ID A0A1Y6BJ70_9PROT Unreviewed; 419 AA.
AC A0A1Y6BJ70;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05428998_103147 {ECO:0000313|EMBL:SMF03579.1};
OS Tistlia consotensis USBA 355.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Fodinicurvataceae; Tistlia.
OX NCBI_TaxID=560819 {ECO:0000313|EMBL:SMF03579.1, ECO:0000313|Proteomes:UP000192917};
RN [1] {ECO:0000313|EMBL:SMF03579.1, ECO:0000313|Proteomes:UP000192917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 355 {ECO:0000313|EMBL:SMF03579.1,
RC ECO:0000313|Proteomes:UP000192917};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC EC=2.7.1.12; Evidence={ECO:0000256|ARBA:ARBA00001329};
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 acid metabolism. {ECO:0000256|ARBA:ARBA00004761}.
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 gluconokinase GntK/GntV family.
CC {ECO:0000256|ARBA:ARBA00008420}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000256|HAMAP-Rule:MF_00170}.
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DR EMBL; FWZX01000003; SMF03579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6BJ70; -.
DR STRING; 560819.SAMN05428998_103147; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000192917; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02021; GntK; 1.
DR CDD; cd01398; RPI_A; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.1360; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR InterPro; IPR006001; Therm_gnt_kin.
DR NCBIfam; TIGR00021; rpiA; 1.
DR NCBIfam; TIGR01313; therm_gnt_kin; 1.
DR PANTHER; PTHR43748; RIBOSE-5-PHOSPHATE ISOMERASE 3, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR43748:SF3; RIBOSE-5-PHOSPHATE ISOMERASE 3, CHLOROPLASTIC-RELATED; 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.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00170};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000192917};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 37..40
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 106..109
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ SEQUENCE 419 AA; 44372 MW; 74A6C633200D565F CRC64;
MSASGTPADA GRNAVKRAAA EAAVELVENG MVVGLGTGST AAFALEALAR RHRQGLRFLG
IPTSERTAAA ARAAGLPLTT FAEHRQIDLT IDGADEVERG TLNLIKGLGG ALLREKIVAA
ASHRLAIVAD AGKLADRLGT LAPVPVEVVG FGLEATRASL EALGASTRLR KAPDGEPFAT
DGGNRILDCS FGPLSDPARL ERRIRHVVGV VECGLFISRA DPVIVADQAG VHRLDSPRAH
RGSPPILLVM GLSGAGKSTV ALELRARLGW PFEEGDALHP EANIAKMHAG IPLTDADREP
WLARVAAWID ARRAARQPGI ITCSALKRSY RQVVVGSRPE VRLVYLRGGR DLIAEHLMGR
RGHFMPPTLM QSQIETLEEP DPDEDPLTVD VGSPARDVAD TIIRRLAAAS PAGWRATPV
//
