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Database: UniProt
Entry: S6FPJ8_9CLOT
LinkDB: S6FPJ8_9CLOT
Original site: S6FPJ8_9CLOT 
ID   S6FPJ8_9CLOT            Unreviewed;       149 AA.
AC   S6FPJ8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Putative Ribose 5-phosphate isomerase B {ECO:0000313|EMBL:SLK22243.1};
GN   ORFNames=CCH01_23170 {ECO:0000313|EMBL:SLK22243.1};
OS   Clostridium chauvoei JF4335.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1351755 {ECO:0000313|EMBL:SLK22243.1, ECO:0000313|Proteomes:UP000190476};
RN   [1] {ECO:0000313|Proteomes:UP000190476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Falquet L., Falquet L.;
RL   Submitted (MAR-2017) 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; LT799839; SLK22243.1; -; Genomic_DNA.
DR   RefSeq; WP_021876607.1; NZ_LT799839.1.
DR   AlphaFoldDB; S6FPJ8; -.
DR   STRING; 1351755.CCH01_23170; -.
DR   GeneID; 66302626; -.
DR   OrthoDB; 1778624at2; -.
DR   Proteomes; UP000190476; Chromosome i.
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:SLK22243.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190476}.
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   149 AA;  16100 MW;  475FD40DCAD891AC CRC64;
     MKIALGSDHG GIELKEEIIK YLQSEGYEIK DFGTNTKDSC DYPDYAVPVA EAVVAKEFDF
     GILVCGTGIG IGIAANKVPG VRAALCSDTF SAHATREHNN ANILTLGQRV VGPGLALDIV
     KTFLNTNFEG GRHQLRIDKV SEVEKKYSK
//
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