ID A0A3D8Y2P7_9BACT Unreviewed; 143 AA.
AC A0A3D8Y2P7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Ribose 5-phosphate isomerase B {ECO:0000313|EMBL:REA55693.1};
DE EC=5.3.1.6 {ECO:0000313|EMBL:REA55693.1};
GN Name=rpiB {ECO:0000313|EMBL:REA55693.1};
GN ORFNames=DSL64_27855 {ECO:0000313|EMBL:REA55693.1};
OS Dyadobacter luteus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=2259619 {ECO:0000313|EMBL:REA55693.1, ECO:0000313|Proteomes:UP000256373};
RN [1] {ECO:0000313|EMBL:REA55693.1, ECO:0000313|Proteomes:UP000256373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS19 {ECO:0000313|EMBL:REA55693.1,
RC ECO:0000313|Proteomes:UP000256373};
RA Chen L.;
RT "Dyadobacter roseus sp. nov., isolated from rose rhizosphere soil.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC {ECO:0000256|ARBA:ARBA00008754}.
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:REA55693.1}.
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DR EMBL; QNUL01000045; REA55693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8Y2P7; -.
DR OrthoDB; 1778624at2; -.
DR Proteomes; UP000256373; Unassembled WGS sequence.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
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 Isomerase {ECO:0000313|EMBL:REA55693.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000256373}.
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT BINDING 9..10
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 67..71
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 100
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 110
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 133
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 137
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ SEQUENCE 143 AA; 15547 MW; 3980A69089F14032 CRC64;
MRKIAIGSDH AGFPYKEPVI NWLTANGFEV KDFGTYSEES ADYADFAHPV ASGVESGEFE
KGVLLCGSGQ GVCITANKHQ GIRAALVWDL PLAPLARQHN DANVICLPVR FIELETALAS
IQAFLNTEFE GGRHQTRVNK IAC
//
