGIE VYDLNNVADL EFYVDGADEC NKHLELIKGG GAALTREKIV AAVAQTFICI
ADESKRVDFL GDFPLPVEVI PMARSHVARQ LVWLGGDPVY REGVVTDNGN VILDVYNMQI
TNPRQLESDI NNIVGVVTNG LFAARPADLL LLGTRNGVER IERPKP
//
