ID A0A1H9Q100_9LACT Unreviewed; 147 AA.
AC A0A1H9Q100;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Ribose-5-phosphate isomerase {ECO:0000313|EMBL:SER53735.1};
GN ORFNames=SAMN04488559_101262 {ECO:0000313|EMBL:SER53735.1};
OS Isobaculum melis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Isobaculum.
OX NCBI_TaxID=142588 {ECO:0000313|EMBL:SER53735.1, ECO:0000313|Proteomes:UP000198948};
RN [1] {ECO:0000313|EMBL:SER53735.1, ECO:0000313|Proteomes:UP000198948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13760 {ECO:0000313|EMBL:SER53735.1,
RC ECO:0000313|Proteomes:UP000198948};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOHA01000001; SER53735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9Q100; -.
DR STRING; 142588.SAMN04488559_101262; -.
DR OrthoDB; 1778624at2; -.
DR Proteomes; UP000198948; Unassembled WGS sequence.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProt.
DR GO; GO:0005988; P:lactose metabolic process; IEA:UniProtKB-KW.
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:SER53735.1};
KW Lactose metabolism {ECO:0000256|ARBA:ARBA00022736};
KW Reference proteome {ECO:0000313|Proteomes:UP000198948}.
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 147 AA; 15889 MW; A1F282AA1B008BFB CRC64;
MKLAIGSDHV GIELKPIIID YIQELGHTVE DFGPFSSDRT DYPKYGKKVA EEVASGNFDA
GILICGTGVG ISISANKVKG IRAVVCSEPY SAKLSKEHNN TNILAFGSRV IGSELAKMIV
KEWLDATFEG GRHGTRVEMI SDIETNC
//