ID A0A0P6WNK1_9BACI Unreviewed; 225 AA.
AC A0A0P6WNK1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AM506_20145 {ECO:0000313|EMBL:KPL57813.1};
OS Rossellomorea vietnamensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL57813.1, ECO:0000313|Proteomes:UP000050398};
RN [1] {ECO:0000313|EMBL:KPL57813.1, ECO:0000313|Proteomes:UP000050398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL57813.1,
RC ECO:0000313|Proteomes:UP000050398};
RA Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.;
RT "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5.";
RL Submitted (AUG-2015) 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:KPL57813.1}.
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DR EMBL; LIXZ01000026; KPL57813.1; -; Genomic_DNA.
DR RefSeq; WP_060674751.1; NZ_LIXZ01000026.1.
DR AlphaFoldDB; A0A0P6WNK1; -.
DR PATRIC; fig|218284.4.peg.2576; -.
DR eggNOG; COG0120; Bacteria.
DR OrthoDB; 5870696at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000050398; 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; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00170};
KW Reference proteome {ECO:0000313|Proteomes:UP000050398}.
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 24..27
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 79..82
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 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ SEQUENCE 225 AA; 24581 MW; 6FC7C2EBC3602A8D CRC64;
MEKKLAGEKA TEYIKDGMTI GLGTGSTVYW TIQKLGELVS QGLQIKAIPS SVDTERLAKK
AGIPLTTFAE VDMLDLSIDG ADEVDAMYNL IKGGGGALVR EKFIDTFTRK FIIVVDESKL
VSRLGSFPLP VEVIPFGWEV TCQSLAELGC TPVLRKRNDE RFISDNGNYI VDCHFTGIDD
PASLHSRLKQ LLGVVETGLF IDLTTLMIVG KRDGVEVVSP KKNLT
//