ID   DRDI_CLOBM              Reviewed;         349 AA.
AC   B1KZY3;
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=CLK_0708;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
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; CP000962; ACA57104.1; -; Genomic_DNA.
DR   RefSeq; WP_012344890.1; NC_010520.1.
DR   AlphaFoldDB; B1KZY3; -.
DR   SMR; B1KZY3; -.
DR   EnsemblBacteria; ACA57104; ACA57104; CLK_0708.
DR   KEGG; cbl:CLK_0708; -.
DR   HOGENOM; CLU_016218_1_2_9; -.
DR   OMA; RLWVDET; -.
DR   Proteomes; UP000000722; 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_0000357165"
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;  38752 MW;  23CE3868324E6AED CRC64;
     MAELLAIKWD DNRDKLILLD QTILPNKIEY IEYDTAEDVY DSIKDMIVRG APAIGVTAAY
     GLYFAAKVAP EDNFKNFFKY LKEKSAYLDS SRPTAVNLSW ALKIMESKAL ENKDKDVKEI
     KSILREEAKR IHEEDIEICK AIGENLVTLL KDGVGILTHC NAGQLATSKY GTATSPMYLA
     KEKGWNFKVY SDETRPRLQG STLTALELYE AGIDVTTITD NMAAMVMSQG KIDAVIVGCD
     RIAANGDTAN KIGTMGVSIL AKYFGIPMYI AAPTPSIDID TKTGKDIPIE ERNPEEVTSR
     FGVWTAPRGV KVYNPGFDVT PHENITAIVT EKGIVYPPFE ENLKKLFEK