ID A0A0M4FTK8_9BACI Unreviewed; 148 AA.
AC A0A0M4FTK8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Ribose 5-phosphate isomerase {ECO:0000313|EMBL:ALC88699.1};
GN ORFNames=AM500_01955 {ECO:0000313|EMBL:ALC88699.1};
OS Bacillus sp. FJAT-18017.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC88699.1, ECO:0000313|Proteomes:UP000060713};
RN [1] {ECO:0000313|EMBL:ALC88699.1, ECO:0000313|Proteomes:UP000060713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC88699.1,
RC ECO:0000313|Proteomes:UP000060713};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) 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; CP012602; ALC88699.1; -; Genomic_DNA.
DR RefSeq; WP_053597695.1; NZ_CP012602.1.
DR AlphaFoldDB; A0A0M4FTK8; -.
DR STRING; 1705566.AM500_01955; -.
DR PATRIC; fig|1705566.3.peg.387; -.
DR Proteomes; UP000060713; 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; 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:ALC88699.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000060713}.
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; 16102 MW; B1A3CC3229A6DB36 CRC64;
MKVALASDHG GVNIRKEIAS LLEELNIEYK DFGCECSTSV DYPDYALPVA EKVASGEFDR
GILICGTGIG MSIAANKVKG IRCALVHDTF SAKATREHND TNMLAMGERV IGPGLARDIA
QIWLTTEFTG GRHANRVGKI TEYEKKNQ
//
