ID A0A0G3WID2_9BACT Unreviewed; 153 AA.
AC A0A0G3WID2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Ribose 5-phosphate epimerase {ECO:0000313|EMBL:AKL97627.1};
GN Name=rpiB {ECO:0000313|EMBL:AKL97627.1};
GN ORFNames=Epro_0248 {ECO:0000313|EMBL:AKL97627.1};
OS Endomicrobium proavitum.
OC Bacteria; Elusimicrobiota; Endomicrobiia; Endomicrobiales;
OC Endomicrobiaceae; Endomicrobium.
OX NCBI_TaxID=1408281 {ECO:0000313|EMBL:AKL97627.1, ECO:0000313|Proteomes:UP000035337};
RN [1] {ECO:0000313|EMBL:AKL97627.1, ECO:0000313|Proteomes:UP000035337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rsa215 {ECO:0000313|EMBL:AKL97627.1,
RC ECO:0000313|Proteomes:UP000035337};
RA Zheng H.;
RT "Complete genome sequence of Endomicrobium proavitum.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC {ECO:0000256|ARBA:ARBA00008754}.
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DR EMBL; CP009498; AKL97627.1; -; Genomic_DNA.
DR RefSeq; WP_052569846.1; NZ_CP009498.1.
DR AlphaFoldDB; A0A0G3WID2; -.
DR STRING; 1408281.Epro_0248; -.
DR KEGG; epo:Epro_0248; -.
DR PATRIC; fig|1408281.3.peg.257; -.
DR OrthoDB; 1778624at2; -.
DR Proteomes; UP000035337; Chromosome.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR InterPro; IPR004785; RpiB.
DR InterPro; IPR003500; RpiB_LacA_LacB.
DR InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR NCBIfam; TIGR01120; rpiB; 1.
DR NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1.
DR PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1.
DR Pfam; PF02502; LacAB_rpiB; 1.
DR PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035337}.
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT BINDING 12..13
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 70..74
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 103
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 113
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 135
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 139
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ SEQUENCE 153 AA; 16643 MW; 8C364C959F9AFA32 CRC64;
MAEIKKLAFG TDHAAAAVRN TVREYLLSLG YEVEDFGYDG EGSCDYPDFA VKVAQSVRDK
KADKGVLICG TGIGMSIAAN KVKGVIAAPC WDEDTAKLAA QHNGADILCL GSRTATVNEI
CSRIKTFLST EFEPRHAKRI EKIKEIENKQ CSK
//
