ID A0A0H0YN76_LACCA Unreviewed; 229 AA.
AC A0A0H0YN76;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ECO:0000313|EMBL:KAB1969490.1};
GN ORFNames=AAW28_09285 {ECO:0000313|EMBL:KLI75677.1}, F9B82_08055
GN {ECO:0000313|EMBL:KAB1969490.1};
OS Lacticaseibacillus casei (Lactobacillus casei).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1582 {ECO:0000313|EMBL:KLI75677.1, ECO:0000313|Proteomes:UP000035289};
RN [1] {ECO:0000313|EMBL:KLI75677.1, ECO:0000313|Proteomes:UP000035289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N87 {ECO:0000313|EMBL:KLI75677.1,
RC ECO:0000313|Proteomes:UP000035289};
RA Zotta T., Bassi D., Parente E., Ricciardi A., Ianniello R.G., Reale A.;
RT "Genetic and physiological basis of aerobic metabolism in Lactobacillus
RT rhamnosus and Lactobacillus paracasei: basic and applied aspects.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAB1969490.1, ECO:0000313|Proteomes:UP000477706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIO5773 {ECO:0000313|EMBL:KAB1969490.1,
RC ECO:0000313|Proteomes:UP000477706};
RA Jaomanjaka F., Blanc P.;
RT "Investigation of probiotic properties of different lactic acid bacteria.";
RL Submitted (SEP-2019) 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=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:KLI75677.1}.
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DR EMBL; WBOC01000004; KAB1969490.1; -; Genomic_DNA.
DR EMBL; LCUN01000013; KLI75677.1; -; Genomic_DNA.
DR RefSeq; WP_010490710.1; NZ_WBOC01000004.1.
DR PATRIC; fig|1582.46.peg.739; -.
DR OrthoDB; 5870696at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000035289; Unassembled WGS sequence.
DR Proteomes; UP000477706; 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 229 AA; 25167 MW; 46B19E2018F313B4 CRC64;
MDQNKLKQEA AQKAAEFVED GMTIGLGTGS TVYYLVEAIA QRVKEEHLNL TGVATSVRTR
KQAESLGIPM KDLDEVAQID LTIDGADEVD KHFQGIKGGG RAHLIEKIVA INSARNIWIV
DETKLVDTLG KFPLPLEVIP FGSGKLLQRL KDEGLKPAYR LNDDGTKALT DSKNYIIDLH
LGRIEHPHLL AEWLNKQVGV VEHGLFLDLV KTVVVGTTHG PEILDAHRG
//
