ID A0A1Y4NQ33_9FIRM Unreviewed; 148 AA.
AC A0A1Y4NQ33;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Ribose 5-phosphate isomerase B {ECO:0000313|EMBL:OUP82600.1};
GN ORFNames=B5F07_13740 {ECO:0000313|EMBL:OUP82600.1};
OS Lachnoclostridium sp. An169.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965569 {ECO:0000313|EMBL:OUP82600.1, ECO:0000313|Proteomes:UP000195962};
RN [1] {ECO:0000313|Proteomes:UP000195962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An169 {ECO:0000313|Proteomes:UP000195962};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP82600.1}.
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DR EMBL; NFKT01000019; OUP82600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4NQ33; -.
DR OrthoDB; 1778624at2; -.
DR Proteomes; UP000195962; Unassembled WGS sequence.
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; PTHR43732:SF1; RIBOSE 5-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR43732; RIBOSE 5-PHOSPHATE ISOMERASE-RELATED; 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:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OUP82600.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195962}.
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT BINDING 8..9
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 66..70
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 99
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 109
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 132
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 136
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ SEQUENCE 148 AA; 15981 MW; 476BA084C83D09DD CRC64;
MKIGIGNDHS ALELKAEIIE HLKEKGHEVV DFGTNSPESC DYPVYGEAVA RAVVSGEVEQ
GILICGTGLG ISLAANKVKG IRAAVCSEPF TAKMARAHNN CNILAFGARV VGAELAKMIV
DTWLETEFEG GRHQRRVDMI MAIEDKED
//
