ID A0A0R1VTM7_9LACO Unreviewed; 234 AA.
AC A0A0R1VTM7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=FD16_GL002048 {ECO:0000313|EMBL:KRM09066.1};
OS Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM09066.1, ECO:0000313|Proteomes:UP000051820};
RN [1] {ECO:0000313|EMBL:KRM09066.1, ECO:0000313|Proteomes:UP000051820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM09066.1,
RC ECO:0000313|Proteomes:UP000051820};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM09066.1}.
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DR EMBL; AZGF01000050; KRM09066.1; -; Genomic_DNA.
DR RefSeq; WP_010622493.1; NZ_BACO01000055.1.
DR AlphaFoldDB; A0A0R1VTM7; -.
DR STRING; 1423807.FD16_GL002048; -.
DR PATRIC; fig|1423807.3.peg.2100; -.
DR eggNOG; COG0120; Bacteria.
DR OrthoDB; 5870696at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000051820; Unassembled WGS sequence.
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}.
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 28..31
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 97..100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ SEQUENCE 234 AA; 25213 MW; 9956309ADDBBFDE9 CRC64;
MNQNELKASV GNEAAKYVEN DMIVGLGSGT TVSYMVDSLG KRVKSEGLNI VCISTSNRTA
DQARCLGMNV TSIDKVGHVD LTIDGADEIS SDLNGIKGGG AALLWEKIVA TNSDRNMWIV
DESKIVDHLG AFPLPVEVIP FGSQHVFDKF KKMGFQPSFR TNVASALVKT DSNNLIIDLH
LGKISAPKEL AELLNDTVGV VEHGLFLDVV DKVIVGKQDG IETIDRIEKF ANAN
//