ID   DRDI_CLOBK              Reviewed;         349 AA.
AC   B1IJF0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=5-deoxyribose 1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_02229};
DE            EC=5.3.1.- {ECO:0000255|HAMAP-Rule:MF_02229};
GN   Name=drdI {ECO:0000255|HAMAP-Rule:MF_02229}; OrderedLocusNames=CLD_3299;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1-
CC       phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose
CC       salvage pathway that recycles this toxic radical SAM enzyme by-product
CC       to mainstream metabolites. {ECO:0000255|HAMAP-Rule:MF_02229}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-deoxy-alpha-D-ribose 1-phosphate = 5-deoxy-D-ribulose 1-
CC         phosphate; Xref=Rhea:RHEA:61296, ChEBI:CHEBI:58749,
CC         ChEBI:CHEBI:144504; Evidence={ECO:0000255|HAMAP-Rule:MF_02229};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61297;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02229};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02229}.
CC   -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC       DrdI subfamily. {ECO:0000255|HAMAP-Rule:MF_02229}.
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DR   EMBL; CP000939; ACA44223.1; -; Genomic_DNA.
DR   RefSeq; WP_015957599.1; NC_010516.1.
DR   AlphaFoldDB; B1IJF0; -.
DR   SMR; B1IJF0; -.
DR   EnsemblBacteria; ACA44223; ACA44223; CLD_3299.
DR   KEGG; cbb:CLD_3299; -.
DR   HOGENOM; CLU_016218_1_2_9; -.
DR   OMA; RLWVDET; -.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:InterPro.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.420; -; 1.
DR   Gene3D; 3.40.50.10470; -; 1.
DR   HAMAP; MF_02229; Deoxyribose1P_isomerase; 1.
DR   HAMAP; MF_01678; Salvage_MtnA; 1.
DR   InterPro; IPR043679; Deoxyribose1P_isomerase_DrdI.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR005251; IF-M1Pi.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   InterPro; IPR027363; M1Pi_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase.
FT   CHAIN           1..349
FT                   /note="5-deoxyribose 1-phosphate isomerase"
FT                   /id="PRO_0000357166"
FT   ACT_SITE        240
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         49..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         250..251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   SITE            160
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
SQ   SEQUENCE   349 AA;  38702 MW;  1AEEF4BC0C718A59 CRC64;
     MAELLAIKWD DNRDKLILLD QTILPNKIEY IEYDTAEGVY DSIKDMIVRG APAIGVTAAY
     GLYFAAKVAP EDNFENFFKY LKEKSSYLDS SRPTAVNLSW ALKVMESKAL ENKDKDVKEI
     KSILREEAKR IHEEDIEICK TIGENLITLL KDGMGILTHC NAGQLATSKY GTATSPMYLA
     KEKGWNFKVY SDETRPRLQG STLTALELYE AGIDVTTITD NMAAMVMSQG KIDAVIVGCD
     RVAANGDTAN KIGTMGVSIL AKYFGIPMYI AAPTPSIDIN TKTGEDIPIE ERNPEEVTSR
     FGAWTAPKGV KVYNPGFDVT PHENITAIVT EKGIVYPPFK ENLKKLFEK